The antiviral lectin cyanovirin-N: probing multivalency and glycan recognition through experimental and computational approaches.
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.
*Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, U.S.A.
Brian W
BW
Woodrum
Jason D
JD
Maxwell
Ashini
A
Bolia
S Banu
SB
Ozkan
Giovanna
G
Ghirlanda
D000595:Amino Acid Sequence; D019380:Anti-HIV Agents / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000627:therapeutic use*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000627:therapeutic use*; D000458:Cyanobacteria / Q000737:chemistry; D006678:HIV / Q000737:chemistry / Q000235:genetics; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000378:metabolism; D015658:HIV Infections / Q000188:drug therapy*; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
D019380:Anti-HIV Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D015699:HIV Envelope Protein gp120; D037102:Lectins; D011134:Polysaccharides; C107733:cyanovirin N