Faculty Profile

Vibha TandonVibha Tandon
Professor & Chairperson
Phone No. 011-26738825, 011-26741640
E-mail: vtandon@mail.jnu.ac.in; vibhadelhi6@gmail.com
Personal webpage: http://www.jnu.ac.in/Faculty/vtandon/cv.pdf


Prof. Vibha Tandon received her Ph.D. from Department of Chemistry, University of Allahabad and postdoc from the Department of Chemistry, Indian Institute of Technology, Kanpur. Prof. Vibha Tandon served as a faculty in the University of Delhi from 1998 to early 2014; and joined SCMM in 2014 as a full time Professor.

Research Interest

Chemical Biology, Radiation Biology & Cell Signalling, Drug Development and Study of their Mechanism of Action based on Genomics & Proteomics, Development of Antibiotics for Gyrase Resistant Strains targeting Topoisomerase IA Gene in Bacteria.

Selected publications:

1. Bansal S, Bajaj P, Pandey S, Tandon V. (2016) Topoisomerases: Resistance vs sensitivity, how far can we go? Med Res Rev. doi: 10.1002/med.21417.

2. Chaudhari TY, Urvashi, Ginotra SK, Yadav P, Kumar G, Tandon V. (2016) Regioselective synthesis of functionalized dihydroisoquinolines from o-alkynyl-arylaldimines via the Reformatsky reaction. Org Biomol Chem. 14: 9896-9906.

3. Alam R, Wahi D, Singh R, Sinha D, Tandon V, Grover A, Rahisuddin. (2016) Design, synthesis, cytotoxicity, HuTopoII a inhibitory activity and molecular docking studies of pyrazole derivatives as potential anticancer agents. Bioorg Chem. 69: 77-90.

4. Singla P, Luxami V, Singh R, Tandon V, Paul K. (2016) Novel pyrazolo[3,4-d]pyrimidine with 4-(1H-benzimidazol-2-yl)-phenylamine as broad spectrum anticancer agents: Synthesis, cell based assay, topoisomerase inhibition, DNA intercalation and bovine serum albumin studies. Eur J Med Chem. 126: 24-35.

5. Kamran MZ, Ranjan A, Kaur N, Sur S, Tandon V. (2016) Radioprotective Agents: Strategies and Translational Advances. Med Res Rev. doi: 10.1002/med.21386. [Epub ahead of print].

6. Tandon V, Urvashi, Yadav P, Sur S, Abbat S, Tiwari V, Hewer R, Papathanasopoulos MA, Raja R, Banerjea AC, Verma AK, Kukreti S, Bharatam PV. (2015) Design, Synthesis, and Biological Evaluation of 1,2-Dihydroisoquinolines as HIV-1 Integrase Inhibitors. ACS Med Chem Lett. 6: 1065-70.

7. Urvashi, Rastogi GK, Ginotra SK, Agarwal A, Tandon V. (2015) An expedient approach to 1,2-dihydroisoquinoline derivatives via cobalt catalysed 6-endo dig cyclization followed by Mannich condensation of o-alkynylarylaldimines. Org Biomol Chem. 13: 1000-7.

8. Mishra RC, Gundala SR, Karna P, Lopus M, Gupta KK, Nagaraju M, Hamelberg D, Tandon V, Panda D, Reid MD, Aneja R. (2015) Design, synthesis and biological evaluation of di-substituted noscapine analogs as potent and microtubule-targeted anticancer agents. Bioorg Med Chem Lett. 25: 2133-40.

9. Nimesh H, Tiwari V, Yang C, Gundala SR, Chuttani K, Hazari PP, Mishra AK, Sharma A, Lal J, Katyal A, Aneja R, Tandon V. (2015) Preclinical Evaluation of DMA, a Bisbenzimidazole, as Radioprotector: Toxicity, Pharmacokinetics, and Biodistribution Studies in Balb/c Mice. Mol Pharmacol. 88: 768-78.

10. Nimesh H, Sur S, Sinha D, Yadav P, Anand P, Bajaj P, Virdi JS, Tandon V. (2014) Synthesis and biological evaluation of novel bisbenzimidazoles as Escherichia coli topoisomerase IA inhibitors and potential antibacterial agents. J Med Chem. 57: 5238-57.

11. Henary M, Narayana L, Ahad S, Gundala SR, Mukkavilli R, Sharma V, Owens EA, Yadav Y, Nagaraju M, Hamelberg D, Tandon V, Panda D, Aneja R. (2015) Novel third-generation water-soluble noscapine analogs as superior microtubule-interfering agents with enhanced antiproliferative activity. Biochem Pharmacol. 92: 192-205.

International Collaboration/Consultancy:

1. International Collaborative Project: Indo South Africa INT/SAFR/P(2/2011)-03/10-2011) Design Synthesis and Evaluation of 1,2 –dihydroisoquinolines as HIV Integrase Inhibitors.

2. Project Title : International collaborative Project: Indo German Project; Validation and Testing of DNA binding ligands as Radiomodulator in Human Cells.

3. International Collaboration with Prof. Yuk-Ching Tse Dinh, Department of Biochemistry & Chemistry, Florida International University, Miami Research Project. We are alongwith her laboratory working on the basic logic that each pathogen has at least one type IA topoisomerase providing a target for discovery of new antibiotics to combat multi –drug resistant infections, including MDR and XDR-TB.

4. International Collaboration with Prof. Ritu Aneja, Georgia State University, Atlanta, USA. We are currently collaborating with her laboratory to explore phytochemicals and Noscapinoids a gentler tubulin binding drugs and investigating these molecules using biochemical, molecular, and cellular biological techniques with in vivo, in vitro, and in silico systems.


CGauranga Mukhopadhyay
Phone No. 011-26738735, 011-26704559
E-mail: gm2300@mail.jnu.ac.in; garunga@hotmail.com
Personal webpage: http://www.jnu.ac.in/Faculty/gm

Professor Mukhopadhyay received his PhD from Jadavpur University (Indian Institute of Chemical Biology), Calcutta and did his postdoctoral study in the laboratory of Biochemistry, National Cancer Institute, NIH, USA.

Research Interests

Major focus of his laboratory is on the study of Type IV Secretion System (Cag-T4SS) of human gastric pathogen Helicobacter pylori.

The laboratory is also studying regulation of gene expression in pathogenic fungus as collaborative project.

Helicobacter pylori Cag-Type IV Secretion System:
Helicobacter pylori are the major cause of chronic gastritis and play an important role in the pathogenesis of peptic ulcer, gastric adeno carcinoma and gastric lymphoma. Although half of the world's population carries the highly diverse bacteria Helicobacter pylori, the clinical sequel develop in only a fraction of colonized individuals and most likely depend on differentially represented bacterial determinants and host characteristics.

