Home Index

AU-KBC RESEARCH CENTRE

Dr. Sulagna Banerjee

 

 

 

 

Education

 

Doctor of Philosophy (Ph.D.) 2004

Bose Institute / Jadavpur University , Kolkata  

 

Research Interests

 

Molecular parasitology, Glycobiology,

Host-parasite interaction

 

Research Area

 

             Protozoan parasites are the single largest cause of infection disease and death in both human and animals. These organisms are responsible for diseases like dysentery (Entamoeba), diarrohoea (Giardia), vaginal infection (Trichomonas) and life threatning infections like Malaria (Plasmodium) which are so prevalent in the South East Asian part of the world. Along with humans, protozoan parasites like Cryptosporidium are pathogenic to cattle thereby jeopardizing the dairy industry to a great extent in this part of the world. My research aims at understanding the biology of infection by these parasites.

 

Glycobiology in the infection process: There has been considerable study on these pathogens with respect to their basic biology and drug resistance, but limited research has been pursued in elucidating the mechanism of host-pathogen interaction. The fundamental basis of interaction of the host (the mammalian gastrointestinal tract or the urogenital region) and the pathogen occurs through recognition of pathogen surface by the host cells and vice versa. The host cell surface is richly decorated with mucin, a glycoprotein with an elaborate glycan moiety. The pathogen cell surface on the other hand has a wide range of glycoconjugates (glycoproteins and glycolipids) as well as a set of carbohydrate binding proteins (lectins) which help it to adhere to the host surface. My area of study aims at this glycan dependent host cell adhesion by the pathogen which lays down the basics of infection by these parasites

 

Gene regulation in the infection process: S/MARs (scaffold or matrix attached regions) are elements of the DNA that attach the chromatin fiber to the proteinaceous network of the nucleus, the nuclear matrix or scaffold. Thereby they subdivide the eukaryotic genome into structural and functional domains. They are found at the base of the chromatin loops into which the eukaryotic genome appears to be organized. S/MAR elements have been reported in Entamoeba histolytica but they have not been identified from any other protozoa. Studying S/MAR elements and elucidating their role in gene regulation in the protozoan parasites is another area of interest which can shed a light in the infection process by these parasites. 

 

Publications

 

Banerjee S, Cui J, Robbins P and Samuelson J.Use of Giardia, which appears to have a single nucleotide-sugar transporter for UDP-GlcNAc, to identify the UDP-Glc transporter of Entamoeba. Mol Biochem Parasitol. 2008

 

Banerjee, S , Vishwanath,P , Robbins, P, Samuelson, J. The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation. Proc Natl Acad Sci U S A. 2007 July 10;104 (28):11676-11681 .

 

Kelleher DJ, Banerjee S, Cura AJ, Samuelson J, Gilmore R. Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist organisms. J Cell Biol. 2007 Apr 9;177(1):29-37.

 

Samuelson J, Banerjee S, Magnelli P, Cui J, Kelleher DJ, Gilmore R, Robbins PW. (2005)The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases. Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1548-53.

 

Banerjee S, Fisher O, Lohia A, Ankri S (2005) Entamoeba histolytica DNA methyltransferase (Ehmeth) is a nuclear matrix protein that binds EhMRS2, a DNA that includes a scaffold/matrix attachment region (S/MAR).Mol Biochem Parasitol. 139(1):91-7.

 

Banerjee, S. and A. Lohia, 2003. Molecular analysis of repetitive DNA elements from Entamoeba histolytica, which encode small RNAs and contain matrix/scaffold attachment recognition sequences.Mol Biochem Parasitol 126(1): 35-42.

 

Banerjee S, Das S and Lohia A., 2002 Eukaryotic Checkpoints are absent in the cell division cycle of Entamoeba. Journal of Biosciences V.27 No.6567-572 

 

 

Positions open 

 

MS, PhD, Post Doc.