Publication: N-linked glycosylation in C2 region of HIV-1 envelope reduces sensitivity to neutralizing antibodies
Issued Date
2005-08-17
Resource Type
ISSN
08828245
Other identifier(s)
2-s2.0-23344435219
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Viral Immunology. Vol.18, No.2 (2005), 343-353
Suggested Citation
Sirilak Teeraputon, Suda Louisirirojchanakul, Prasert Auewarakul N-linked glycosylation in C2 region of HIV-1 envelope reduces sensitivity to neutralizing antibodies. Viral Immunology. Vol.18, No.2 (2005), 343-353. doi:10.1089/vim.2005.18.343 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/16304
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
N-linked glycosylation in C2 region of HIV-1 envelope reduces sensitivity to neutralizing antibodies
Other Contributor(s)
Abstract
N-linked glycosylation at specific sites on human immunodeficiency virus (HIV)-1 gp120 envelope glycoprotein is believed to act as a glycan shield to protect the viral neutralizing epitopes. Various glycosylation sites have been shown to affect the sensitivity to antibody-mediated neutralization. These include sites on V1V2, C2, base of V3, V5 and C5. Among these, the sites around the base of V3 loop have been most consistently found to associate with neutralization sensitivity in subtype B viruses. In contrast, we found that N-linked glycosylation sites at the junction of V2-C2 and in the middle of C2 were responsible for the neutralization resistance in CRF01_A/E, whereas sites at the base of V3 loop and in V1 and V5 did not affect the neutralization phenotype. © Mary Ann Liebert, Inc.