1048 A NOVEL HUMAN MONOCLONAL ANTIBODY DIRECTED AGAINST THE E2 GLYCOPROTEIN OF HEPATITIS C VIRUS (HCV) PREVENTS INFECTION IN CHIMPANZEES

2009 ◽  
Vol 50 ◽  
pp. S381 ◽  
Author(s):  
B.M. Blair ◽  
T.J. Broering ◽  
G.J. Babcock ◽  
G. Szabo ◽  
R.W. Finberg ◽  
...  
2008 ◽  
Vol 82 (12) ◽  
pp. 6067-6072 ◽  
Author(s):  
Zhen-Yong Keck ◽  
Oakley Olson ◽  
Meital Gal-Tanamy ◽  
Jinming Xia ◽  
Arvind H. Patel ◽  
...  

ABSTRACT A challenge in hepatitis C virus (HCV) vaccine development is defining conserved protective epitopes. A cluster of these epitopes comprises an immunodominant domain on the E2 glycoprotein, designated domain B. CBH-2 is a neutralizing human monoclonal antibody to a domain B epitope that is highly conserved. Alanine scanning demonstrated that the epitope involves residues G523, G530, and D535 that are also contact residues for E2 binding to CD81, a coreceptor required for virus entry into cells. However, another residue, located at position 431 and thus at a considerable distance in the linear sequence of E2, also contributes to the CBH-2 epitope. A single amino acid substitution at this residue results in escape from CBH-2-mediated neutralization in a genotype 1a virus. These results highlight the challenges inherent in developing HCV vaccines and show that an effective vaccine must induce antibodies to both conserved and more invariant epitopes to minimize virus escape.


2007 ◽  
Vol 46 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Eithan Galun ◽  
Norah A. Terrault ◽  
Rachel Eren ◽  
Arie Zauberman ◽  
Ofer Nussbaum ◽  
...  

2011 ◽  
Vol 286 (51) ◽  
pp. 44218-44233 ◽  
Author(s):  
Yong Wang ◽  
Zhen-yong Keck ◽  
Anasuya Saha ◽  
Jinming Xia ◽  
Fraser Conrad ◽  
...  

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