Type IV secretion systems (TFSS) play an important role for the virulence of a number of pathogenic bacteria including H. pylori. TFSS are ancestrally related to the bacterial conjugation system and are thought to be versatile transporters of proteins and/or nucleic acids (effectors molecules) across the bacterial membrane to the extra cellular space or into eukaryotic target cells. Basic aims of this work are to understand the biogenesis and adaptation of TFSS to pathogen-host interactions using variety of biochemical, cell biological and molecular biological methods. In the long run the study may help to identify new target(s) for anti bacterial treatments and use of the system as transporter of foreign molecule(s).

Selected publications:

1. Gopal GJ, Pal J, Kumar A, Mukhopadhyay G. (2015) C-terminal domain of CagX is responsible for its interaction with CagT protein of Helicobacter pylori type IV secretion system. Biochem Biophys Res Commun. 456: 98-103.

2. Kumari S, Saradhi M, Rana M, Chatterjee S, Aumercier M, Mukhopadhyay G, Tyagi RK. (2015) Pregnane and Xenobiotic Receptor gene expression in liver cells is modulated by Ets-1 in synchrony with transcription factors Pax5, LEF-1 and c-Jun. Exp Cell Res. 330: 398-411.

3. Dhamgaye S, Devaux F, Vandeputte P, Khandelwal NK, Sanglard D, Mukhopadhyay G, Prasad R. (2014) Molecular mechanisms of action of herbal antifungal alkaloid berberine, in Candida albicans. PLoS One. 9(8): e104554. doi: 10.1371/journal.pone.0104554.

4. Kumar N, Shariq M, Kumari R, Tyagi RK, Mukhopadhyay G. (2013) Cag type IV secretion system: CagI independent bacterial surface localization of CagA. PLoS One. 8(9): e74620. doi: 10.1371/journal.pone.0074620.

5. Kumari S, Mukhopadhyay G, Tyagi RK. (2012) Transcriptional regulation of mouse PXR gene: an interplay of transregulatory factors. PLoS One. 7(8): e44126. doi: 10.1371/journal.pone.0044126.

6. Shukla S, Yadav V, Mukhopadhyay G, Prasad R. (2011) Ncb2 is involved in activated transcription of CDR1 in azole-resistant clinical isolates of Candida albicans. Eukaryot Cell. 10(10): 1357-66.


CChinmay K. Mukhopadhyay
Phone No. 011-2673-8738
E-mail: mukhopc@yahoo.com; ckm2300@mail.jnu.ac.in
Personal webpage: http://www.jnu.ac.in/Faculty/ckm


Prof. Mukhopadhyay did his doctoral studies in Biochemistry in the Department of Biochemistry from Calcutta University under the supervision of Prof. I. B. Chatterjee and received the postdoctoral training under the mentorship of Dr. Paul Fox in the Department of Cell Biology, Cleveland Clinic Foundation, USA. He joined the centre in the year 2001.

Research Interests

Prof. Mukhopadhyay's research interest is to understand the role of iron in metabolic disorders like insulin resistance related pathogenesis, Neurodegenerative disorders like Parkinson and Alzheimer diseases. His research interest also includes role of iron in host-pathogen (primarily leishmania donovani) interaction, drug resistance and inflammation.

Selected Publications:

1. Dev S, Kumari S, Singh N, Bal SK, Seth P, Mukhopadhyay CK. (2015) Role of extracellular hydrogen peroxide on regulation of iron homeostasis genes in neuronal cell: Implication in iron accumulation. Free Radical Biol Med. 86: 78-89.

2. Mandal SM, Chakraborty A, Hossain M, Mahata D, Porto WF, Chakraborty R, Mukhopadhyay CK, Franco OL, Hazra TK, Basak A. (2015) Amphotericin B and anidulafungin directly interact with DNA and induce oxidative damage in the mammalian genome. Mol Biosyst. 11: 2551-2559.

3. Tapryal N, Vivek VG, Mukhopadhyay CK. (2015) Catecholamine stress hormones regulate cellular iron homeostasis by a posttranscriptional mechanism mediated by iron regulatory protein: Implication in energy homeostasis. J. Biol. Chem. 290: 7634-7646.

4. Biswas S, Tapryal N, Mukherjee R, Kumar R, Mukhopadhyay CK. (2013) Insulin promotes iron uptake in human hepatic cell by regulating transferrin receptor-1 transcription mediated by hypoxia inducible factor-1. Biochim Biophys Acta. 1832: 293-301.

5. Tapryal N, Mukhopadhyay C, Das D, Fox PL, Mukhopadhyay C.K. (2009) Reactive oxygen species regulate ceruloplasmin by a novel mRNA decay mechanism involving its 3'-untranslated region: Implications in neurodegenerative diseases. J. Biol. Chem. 284: 1873-1883.

6. Das NK, Biswas S, Solanki S, Mukhopadhyay CK. (2009) Leishmania donovani depletes labile iron pool to exploit iron uptake capacity of macrophage for its intracellular growth. Cell Microbiol. 11: 83-94.

7. Biswas S, Gupta MK, Chattopadhyay D, Mukhopadhyay CK (2007) Insulin induced activation of hypoxia inducible factor-1 requires generation of reactive oxygen species by NADPH oxidase. Am J Physiol Heart and Circulatory Physiology. 292: 758-766.

8. Das D, Tapryal N, Goswami SK, Fox PL, Mukhopadhyay CK. (2007) Regulation of Ceruloplasmin in human hepatic cells by redox active copper: Identification of a novel AP-1 site in ceruloplasmin gene. Biochem J. 402: 135-141.

Currently, research projects in Prof. Mukhopadhyay's laboratory are sponsored by DBT.

• Prof. Neena Singh, Case Western Reserve University, USA- Iron in neurodegenerative disorders.
• Prof. Amit Dinda, Department of Pathology, All India Institute of Medical Sciences, New Delhi- Role of iron in diabetic nephropathy
• Dr. Amitabha Mukhopadhyay, National Institute of Immunology, New Delhi- Gene regulation in host-leishmania interaction
• Dr. Santi M Mandal, Indian Institute of Technology, Kharagpur, West Bengal- Identification of small molecule inhibitors
• Prof. Rajendra Prasad, Director, Amity Institute of Integrative Sciences and Health, Gurgaon- Iron in multidrug resistance in Candida


CRakesh K. Tyagi
Phone No. 011-26738741/26704559
E-mail: rkt2300@mail.jnu.ac.in; rktyagi@yahoo.com
Personal webpage: http://www.jnu.ac.in/Faculty/rtyagi

Prof. R. K. Tyagi carried out his doctoral studies in biochemistry at Jawaharlal Nehru University, New Delhi. Subsequently, he pursued his research work in the area of 'Molecular Endocrinology' as a Feinberg Research Fellow at the Weizmann Institute of Science, Israel and later as INSERM international fellow in France. Prior to joining the 'Special Centre for Molecular Medicine' in April 2001 he was working in an NIH-sponsored research scheme at the University of Texas Health Science Centre, USA. He was elected to the National Academy Sciences, India during the year 2010.

