4.4 Article

The antiviral lectin cyanovirin-N: probing multivalency and glycan recognition through experimental and computational approaches

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 41, 期 -, 页码 1170-1176

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BST20130154

关键词

antiviral lectin; cyanovirin; glycoprotein 120 (gp120); multivalency; perturbation response scanning; protein-glycan interaction

资金

  1. National Science Foundation - Division of Molecular and Cellular Biosciences [1121276]
  2. Direct For Biological Sciences
  3. Div Of Molecular and Cellular Bioscience [1121276] Funding Source: National Science Foundation

向作者/读者索取更多资源

CVN (cyanovirin-N), a small lectin isolated from cyanobacteria, exemplifies a novel class of anti-HIV agents that act by binding to the highly glycosylated envelope protein gp120 (glycoprotein 120), resulting in inhibition of the crucial viral entry step. In the present review, we summarize recent work in our laboratory and others towards determining the crucial role of multivalency in the antiviral activity, and we discuss features that contribute to the high specificity and affinity for the glycan ligand observed in CVN. An integrated approach that encompasses structural determination, mutagenesis analysis and computational work holds particular promise to clarify aspects of the interactions between CVN and glycans.

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