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Your search keyword '"Shridhar, Surekha"' showing total 13 results
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13 results on '"Shridhar, Surekha"'

7. Development of a broad spectrum glycoconjugate vaccine to prevent wound and disseminated infections with Klebsiella pneumoniae and Pseudomonas aeruginosa

Author

Hegerle, Nicolas, primary, Choi, Myeongjin, additional, Sinclair, James, additional, Amin, Mohammed N., additional, Ollivault-Shiflett, Morgane, additional, Curtis, Brittany, additional, Laufer, Rachel S., additional, Shridhar, Surekha, additional, Brammer, Jerod, additional, Toapanta, Franklin R., additional, Holder, Ian Alan, additional, Pasetti, Marcela F., additional, Lees, Andrew, additional, Tennant, Sharon M., additional, Cross, Alan S., additional, and Simon, Raphael, additional

Published
2018
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8. Development of a glycoconjugate vaccine to prevent invasive Salmonella Typhimurium infections in sub-Saharan Africa

Author

Baliban, Scott M., primary, Yang, Mingjun, additional, Ramachandran, Girish, additional, Curtis, Brittany, additional, Shridhar, Surekha, additional, Laufer, Rachel S., additional, Wang, Jin Y., additional, Van Druff, John, additional, Higginson, Ellen E., additional, Hegerle, Nicolas, additional, Varney, Kristen M., additional, Galen, James E., additional, Tennant, Sharon M., additional, Lees, Andrew, additional, MacKerell, Alexander D., additional, Levine, Myron M., additional, and Simon, Raphael, additional

Published
2017
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9. Galectin CvGal2 from the Eastern Oyster (Crassostrea virginica) Displays Unique Specificity for ABH Blood Group Oligosaccharides and Differentially Recognizes Sympatric Perkinsus Species

Author

Feng, Chiguang, primary, Ghosh, Anita, additional, Amin, Mohammed N., additional, Bachvaroff, Tsvetan R., additional, Tasumi, Satoshi, additional, Pasek, Marta, additional, Banerjee, Aditi, additional, Shridhar, Surekha, additional, Wang, Lai-Xi, additional, Bianchet, Mario A., additional, and Vasta, Gerardo R., additional

Published
2015
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13. The Galectin CvGal1 from the Eastern Oyster (Crassostrea virginica) Binds to Blood Group A Oligosaccharides on the Hemocyte Surface.

Author

Chiguang Feng, Ghosh, Anita, Amin, Mohammed N., Giomarelli, Barbara, Shridhar, Surekha, Banerjee, Aditi, Fernández-Robledo, José A., Bianchet, Mario A., Lai-Xi Wang, Wilson, Iain B. H., and Vasta, Gerardo R.

Subjects
*OYSTERS, *LIGANDS (Biochemistry), *GLYCOPROTEINS, *AMERICAN oyster, *BLOOD
Abstract

The galectin CvGal1 from the eastern oyster (Crassostrea virginica), which possesses four tandemly arrayed carbohydrate recognition domains, was previously shown to display stronger binding to galactosamine and N-acetylgalactosamine relative to D-galactose. CvGal1 expressed by phagocytic cells is "hijacked" by the parasite Perkinsus marinus to enter the host, where it proliferates and causes systemic infection and death. In this study, a detailed glycan array analysis revealed that CvGal1 preferentially recognizes type 2 blood group A oligosaccharides. Homology modeling of the protein and its oligosaccharide ligands supported this preference over type 1 blood group A and B oligosaccharides. The CvGal ligand models were further validated by binding, inhibition, and competitive binding studies of CvGal1 and ABH-specific monoclonal antibodies with intact and deglycosylated glycoproteins, hemocyte extracts, and intact hemocytes and by surface plasmon resonance analysis. A parallel glycomic study carried out on oyster hemocytes (Kurz, S., Jin, C., Hykollari, A., Gregorich, D., Giomarelli, B., Vasta, G. R., Wilson, I. B. H., and Paschinger, K. (2013)J. Biol. Chem. 288, ) determined the structures of oligosaccharides recognized by CvGal1. Proteomic analysis of the hemocyte glycoproteins identified β-integrin and dominin as CvGal1 "self"-ligands. Despite strong CvGal1 binding to P. marinus trophozoites, no binding of ABH blood group antibodies was observed. Thus, parasite glycans structurally distinct from the blood group A oligosaccharides on the hemocyte surface may function as potentially effective ligands for CvGal1. We hypothesize that carbohydrate-based mimicry resulting from the host/parasite co-evolution facilitates CvGal1-mediated cross-linking to β-integrin, located on the hemocyte surface, leading to cell activation, phagocytosis, and host infection. [ABSTRACT FROM AUTHOR]

Published
2013
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