Research Interests

Nuclear Receptors in health and diseases
Nuclear Receptor (NR) superfamily is a large group ligand-modulated transcription factors that regulate plethora of normal and patho-physiological processes associated with metabolism, cell differentiation, energy homeostasis, embryonic development, reproduction, xenobiotic and drug elimination. In humans, the NR superfamily comprises of 48 members which prototypically, in presence of their cognate ligands, modulate gene expression. Their dysfunction can exert a wide range of proliferative, reproductive and metabolic diseases including obesity, diabetes, inflammation, cancer etc. Being ligand-modulated transcription factors these receptors represent enormous potential to serve as targets for drug discovery for the treatment of several major diseases. Nuclear Receptors are one of the major target areas of modern therapy and research. Evidently 15% of the drugs approved for sale are used to target nuclear receptors and there is enormous scope to explore new molecules and improve upon the existing one.

Presently, the goal of our laboratory is to gain insights into the underlying molecular mechanism of nuclear receptor functions with specific reference to nuclear receptor PXR, RXR, CAR, SHP and their interacting partners. In this context, our laboratory is investigating the involvement of PXR in drug metabolism, hepatic cancer and, involvement of its polymorphic and SNP forms in normal and diseased conditions. We are also studying the interaction and dynamics of RXR with its key heterodimeric partners during cell cycle in live cells. The work has been initiated to study functional dynamics and transcriptional regulation of CAR and SHP. In addition, development of high throughput screening of therapeutics/novel drugs for assessing the clinical efficacy at PXR and CAR level is in progress. By studying the areas as defined above, we hope to identify new therapeutic targets and efficient drug screening platforms for the treatment of diseases and/or discovery of novel therapeutic molecules.

Selected Publications (since 2010)
1. Kotiya D, Jaiswal B, Ghose S, Kaul R, Datta K, Tyagi RK. (2016) Role of PXR in Hepatic Cancer: Its Influences on Liver Detoxification Capacity and Cancer Progression. PLoS One. 11: e0164087.

2. Rana M, Devi S, Gourinath S, Goswami R, Tyagi RK. (2016) A comprehensive analysis and functional characterization of naturally occurring non-synonymous variants of nuclear receptor PXR. Biochim Biophys Acta. 1859: 1183-97.

3. Priyanka, Kotiya D, Rana M, Subbarao N, Puri N and Tyagi RK. (2016) Transcription regulation of nuclear receptor PXR: role of SUMO-1 modification and NDSM in receptor function. Molecular and Cellular Endocrinology. 420: 194-207.

4. Maiti P, Ghorai P, Ghosh S, Kamthan M, Tyagi RK, Datta A. (2015) Mapping of functional domains and characterization of the transcription factor Cph1 that mediate morphogenesis in Candida albicans Fungal Genetics and Biology. 83: 45–57.

5. Kumari S, Saradhi M, Rana M, Chatterjee S, Aumercier M, Mukhopadhyay G and Tyagi RK. (2015) Pregnane & Xenobiotic Receptor gene expression in liver cells is modulated by Ets-1 in synchrony with transcription factors Pax5, LEF-1 and c-Jun. Experimental Cell Research. 330: 398-411.

6. Dash AK, Yende AS, Kumar S, Singh SK, Kotiya D, Rana M, Tyagi RK. (2014) The Constitutive Androstane Receptor (CAR): a Nuclear Receptor in Health and Disease. Journal of Endocrinology and Reproduction. 18: 59-74.

7. Kumar S and Tyagi RK. (2012) Androgen receptor association with mitotic chromatin - analysis with introduced deletions and disease-inflicting mutations. FEBS Journal. 279:4598-4614.(journal cover article)

8. Kumari S, Mukhopadhyay G, Tyagi RK. (2012) Transcriptional regulation of mouse PXR gene: an interplay of transregulatory factors. PLoS One. 7(8):e44126.

9. Kaul R, Shah P, Saradhi M, Prasad RL, Chatterjee S, Ghosh I, Tyagi RK and Datta K. (2012) Overexpression of Hyaluronan Binding Protein 1 (HABP1/p32/gC1qR) in HepG2 Cell Leads to Increased Hyaluronan Synthesis and Cell Proliferation by Upregulation of Cyclin D1 in AKT-Dependent Pathway. Journal of Biological Chemistry. 287: 19750-19764.

10. Kumar S, Saradhi M, Chaturvedi NK, Tyagi RK. (2012) Retention and transmission of active transcription memory from progenitor to progeny cells via ligand-modulated transcription factors. Cell Biology International. 36: 177-182. (Journal issue highlight)

11. Biswas A, Pasquel D, Tyagi RK, Mani S. (2011) Acetylation of Pregnane X Receptor protein determines selective function independent of ligand activation. Biochem Biophys Res Commun. 406:371-376.

12. Amazit L, Roseau1 A, Ali-Khan J, Chauchereau A, Tyagi RK, Loosfelt H, Leclerc P, Lombes M, Guiochon-Mantel A. (2011). Ligand-dependent Degradation of SRC-1 is Pivotal for Progesterone Receptor Transcriptional Activity. Molecular Endocrinology. 25:394-408.

13. Kumar S, Tyagi RK. (2010) Networking Strategies and Emerging Roles of Pregnane & Xenobiotic Receptor (PXR) in Normal and Pathological States. Journal of Endocrinology and Reproduction. 14: 1-8

14. Chaturvedi NK, Kumar S, Negi S, Tyagi RK. (2010) Endocrine disruptors provoke differential modulatory responses on Androgen Receptor and Pregnane & Xenobiotic Receptor: potential implications in metabolic disorders. Molecular and Cellular Biochemistry. 345:291-308.

15. Kumar S, Jaiswal B, Kumar S, Negi S, Tyagi RK. (2010) Cross-talk between Androgen Receptor and Pregnane & Xenobiotic Receptor reveals existence of a novel modulatory action of antiandrogenic drugs. Biochemical Pharmacology. 80: 964-976.

Research projects sponsored by ICMR, CSIR, DST & UGC



CSuman K. Dhar
Phone No. 011-26742572/ 26738774
E-mail: skdhar2002@yahoo.co.in, skdhar@mail.jnu.ac.in
Weblink: http://www.jnu.ac.in/faculty/sdhar

Prof. Suman Kumar Dhar did his Ph. D. in Molecular Parasitology from Jawaharlal Nehru University, New Delhi. During his graduate school, he studied the replication and maintenance of ribosomal DNA circle in the protozoan parasite Entamoeba histolytica, which causes amebiasis in humans. Later during his post-doctoral tenure he studied the initiation of mammalian DNA replication at the Brigham and Women's Hospital, Harvard Medical School, Boston, USA. He returned to India in 2001 and started his independent research career in SCMM, JNU.

Research Interests

DNA replication initiation and cell division in the pathogenic bacteria Helicobacter pylori
Helicobacter pylori is a gram-negative, spiral-shaped pathogenic bacterium which causes peptic ulcer diseases and chronic gastritis. WHO has recognized H. pylori as a primary risk factor for the development of intestinal type gastric adenocarcinoma. There is no vaccine available in the market at present and prevalence of antibiotic resistant strains is on the rise. Experimental data to understand the basic biology of the bacteria concerning the chromosomal DNA replication of H. pylori are scarce. Our current research interests include structure-function aspects of replicative helicase HpDnaB and its interacting partners, understanding the biological significance of polar replisome/divisome complex and looking for small molecule inhibitors that may block these processes.

