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J Korean Med Sci. 2014 Mar;29(3):456-9. doi: 10.3346/jkms.2014.29.3.456. Epub 2014 Feb 27.

Characterization of Gp41 polymorphisms in the fusion peptide domain and T-20 (Enfuvirtide) resistance-associated regions in Korean HIV-1 isolates.

Author information

  • 1Division of AIDS, Korea National Institute of Health, Cheongwon, Korea. ; School of Life Sciences and Biotechnology, Korea University, Seoul, Korea.
  • 2Division of AIDS, Korea National Institute of Health, Cheongwon, Korea.
  • 3School of Life Sciences and Biotechnology, Korea University, Seoul, Korea.

Abstract

HIV-1 gp41 is an envelope protein that plays an essential role in virus entry. The mutation of gp41 affects HIV-1 entry and susceptibility to the fusion inhibitor T-20. Therefore, we analyzed the natural polymorphism of gp41 of 163 HIV-1 isolates from T-20-naïve Koreans infected with HIV-1. This study of gp41 polymorphisms showed that insertions in the fourth threonine (74.8%) and L7M substitutions (85.3%) were more frequent in the fusion peptide motif in Korean HIV-1 isolates compared with those from other countries. Minor T-20 resistance mutations such as L45M (1.2%), N126K (1.2%), and E137K (6.7%) were detected, but the critical T-20 resistance mutations were not detected in the gp41 HR1 and HR2 regions. In addition, the N42S mutation (12.9%) associated with T-20 hypersusceptibility was detected at a high frequency. These results may serve as useful data for studies considering T-20 for use in the development of a more effective anti-retroviral treatment in Korea.

KEYWORDS:

Fusion Inhibitor; Fusion Peptide; Gp41 Polymorphism; HIV-1 Envelope Glycoprotein; T-20 Resistance Mutation

PMID:
24616600
[PubMed - indexed for MEDLINE]
PMCID:
PMC3945146
Free PMC Article
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