Journal article

Role of Conserved Cysteine Residues in Hepatitis C Virus Glycoprotein E2 Folding and Function

Kathleen McCaffrey, Irene Boo, Kevin Tewierek, Mark L Edmunds, Pantelis Poumbourios, Heidi E Drummer

JOURNAL OF VIROLOGY | AMER SOC MICROBIOLOGY | Published : 2012

Abstract

Hepatitis C virus glycoprotein E2 contains 18 conserved cysteines predicted to form nine disulfide pairs. In this study, a comprehensive cysteine-alanine mutagenesis scan of all 18 cysteine residues was performed in E1E2-pseudotyped retroviruses (HCVpp) and recombinant E2 receptor-binding domain (E2 residues 384 to 661 [E2(661)]). All 18 cysteine residues were absolutely required for HCVpp entry competence. The phenotypes of individual cysteines and pairwise mutation of disulfides were largely the same for retrovirion-incorporated E2 and E2(661), suggesting their disulfide arrangements are similar. However, the contributions of each cysteine residue and the nine disulfides to E2 structure an..

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University of Melbourne Researchers

Grants

Awarded by NHMRC


Funding Acknowledgements

This work was supported by NHMRC project grants 543113, 603735, and 433913. H. E. D. was the recipient of an NHMRC R. D. Wright Biomedical Research Fellowship, and K. M. was the recipient of a Dora Lush Postgraduate Scholarship.