Cell cycle regulation and DNA synthesis in Plasmodium falciparum
Malaria continues to be a major health problem globally. The situation is becoming alarming due to the lack of an effective vaccine and increasing incidence of antimalarial drug resistance. There is an urgent need to understand the fundamental biology and biochemical processes at the different stages of the parasite. This will help to identify new targets for the development of novel drugs and vaccines. One aspect of parasite metabolism, which could be useful in this regard, is DNA replication. DNA replication takes place at five distinct points in the parasite life cycle. DNA replication initiation, the rate determining step in DNA replication has not been characterized in P. falciparum. Our goal is to understand the mechanism of chromosomal DNA replication initiation by biochemical and genetic analysis of these proteins at different points during erythrocytic stage of the parasite life cycle. The role of replication initiation proteins in apicoplast DNA replication are also being explored. Using protein-protein interaction, we are trying to identify and characterize other members of the preRC which might reveal features unique to the parasite DNA replication machinery. Investigation of the components involved in chromosomal and plastid DNA replication initiation and identification of chromosomal DNA replication origin may lead to the identification of new potential drug targets for malaria therapy. Further, some of these proteins are also involved in parasite var gene regulation involved in immune evasion. We are interested in finding the regulation of these proteins that may control important aspects of parasite biology. A Chemical Biology approach has also been undertaken for finding potential antimalarials.

Research projects in Dr. Dhar's laboratory are sponsored by Department of Science and technology, Department of Biotechnology and University Grant Commission, India.

Selected Publications:
1. Deshmukh AS, Agarwal M, Dhar SK. (2016) Regulation of DNA replication proteins in parasitic protozoans: possible role of CDK-like kinases. Curr Genet. 62:481-486.

2. Verma V, Kumar A, Nitharwal RG, Alam J, Mukhopadhyay AK, Dasgupta S, Dhar SK. (2016) Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori. Nucleic Acids Res, 44:3288-3303.

3. Kamran M, Sinha S, Dubey P, Lynn AM, Dhar SK. (2016) Identification of putative Z-ring-associated proteins, involved in cell division in human pathogenic bacteria Helicobacter pylori. FEBS Lett, 590:2158-2171.

4. Narayanaswamy N, Das S, Samanta PK, Banu K, Sharma GP, Mondal N, Dhar SK, Pati SK, Govindaraju T. (2015) Sequence-specific recognition of DNA minor groove by an NIR-fluorescence switch-on probe and its potential applications. Nucleic Acids Res. 43:8651-63.

5. Deshmukh AS, Agarwal M, Mehra P, Gupta A, Gupta N, Doerig CD, Dhar SK. (2015) Regulation of Plasmodium falciparum Origin Recognition Complex subunit 1 (PfORC1) function through phosphorylation mediated by CDK like kinase PK5. Molecular Microbiology, 98: 17-33.

6. Mitra P, Banu K, DeshmukhAS, Subbarao N, Dhar SK. (2015) Functional dissection of Proliferating Cell Nuclear Antigens (1&2) in human malarial parasite Plasmodium falciparum : possible involvement in DNA replication and DNA damage response. Biochemical Journal, 470: 115-29.

7. Narayanaswamy N, Kumar M, Das S, Sharma R, Samanta PK, Pati SK, Dhar SK, Kundu TK, Govindaraju T. (2014) A Thiazole Coumarin (TC) Turn-On Fluorescence Probe for AT-Base Pair Detection and Multipurpose Applications in Different Biological Systems. Sci Rep. 4: 6476.

8. Srivastava S, Bhowmick K, Chatterjee S, Basha J, Kundu TK, Dhar SK. (2014) Histone H3K9 acetylation level modulates gene expression and may affect parasite growth in human malaria parasite Plasmodium falciparum. FEBS J. 281: 5265-78

9. Dana S, Prusty D, Dhayal D, Gupta MK, Dar A, Sen S, Mukhopadhyay P, Adak T, Dhar SK. (2014) The potent Anti-malarial activity of Acriflavine in vitro and in vivo. ACS Chem Biol. 9: 2366-73.

10. Sharma A, Kamran M, Verma V, Dasgupta S, Dhar SK. (2014) Intracellular Locations of Replication Proteins and the Origin of Replication during Chromosome Duplication in the Slowly Growing Human Pathogen Helicobacter pylori. J Bacteriol. 196: 999-1011. Journal cover article.

11. Bhowmick K, Dhar SK. (2013) Plasmodium falciparum single-stranded DNA-binding protein (PfSSB) interacts with PfPrex helicase and modulates its activity. FEMS Microbiol Lett. 351: 78-87.

12. Abdul Rehman SA, Verma V, Mazumder M, Dhar SK1, Gourinath S1. (2013) Crystal structure and mode of helicase binding of the C-terminal domain of primase from Helicobacter pylori. J Bacteriol. 195: 2826-38. (1Co-corresponding author)

13. Deshmukh A, Srivastava S, Herrmann S, Gupta A, Mitra P, Gilberger TW and Dhar SK. (2012) The role of N-terminus of Plasmodium falciparum ORC1 in telomeric localization and var gene silencing. Nucleic Acids Research, 40: 5313-31.

14. Nitharwal RG, Verma V, Subbarao N, Dasgupta S, Choudhury NR and Dhar SK. (2012) DNA binding activity of Helicobacter pylori DnaB helicase: the role of the N-terminal domain in modulating DNA binding activities. FEBS J. 279:234-50. Journal cover article.



CGobardhan Das
Phone No. 011 -26738824
E-mail: ckm2300@mail.jnu.ac.in
Personal webpage: http://www.jnu.ac.in

Prof. Gobardhan Das received his Ph.D. from Institute of Microbial Technology, Chandigarh, India and postdoc from Yale University. He has been Principal Investigator at Aventis Pharmaceuticals, Bridgewater, NJ (2002-2007); Staff Research Scientist at ICGEB, New Delhi (2007-2013); and Professor at University of KwaZulu-Natal, Durban, South Africa (2013-present). Prof. Das joined SCMM as Professor in 2014.

Research Interest

Infection and Immunology especially, discovery of small molecules and new method for the treatment of TB which devoid generation of drug resistant forms (MDR and XDR) of TB.

Tuberculosis remains the biggest threat to the modern society, which claims 2 millions of lives every year. An estimation by World Heath Organization (WHO) indicated that one third of global population is infected with latent form of TB, which is an enormous reservoir for an epidemic in the event of natural calamities especially that impacts on immune system.

Our Research Group focus on:
Aim 1. Identification of bacterial genes that are required for the adaptation and prolonged survival within MSCs.
Aim 2. Identification of host genes that restricts the growth of invaded organisms, and in turn allows the establishment of persistent infection.

