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 hyper-susceptibility 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.
Original language | English |
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Pages (from-to) | 456-459 |
Number of pages | 4 |
Journal | Journal of Korean medical science |
Volume | 29 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2014 |
Keywords
- Fusion inhibitor
- Fusion peptide
- Gp41 polymorphism
- HIV-1 envelope glycoprotein
- T-20 resistance mutation
ASJC Scopus subject areas
- Medicine(all)