Interaction between HIV type 1 glycoprotein 120 and CXCR4 coreceptor involves a highly conserved arginine residue in hypervariable region 3
Journal
AIDS Research and Human Retroviruses
Journal Volume
16
Journal Issue
17
Pages
1821-1829
Date Issued
2000
Author(s)
Abstract
Several seven-transmembrane chemokine receptors are known to function as entry coreceptors for human immunodeficiency virus type 1. CCR5 and CXCR4 are the major coreceptors for non-syncytium-inducing (NSI) and syncytium-inducing (SI) viruses, respectively. During the natural course of infection, the emergence of variants with a phenotypic transition from NSI to SI and rapid disease progression is associated with expanded coreceptor usage to CXCR4. Characteristic amino acids at several positions in the hypervariable region 3 (V3) of gp120 have been linked to CXCR4 utilization. Previously, we reported that a highly conserved arginine residue of V3 played an important role in CCR5 utilization. In this study, the possible involvement of the same arginine residue in CXCR4 utilization was investigated. Amino acid substitutions introduced to this arginine on R5X4 viruses were found to have a significant effect on their utilization of CXCR4. These results, taken together with those reported previously, suggest that this highly conserved arginine may contribute to the functional convergence of chemokine coreceptor utilization by human immunodeficiency viruses and may represent a unique target for future antiviral design.
SDGs
Other Subjects
chemokine receptor CXCR4; glycoprotein gp 120; amino acid sequence; amino acid substitution; article; human; human cell; Human immunodeficiency virus 1; Human immunodeficiency virus infection; nonhuman; priority journal; protein analysis; protein structure; virus infectivity; Amino Acid Sequence; Amino Acid Substitution; Arginine; Cell Line; Complementarity Determining Regions; HIV Envelope Protein gp120; HIV-1; Humans; Molecular Sequence Data; Peptide Fragments; Receptors, CXCR4
Type
journal article