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

Brian W. Woodrum, Jason D. Maxwell, Ashini Bolia, S. Banu Ozkan, Giovanna Ghirlanda

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1170-1176
Number of pages7
JournalBiochemical Society Transactions
Volume41
Issue number5
DOIs
Publication statusPublished - Oct 2013

Fingerprint

Lectins
Antiviral Agents
Polysaccharides
Anti-HIV Agents
Mutagenesis
Cyanobacteria
Ligands
cyanovirin N
Proteins

Keywords

  • Antiviral lectin
  • Cyanovirin
  • Glycoprotein 120 (gp120)
  • Multivalency
  • Perturbation response scanning
  • Protein-glycan interaction

ASJC Scopus subject areas

  • Biochemistry

Cite this

The antiviral lectin cyanovirin-N : Probing multivalency and glycan recognition through experimental and computational approaches. / Woodrum, Brian W.; Maxwell, Jason D.; Bolia, Ashini; Banu Ozkan, S.; Ghirlanda, Giovanna.

In: Biochemical Society Transactions, Vol. 41, No. 5, 10.2013, p. 1170-1176.

Research output: Contribution to journalArticle

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