Published in Medical Letter on the CDC and FDA, March 12th, 2006
"HIV-1 Gag protein interaction with cyclophilin A (CypA) is critical for viral fitness. Among the amino acid substitutions identified in Gag noncleavage sites in HIV-1 variants resistant to protease inhibitors, H219Q (Gatanaga, H. et al., (2002) J. Biol. Chem. 277, 5952-5961) and H219P substitutions in the viral CypA binding loop confer the greatest replication advantage to HIV-1. These substitutions represent polymorphic amino acid residues," scientists writing in the Journal of Biological Chemistry report.
Want to see the full article?
Welcome to NewsRx!
Learn more about a six-week, no-risk free trial of Medical Letter on the CDC and FDA
NewsRx also is available at LexisNexis, Gale, ProQuest, Factiva, Dialog, Thomson Reuters, NewsEdge, and Dow Jones.