Institute of Molecular Medicine,
254 , Okhla Industrial Estate,
Phase III
New Delhi 110020, India
Phone: Off: 41028710 Ext: 210
E-mail: anuja@immindia.org
PhD, National Institute of Immunology, New Delhi (2001).
M.Sc Biochemistry, All India Institute of Medical Sciences, New Delhi (1995).
2008-Present, Research Scientist; Institute of Molecular Medicine, New Delhi
2005 -2008, Research Associate, Biochemistry Department, University of Delhi South campus
2004-2005, Post Doctoral Fellow, Biochemistry Department, University of Delhi South campus
2001-2003, Knowledge Scientist, Spectramind
Grant award under the FAST TRACK Scheme for Young Scientists by the Department of Science and Technology (DST), Ministry of Science and Technology, Govt. of India, (2009).
Rapid Grant for Young Investigators by Department of Biotechnology (DBT), Ministry of Science and Technology, Govt. of India (2009).
SERC Fast Track Proposal for Young Scientist (Life Sciences) awarded by Department of Science and Technology, Government of India (2005).
Society of Young Scientist (SYS) award for obtaining 1st rank in Masters Degree, AIIMS
Junior Research Fellowship, CSIR at National Institute of Immunology (1995-1997).
Senior Research Fellowship, CSIR at National Institute of Immunology (1997-2000).
Molecular mechanism of membrane fusion
Cellular membrane fusion is one of the most common ways for molecules to enter or exit cells, in processes such as fertilization and viral infection. When two cells fuse together, their membranes come together at one location and create a connection between the cells that allows the exchange of material between them. Eventually, the two membranes form one single, continuous membrane surrounding the contents of both cells. Knowledge about membrane fusion could help develop systems in which a drug or gene of interest is enclosed in a membrane known to fuse with specific cells in our body, thus facilitating drug delivery or improving gene therapy. Understanding cell fusion may be key to preventing viral infection also. So we want to study the determinants or residues of fusion proteins involved in fusion process.
Mapping of serotype specific Dengue virus neutralizing epitope
Infection by a Dengue (DEN) virus can result in a wide spectrum of outcomes ranging from mild febrile illness and classic dengue fever to the severe and potentially fatal forms of Dengue hemorrhagic fever (DHF) and Dengue shock syndrome (DSS). There are four serotypes of dengue virus which have similar clinical presentation, epidemiology and distribution. Infection with any one serotype of DEN appears to confer lifelong immunity to reinfection with the same serotype, but not to the other serotypes. Individuals sequentially infected with a different dengue serotype appear to be at higher risk for developing more severe disease. Immune enhancement has been proposed as the mechanism responsible for DHF/DSS. Because of this phenomenon, an effective vaccine must be either serotype specific or be against all four serotypes of dengue virus to ensure that vaccination against a single serotype does not enhance infection with a different serotype. It is known that self limited Dengue infected individuals tend to have potent serum antibodies that neutralize Dengue virus well. Our goal is to develop vaccine candidate which are able to elicit only neutralizing antibodies. One way to reach this goal could be to backtrack from the neutralizing antibody to its corresponding epitope and use the latter as an immunogen. Once we are able to identify effective neutralizing epitopes of each serotype, a chimeric vaccine combining protective epitopes of all four serotypes should help us develop safe and efficient vaccine candidate which is able to induce effective balanced immune response.
Krishnan, A., S. K. Verma, P. Mani, R. Gupta, S. Kundu and D. P. Sarkar. 2009. A histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusion. J Virol 83:1727-1741.
Alone, V, P., G. Malik, A. Krishnan and L.C. Garg. 2007. Deletion mutations in N-terminal a1 helix render heat labile enterotoxin S subunit susceptible to degradation. Proc. Natl. Acad Sci 104 (41): 16056-16061.
Verma, S. K, P. Mani, N. R. Sharma, A. Krishnan, V. K. Valluripalli, S. Bathular, Reddy, A. Chaudhuri, R. P. Roy, and D. P. Sarkar. 2005. Histidylated Lipid-modified Sendai Viral Envelopes Mediate Enhanced Membrane Fusion and Potentiate Targeted Gene Delivery.J Biol Chem 280: 35399-35409. Patra, K. A., R. Mukhopadhyay, R. Mukhija, A. Krishnan, L. C. Garg and A. K. Panda. 2000.
Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone
from Escherichia coli. Protein Expression and Purification 18, 182-192.
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