Besides, current therapy of tuberculosis consists of several expensive antibiotics and the treatment period is long, which incorporates the risk for the generation of drug resistant variants of TB. All most all the countries irrespective of their socio-economic status are under threat from drug resistant TB. Unfortunately, the rate the bacteria acquiring rug resistance and the discovery of new lines of drugs is much faster, which resulted in the appearance of totally drug resistant (TDR) form of TB. Furthermore, patients treated with conventional antibiotics are more vulnerable for reactivation and reinfection of the disease at post treatment. As a result current therapy has a deleterious effect on the host protective immunity.

Thus, our group further aims to:
1. Generate Curcumin-Allicin hybrid compound
2. Development of bio-assay for screening compounds.
3. In vivo validation of compound.

Selected publications:

1. Singh DK, Dwivedi VP, Ranganathan A, Bishai WR, Kaer LV, Das G. (2016) Blockade of the Kv1.3 K+ channel enhances BCG vaccine efficacy by expanding central memory T lymphocytes. J Infect Dis. [Epub ahead of print]

2. Rahman MA, Sobia P, Dwivedi VP, Bhawsar A, Singh DK, Sharma P, Moodley P, Van Kaer L, Bishai WR, Das G. (2015) Mycobacterium tuberculosis TlyA Protein Negatively Regulates T Helper (Th) 1 and Th17 Differentiation and Promotes Tuberculosis Pathogenesis. J Biol Chem. 290: 14407-17.

3. Yadav V, Dwivedi VP, Bhattacharya D, Mittal A, Moodley P, Das G. (2015) Understanding the Host Epigenetics in Mycobacterium tuberculosis Infection. J Genet Genome Res. 2: 016.

4. Bali P, Tousif S, Das G, Van Kaer L. (2015) Strategies to improve BCG vaccine efficacy. Immunotherapy. 7: 945-8.

5. Rahman MA, Sobia P, Dwivedi VP, Bhawsar A, Singh DK, Sharma P, Moodley P, Van Kaer L, Bishai WR, Das G. (2015) Mycobacterium tuberculosis TlyA Protein Negatively Regulates T Helper (Th) 1 and Th17 Differentiation and Promotes Tuberculosis Pathogenesis. J Biol Chem. 290: 14407-17.

6. Kumar P, Tyagi R, Das G, Bhaskar S. (2014) Mycobacterium indicus pranii and Mycobacterium bovis BCG lead to differential macrophage activation in Toll-like receptor-dependent manner. Immunology. 143: 258-68.

7. Tousif S, Singh DK, Ahmad S, Moodley P, Bhattacharyya M, Van Kaer L, Das G. (2014) Isoniazid induces apoptosis of activated CD4+ T cells: implications for post-therapy tuberculosis reactivation and reinfection. J Biol Chem. 289: 30190-5.

8. Bhattacharya D, Dwivedi V P, Kumar S, Reddy M C, Kaer LV, Moodley P, Das G. (2014) Simultaneous Inhibition of T Helper 2 and T Regulatory Cell Differentiation by Small Molecules Enhances Bacillus Calmette - Guerin vaccine Efficacy against Tuberculosis. J Biol Chem. 289: 33404–11.

Current External collaborations:
1. Prof. Alfred Bothwell, Yale University School of medicine, New Haven, CT.
2. Luc Van Kaer, Ph.D., Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Vanderbilt, TN
3. Yufang Shi, Ph.D., Robert Wood Johnson Medical School, UMDNJ, Piscataway, NJ.


CAnand Ranganathan
Associate Professor
E-mail: aranganathan@mail.jnu.ac.in
Personal webpage: http://www.jnu.ac.in

Dr. Ranganathan did his Ph.D. in Biochemistry from Pembroke College, University of Cambridge, UK; and Postdoc from the Department of Biochemistry, University of Cambridge, UK. He has also worked as a Research Scientist in the Recombinant Gene Products Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), New Delhi, India before joining SCMM as Associate Professor in 2015.

Research Interests

Inhibiting Protein-Protein Interactions in Pathogens
Our laboratory had previously developed a method for laboratory-directed evolution of proteins, called 'codon-shuffling'. The potential of this method to create stand-alone de novo protein/peptide libraries, for their eventual use as antibacterial and drug-like entities has since been realised. Because of an inherent property of each of the fourteen dicodons (oligonucleotides 6 bases in length) in the 'dicodon set' to possess a secondary structure imprint, the assembly of such dicodons creates proteins with well-folded characteristics, largely due to the accumulation of so-called secondary structure imprints that form predefined helical and sheet protein folds. The application of codon-shuffling has been the underlying theme of research in our laboratory for more than a decade. Recently, we isolated a peptide that can disrupt the crucial ESAT6:CFP10 protein-protein interaction in M. tuberculosis. Exo- or endogenous presence of this peptide, named HCL2, severely affects mycobacterial growth as well as its cell-wall structure and colony morphology. It was shown that mycobacteria expressing this peptide show a drastic reduction in colony forming units. Efforts are now directed towards exploring the possibility of an HCL2-attenuated M. tuberculosis strain to act as a viable vaccine candidate.

More recently, we discovered a codon-shuffled de novo protein M5, of 100 amino acid length, that was able to disrupt the ICAM-1 dimer formation in vivo. The presence of ICAM-1 (Intercellular adhesion molecule) is crucial for the progression of diseases like tuberculosis, HIV, and Malaria. It was shown that M5, in quantities as little as 25 µM, is able to block the entry of P. falciparum into red blood cells by almost 80%. Not only has this discovery opened avenues to study the role of ICAM-1 or ICAM-like molecules in the invasion process, the drug-like potential of M5, or peptidomimetics based on M5, is also being explored.

Selected publications:

1. Singh DK, Dwivedi VP, Ranganathan A, Bishai WR, Kaer LV, Das G. (2016) Blockade of the Kv1.3 K+ channel enhances BCG vaccine efficacy by expanding central memory T lymphocytes. J Infect Dis. [Epub ahead of print]

2. Bhalla K, Chugh M, Mehrotra S, Rathore S, Tousif S, Dwivedi VP, Prakash P, Samuchiwal SK, Kumar S, Singh DK, Ghanwat S, Kumar D, Das G, Mohmmed A, Malhotra P*, Ranganathan A*. (2015) Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum. Nat Commun. 6: 6049.

3. Samuchiwal SK, Tousif S, Singh DK, Kumar A, Ghosh A, Bhalla K, Prakash P, Kumar S, Bhattacharyya M, Moodley P, Das G, Ranganathan A*. (2014) A peptide fragment from the human COX3 protein disrupts association of Mycobacterium tuberculosis virulence proteins ESAT-6 and CFP10, inhibits mycobacterial growth and mounts protective immune response. BMC Infect Dis. 14: 355.

4. Samuchiwal SK, Tousif S, Singh DK, Kumar A, Ghosh A, Bhalla K, Prakash P, Kumar S, Trivedi AC, Bhattacharyya M, Das G, Ranganathan A*. (2014) A novel peptide interferes with Mycobacterium tuberculosis virulence and survival. FEBS OpenBio 4: 735-40.

