| Autor: |
Yuan W; Division of Infectious Diseases and International Health, Department of Medicine, University of Virginia, Charlottesville, Virginia 22908, USA. wy5e@virginia.edu, Li X, Kasterka M, Gorny MK, Zolla-Pazner S, Sodroski J |
| Jazyk: |
angličtina |
| Zdroj: |
AIDS research and human retroviruses [AIDS Res Hum Retroviruses] 2009 Mar; Vol. 25 (3), pp. 319-28. |
| DOI: |
10.1089/aid.2008.0213 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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