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Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions.

Abstract：

:The entry of human immunodeficiency virus (HIV-1) into cells is initiated by binding of the gp120 exterior envelope glycoprotein to the receptor, CD4. How does CD4 binding trigger conformational changes in gp120 that allow the gp41 transmembrane envelope glycoprotein to mediate viral-cell membrane fusion? The transition from the unliganded to the CD4-bound state is regulated by two potentially flexible topological layers (layers 1 and 2) in the gp120 inner domain. Both layers apparently contribute to the noncovalent association of unliganded gp120 with gp41. After CD4 makes initial contact with the gp120 outer domain, layer 1-layer 2 interactions strengthen gp120-CD4 binding by reducing the off rate. Layer 1-layer 2 interactions also destabilize the activated state induced on HIV-1 by treatment with soluble CD4. Thus, despite lack of contact with CD4, the gp120 inner-domain layers govern CD4 triggering by participating in conformational transitions within gp120 and regulating the interaction with gp41.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Finzi A,Xiang SH,Pacheco B,Wang L,Haight J,Kassa A,Danek B,Pancera M,Kwong PD,Sodroski J

doi

10.1016/j.molcel.2010.02.012

subject

Has Abstract

pub_date

2010-03-12 00:00:00

pages

656-67

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(10)00154-1

journal_volume

37

pub_type

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