5. Ghosh A, Tousif S, Bhattacharya D, Samuchiwal SK, Bhalla K, Tharad M, Kumar S, Prakash P, Kumar P, Das G, Ranganathan A*. (2013) Expression of the ARPC4 subunit of Human Arp2/3 severely affects Mycobacterium tuberculosis growth and suppresses immunogenic response in murine macrophages. PLoS One 8, e69949.

6. Tharad M, Samuchiwal SK, Bhalla K, Ghosh A, Kumar K, Kumar S, Ranganathan A*. (2011) A Three-Hybrid System to Probe in vivo Protein-Protein Interactions: Application to the Essential Proteins of the RD1 Complex of M. tuberculosis. PLoS One 6, e27503.

7. Kumar K, Tharad M, Ganapathy S, Ram G, Narayan A, Khan JA, Pratap R, Ghosh A, Samuchiwal SK, Kumar S, Bhalla K, Gupta D, Natarajan K, Singh Y, Ranganathan A*. (2009) Phenylalanine-rich peptides potently bind ESAT6, a virulence determinant of Mycobacterium tuberculosis, and concurrently affect the pathogen's growth. PLoS One 4, e7615.

8. Rao A, Chopra S, Ram G, Gupta A, Ranganathan A*. (2005) Application of the "codon-shuffling" method. Synthesis and selection of de novo proteins as antibacterials. J Biol Chem 280: 23605-14.

9. Chopra S, Ranganathan A*. (2003) Protein evolution by "codon shuffling": a novel method for generating highly variant mutant libraries by assembly of hexamer DNA duplexes. Chem Biol 10: 917-26.

CSouvik Bhattacharjee
Associate Professor
Phone No. 011-2670-4559
E-mail : souvik@jnu.ac.in; sbh174@gmail.com
Personal webpage: http://www.jnu.ac.in

Dr. Souvik Bhattacharjee received his Ph.D. from Institute of Microbial Technology, Chandigarh. He did his Postdoc from Department of Pathology, Feinberg School of Medicine, Northwestern University, Chicago and Center for Rare and Neglected Diseases, Department of Biological Sciences, University of Notre Dame, Notre Dame, Indiana. Dr. Bhattacharjee has been Research Assistant Professor at the Center for Rare and Neglected Diseases, Department of BiologicalSciences, University of Notre Dame, Notre Dame, Indiana from 2010 – 2015; and joined SCMM (JNU) in 2015.

Research Interest

Malaria: Molecular Target
Biology of Plasmodium falciparum infection
Protein trafficking pathways in malaria infected erythrocytes
Molecular mechanism for antimalarial drug-resistance

According to the WHO Malaria Report 2013, around 3.3 billion people are at risk of contracting malaria annually, leading to an estimated 198 million cases and 584,000 deaths. Concerted global efforts have been largely successful in bringing down this disease burden, using artemisinin-based combination therapies (ACTs). However, the parasite resistance to the frontline antimalarial has been detected in the Greater Mekong sub-region (Cambodia, Laos, Myanmar, Thailand and Viet Nam), and in some areas the parasite has become resistant to most available antimalarials. This emergence of multi-drug resistance and its potential to rapidly spread worldwide is a major concern.

Plasmodium falciparum causes the most deadly form of human malaria. It has two distinct life cycle stages that involves female Anopheles mosquitoes (sexual stage) and human hosts (asexual stage). A part of the asexual life cycle involves infection and propagation with mature human red blood cells and this intraerythrocytic cycle manifests as classical clinical pathologies like fever, chills and anemia that can lead to coma and death if untreated. Extracellular 'merozoites' (free-form of the parasite liberated after a brief intra-hepatocytic cycle) actively invade human erythrocytes and proliferate from an early 'ring' to a more mature 'trophozoite' and finally differentiating to a segmented 'schizont'. Schizonts rupture to liberate 16-32 daughter merozoites that reinvade red blood cells to continue the parasite's asexual life cycle.

My laboratory places primary emphasis on this intraerythrocytic stage of infection. We use latest technologies in cell biology and molecular biology to genetically manipulate the parasite in an effort to understand its mechanism of pathogenesis and the development of drug-resistance.

The two distinct (yet interconnected) areas that we are actively focusing are:

1) Protein trafficking pathways of P. falciparum infected erythrocytes

While the intraerythrocytic residence provides a safe haven for P. falciparum away from threats of the host immune challenges; it also places a huge burden on the parasite's nutritional demand. The mature human red cell is metabolically inert with no de novo protein or lipid synthesis capability, and 'nutrients' generated by the digestion of hemoglobin by the parasite are simply insufficient to sustain its survival. So, P. falciparum extensively modifies this infected host cell with several hundred parasite-encoded proteins exported beyond its double-membrane barrier that separates the parasite from the host cell cytosol: the parasite plasma membrane (PPM) and the parasitophorous vacuolar membrane (PVM). These proteins play essential roles in virulence and/or growth. It is our keen interest to reveal the molecular mechanism regulating how proteins are exported and whether common machineries are involved in trafficking the different classes of exported proteins.

2) Development of artemisinin-resistance in P. falciparum

Artemisinins are rapidly acting drugs, used in in combination with longer acting antimalarials in ACT. Currently there is no vaccine against malaria and the recent development of clinical resistance of P. falciparum to artemisinin derivatives threatens malaria control and eradication strategies worldwide. Clinically, artemisinin-resistance is defined as a reduced parasite clearance rate from peripheral blood and a parasite clearance half-life of >5 h, following ACT. Resistance to artemisinin has recently been reported to be a heritable trait and linked to mutations in P. falciparum kelch-propeller domain protein PfKelch13. However, little is known about the role of PfKelch13 and why it is a marker for resistance. A complex molecular and cellular reprogramming is predicted to underlie PfKelch13 function. We attempt to systematically dissect the role PfKelch13 through mutations commonly seen in clinical isolates and evaluate their impact at the host and parasite interface.

Selected publications:

1. Mbengue A *, Bhattacharjee S *, Pandharkar T, Liu H, Estiu G, Stahelin RV, Rizk SS, Njimoh DL, Ryan Y, Chotivanich K, Nguon C, Ghorbal M, Lopez-Rubio JJ, Pfrender M, Emrich S, Mohandas N, Dondorp AM, Wiest O, Haldar K. (2015) A molecular mechanism of artemisinin resistance in Plasmodium falciparum malaria. Nature. 520: 683–687. *Equal contributing first author.

2. Bhattacharjee S, Stahelin RV, Speicher KD, Speicher DW, Haldar K. (2012) Endoplasmic Reticulum PI(3)P lipid binding targets malaria proteins to the host cell. Cell. 148: 201-12.

3. Bhattacharjee S, van Ooij C, Balu B, Adams JH, Haldar K. (2008) Maurer`s clefts of P. falciparum are secretory organelles that concentrate virulence protein reporters for delivery to the host erythrocyte. Blood. 111: 2418-26.

