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Residue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.

Abstract：

:Alphavirus envelope proteins, organized as trimers of E2-E1 heterodimers on the surface of the pathogenic alphavirus, mediate the low pH-triggered fusion of viral and endosomal membranes in human cells. The lack of specific treatment for alphaviral infections motivates our exploration of potential antiviral approaches by inhibiting one or more fusion steps in the common endocytic viral entry pathway. In this work, we performed constant pH molecular dynamics based on an atomic model of the alphavirus envelope with icosahedral symmetry. We have identified pH-sensitive residues that cause the largest shifts in thermodynamic driving forces under neutral and acidic pH conditions for various fusion steps. A series of conserved interdomain His residues is identified to be responsible for the pH-dependent conformational changes in the fusion process, and ligand binding sites in their vicinity are anticipated to be potential drug targets aimed at inhibiting viral infections.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Zeng X,Mukhopadhyay S,Brooks CL 3rd

doi

10.1073/pnas.1414190112

subject

Has Abstract

pub_date

2015-02-17 00:00:00

pages

2034-9

issue

7

eissn

0027-8424

issn

1091-6490

pii

1414190112

journal_volume

112

pub_type

杂志文章

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