Oligomer-specific conformations of the Human Immunodeficiency Virus (HIV-1) gp41 envelope glycoprotein ectodomain recognized by human monoclonal antibodies

Wen Yuan, Xing Li, Marta Kasterka, Miroslaw K. Gorny, Susan Zolla-Pazner, Joseph Sodroski

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Trimerization of the human immunodeficiency virus (HIV-1) envelope glycoproteins is mediated by the ectodomain of the gp41 transmembrane glycoprotein. Here we investigate oligomer-specific conformations of gp41 by using monoclonal antibodies (MAbs) from HIV-1-infected humans. Human MAbs directed against the cluster I region of gp41 recognized trimeric, dimeric, and monomeric forms of soluble envelope glycoproteins; thus, the integrity of the cluster I epitopes is minimally affected by the oligomeric state. In contrast, human MAbs to the cluster II region were all oligomers specific. One cluster II MAb, 126-6, recognized exclusively the trimeric form of envelope glycoproteins, whereas the others recognized both trimeric and dimeric forms. Thus, a distinct trimer-specific conformation exists in the cluster II region of gp41. Analysis of soluble envelope glycoprotein mutants revealed that gp41 sequences immediately N-terminal to isoleucine 646 contribute to the formation of both the trimer and the trimer-specific conformational epitope.

Original languageEnglish
Pages (from-to)319-328
Number of pages10
JournalAIDS Research and Human Retroviruses
Volume25
Issue number3
DOIs
StatePublished - 1 Mar 2009
Externally publishedYes

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