4. Bhattacharjee S, Hiller NL, Liolios K, Win J, Kanneganti TD, Young C, Kamoun S, Haldar K. (2006) The malarial host-targeting signal is conserved in the Irish potato famine pathogen. PLoS Pathog. 2: e50.

5. Hiller NL, Bhattacharjee S, van Ooij C, Liolios K, Harrison T, Lopez-Estrano C, Haldar K. (2004) A host-targeting signal in virulence proteins reveals a secretome in malarial infection. Science. 306: 1934-7.

Current members of the lab
Ms. Pragya Namdev (Ph.D. student)
Mr. Tarkeshwar Kumar (Ph.D. student)
Ms. Satarupa Maitra (DBT Builder Program)
Mr. Ajay Kumar (Lab helper)


CShailja Singh
Associate Professor
E-mail: shailja.singh@jnu.ac.in
Personal Webpage: http://www.jnu.ac.in/Faculty

Dr. Shailja Singh gained her PhD from University of Delhi in the area of Biomedical Sciences. Following this, she joined Malaria Group at International Centre for Genetic Engineering and Biotechnology as postdoctoral fellow. In 2009, she got innovative Young Biotechnologist Award from Department of Biotechnology, Govt. of India, to conduct her independent research on molecular signal and machinery involved in egress of Plasmodium falciparum merozoites from host erythrocytes. In 2013, she joined as Associate Professor in Shiv Nadar University. She joined SCMM in 2016 as Associate Professor.

Research Interest
• Parasitic infections: Molecular Mechanisms of Host Pathogen Interactions
• Molecular signal and signaling machinery involved in invasion and egress of parasites

During the blood stage, Plasmodium parasites invade host red blood cells, multiply, egress and reinvade uninfected red blood cells to continue the life cycle. Entry into (invasion) and exit from (egress) are highly regulated processes that are mediated by array of parasite molecules. These parasite molecules are stored in specialized apical secretory vesicles and the timely release of these proteins to the merozoite surface or to the host cell membrane is critical for successful invasion and egress. The discharge of parasite ligands to the merozoites apical surface mediates the formation and movement of a junction between the invading merozoite and host erythrocyte during invasion. The timely discharge of many parasite proteases and pore forming proteins helps in permeabilization and dismantling of limiting membranes during egress.

Our research focuses on understanding of the molecular signal and machinery involved in invasion and egress of Plasmodium falciparum merozoites from host erythrocytes, involving multidisciplinary approach such as live cell imaging, molecular biology, cell biology and protein chemistry. Real-time light microscopic visualization of in vitro blood-stage egress in live parasites has played a special role in studies on signals regulating theses processese. We have demonstrated for the first time a role of intracellular Ca2+ in regulation of egress of P. falciparum merozoites from schizonts. A sharp rise in intracellular Ca2+ just before egress, observed by time-lapse video microscopy, suggested a role for intracellular Ca2+ in this process. Chelation of intracellular free Ca2+ with chelators such as BAPTA-AM or inhibition of Ca2+ release with phospholipase C (PLC) inhibitors blocks merozoite egress. Interestingly, chelation of intracellular Ca2+ in schizonts was found to block the discharge of a key protease PfSUB1 (subtilisin like protease1) and Perforin like proteins from apical organelles of P. falciparum merozoites to parasitophorous vacuole (PV) and host cell membranes. This leads to inhibition of processing of PfSERA5 (serine repeat antigen5); block in parasitophorous vacuolar membrane (PVM) rupture and permeabilization and merozoite egress. A complete understanding of the steps regulating egress and invasion of P. falciparum merozoites may provide novel targets for synthetic biology approaches that block invasion and egress and limit parasite growth. We are now studying the role of effectors od signaling cascades in invasion and egress of P. falciparum merozoites.

Description: invasion Description: egress

Running Grants:
1. Singh, S. Role of calcium signaling in egress of Plasmodium falciparum merozoites from host erythrocytes. Innovative Young Biotechnologist Grant, DBT, (2013-2016)

2. Singh, S. Antiperforin as antimalarial. DST, (2013-2016)

3. Singh, S. Understanding Critical Events in Biology of Blood Stage of Malaria Parasite. DBT, (2011-2016; as Co-Investigator)

4. Singh S. Marine Synthetic Biology. capacity building and human resources. DBT, (2017-2020; as Co-Investigator)

5. Singh, S. Mining the secretome of Plasmodium falciparum merozoites for identification of
Novel targets involved in blood stage malaria parasite infection. DST, (2017-2019)

Selected Publications:

1. Alam MM, Solyakov L, Bottrill AR, Flueck C, Siddiqui FA, Singh S, Mistry S, Viskaduraki M, Lee K, Hopp CS, Chitnis CE, Doerig C, Moon RW, Green JL, Holder AA, Baker DA, Tobin AB. (2015) Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion. Nat Commun 6: 7285.

2. Kaderi Kibria KM, Rawat K, Klinger CM, Datta G, Panchal M, Singh S, Iyer GR, Kaur I, Sharma V, Dacks JB, Mohmmed A, Malhotra P. (2015). A role for adaptor protein complex 1 in protein targeting to rhoptry organelles in Plasmodium falciparum. Biochim Biophys Acta 1854: 699-710.

3. Prabhu G, Agarwal S, Sharma V, Madurkar SM, Munshi P, Singh S*, Sen S. (2015). A natural product based DOS library of hybrid systems. Eur J Med Chem 95: 41-48.

4. Hati S, Madurkar SM, Bathula C, Thulluri C, Agarwal R, Siddiqui FA, Dangi P, Adepally U, Singh A, Singh S*, Sen S. (2015). Design, synthesis and biological evaluation of small molecules as potent glycosidase inhibitors and antimalarials. Eur J Med Chem. 100: 188-96.

5. Krishnan R, Kumar V, Ananth V, Singh S, Nair AS, Dhar PK. (2015). Computational identification of novel microRNAs and their targets in the malarial vector, Anopheles stephensi. Syst Synth Biol. 9: 11-7.

6. Dawn A, Singh S*, More KR, Siddiqui FA, Pachikara N, Ramdani G, Langsley G, Chitnis CE. (2014) The central role of cAMP in regulating Plasmodium falciparum merozoite invasion of human erythrocytes. PLoS Pathog. 10: e1004520.

7. Sharma V, Agarwal S, Madurkar SM, Datta G, Dangi P, Dandugudumula R, Sen S, Singh S*. (2014) Diversity-oriented synthesis and activity evaluation of substituted bicyclic lactams as anti-malarial against Plasmodium falciparum. Malar J 13: 467.

8. Agarwal S, Sharma V, Kaul T, Abdin MZ, Singh S*. (2014) Cytotoxic effect of carotenoid phytonutrient lycopene on P. falciparum infected erythrocytes. Mol Biochem Parasitol. 197: 15-20.

9. Sharma M, Dhiman C, Dangi P, Singh S. (2014) Designing synthetic drugs against Plasmodium falciparum: a computational study of histone-lysine N methyltransferase (PfHKMT). Syst Synth Biol. 8: 155-160.

10. Garg S, Agarwal S, Kumar S, Yazdani SS, Chitnis CE, Singh S*. (2013) Calcium-dependent permeabilization of erythrocytes by a perforin-like protein during egress of malaria parasites. Nat Commun. 4:1736.

11. Agarwal S, Singh MK, Garg S, Chitnis CE, Singh S*. (2013) Ca(2+)-mediated exocytosis of subtilisin-like protease 1: a key step in egress of Plasmodium falciparum merozoites. Cell Microbiol 15:910-921.

12. Hans N, Singh S, Pandey AK, Reddy KS, Gaur D and Chauhan VS. (2013) Identification and characterization of a novel Plasmodium falciparum adhesin involved in erythrocyte invasion. PLoS One 8: e74790.


Saima Aijaz
Assistant Professor
Phone No. 011-2673 8733
E-mail: s_aijaz@mail.jnu.ac.in
Personal Webpage: http://www.jnu.ac.in/Faculty/saijaz

Dr. Saima Aijaz obtained her Ph.D from the Indian Institute of Science, Bangalore, India where she worked on the characterization of the outer capsid protein of rotavirus to evaluate its role as a recombinant vaccine candidate. She carried out post-doctoral work at the University of Bath and University College London (UCL), United Kingdom. At UCL, she worked extensively on the functional characterization of proteins associated with epithelial tight junctions. Dr. Aijaz joined SCMM in 2008.

Research Interests

Epithelial and endothelial cells are held together by adhesive junctional complexes that consist of tight junctions, adherens junctions and desmosomes. Tight junctions selectively regulate paracellular permeability and prevent the intermixing of apical and basolateral proteins of the plasma membrane. Regulation of paracellular permeability is a critical function of tight junctions and increased permeability is associated with diverse disease conditions ranging from bacterial and viral infections to cancer and metastasis. Research in the laboratory is focused on the molecular mechanisms that regulate the disruption of tight junctions in epithelial and endothelial cells in response to pathologic stimuli. In one approach, Enteropathogenic E.coli (EPEC) is used as a model to study the regulation of paracellular permeability. EPEC disrupts epithelial tight junctions and is a leading cause of diarrhea in the developing world. Several EPEC effectors such as EspF, EspG, Map and NleA have been reported to disrupt the tight junction barrier causing severe loss of water and electrolytes from the body and is fatal in infants. However, the underlying mechanisms that cause the drastic increase in permeability through intestinal junctions have not been elucidated yet

The laboratory is engaged in the identification of tight junction-based signaling pathways that regulate the EPEC-mediated leakage through tight junctions with the ultimate goal of identifying molecules to block/reverse this leakage.

Selected Publications:

1. Singh AP, Aijaz S. (2015). Generation of a MDCK cell line with constitutive expression of the Enteropathogenic E. coli effector protein Map as an in vitro model of pathogenesis. Bioengineered. 6: 335-341.

2. Singh AP, Aijaz S. (2015). Enteropathogenic E. coli:Breaking the intestinal tight junction barrier. F1000Research. 4: 231.

3. Nie M, Aijaz S, Leefa Chong San IV, Balda MS, Matter K. (2009). The Y-box factor ZONAB/DbpA associates with GEF-H1/Lfc and mediates Rho-stimulated transcription. EMBO Reports. 10: 1125-1131.

4. Aijaz S, Sanchez-Heras E, Balda MS, Matter K. (2007). Regulation of tight junction assembly and epithelial morphogenesis by the heat shock protein Apg-2. BMC Cell Biology. 8: 49.

5. Aijaz S, Balda MS, Matter K. (2006) Tight junctions: Molecular architecture and function. International Reviews in Cytology. 248: 261-298.

Research Funding:
Department of Biotechnology, ICMR, UPE2 and DST-PURSE


Dipankar Ghosh
Assistant Professor
Phone No. 011-26738781
E-mail : ghoshd@jnu.ac.in
Personal webpage: http://www.jnu.ac.in

Dr. Ghosh did his Ph.D. from Jadavpur University Kolkata and Postdoctoral Training (Immunology) from The Cleveland Clinic Ohio, USA.

Research Interest

Early host-microbe interactions, Quorum Signaling in gut microbiome, Probiotics, Mass Spectrometry based metabolomics.

The human commensal microbiome in the gut, skin and other physiologically important niche, play critical role in health and disease. Accumulating evidences indicate that host-microbiota associations involve complex inter-species, intra-species and cross-kingdom communications, mediated by a diverse array of small MW signalling molecules similar to eukaryotic hormones. The bacterial Quorum Signalling (QS) molecules are increasingly investigated in these functions. A very large number of QS molecules, spanning several discrete chemical classes exist in bacterial kingdom. However, many of these are still uncharacterized. Our Research Group aims to:

1. Chemically characterize QS molecules in specific bacteria and/or mixed community microbiota (associated with human diseases like Irritable Bowel Syndrome) using Non-targetted Metabolomics.

2. Characterize mammalian post-translational phosphorylation cascades associated with cross-kingdom signalling by specific (bacterial) QS metabolites.

Selected publications:

1. Pluhácek T, Lemr K, Ghosh D, Milde D, Novák J, Havlícek V. (2016) Characterization of microbial siderophores by mass spectrometry. Mass Spectrom Rev. 35(1):35-47.

2. Augustine J, Maity C, Kumar P, Gupta S, Ghosh D, Verma M. (2015) Epithelial Loss Correlated with Decreased Beta Defensins and Increased Risk of Candida Infections in Oral Lichen Planus. Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology. 3: e111.

3. Kumar A, Sarkar S K, Ghosh D, Ghosh AS. (2012) Deletion of penicillin binding protein 1b impairs biofilm formation and motility in Escherichia coli. Res. in Microbiol. 163: 254-7.

4. Shireen T, Venugopal SK, Ghosh D, Gadepalli R, Dhawan B, Mukhopadhyay K. (2009). In vitro antimicrobial activity of alpha-melanocyte stimulating hormone against major human pathogen Staphylococcus aureus. Peptides 30: 1627-1635.

5. Salzman NH, Ghosh D, Huttner KM, Paterson Y, Bevins CL. (2003) Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature. 422: 522-6.

International Collaboration/Consultancy:

• Prof. Sanjoy K. Bhattacharya, Bascom Palmer Eye Institute, Florida, USA (Lipiodomics and Innate Immunity of Eye Diseases).

National Collaborations:

• Prof. Anindya Ghosh, Department of Biotechnology, Indian Institute of Technology, Kharagpur (Bacterial Biofilms).

• Dr. Venkat Panchagnula, National Chemical Laboratory, Pune (Laser Desorption Ionization Mass Spectrometry).
• Prof. Uday Ghoshal, Department of Gastroenterology, Sanjay Gandhi Post Graduate Institute of Medical Sciences, Lucknow (Pathobiology of Noninfectious Gastrointestinal Diseases and Probiotics).

• Dr. Saugata Saha, Department of Molecular Biology & Biotechnology, Tezpur University, Assam (Post-translational Modification (PTM) analysis of Protein Arginylation).

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