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Heterogeneity of Envelope Molecules Shown by Different Sensitivities to Anti‐V3 Neutralizing Antibody and CXCR4 Antagonist Regulates the Formation of Multiple‐Site Binding of HIV‐1
Author(s) -
Harada Shinji,
Yusa Keisuke,
Maeda Yosuke
Publication year - 2004
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2004.tb03517.x
Subject(s) - infectivity , biology , virology , neutralization , antibody , virus , neutralizing antibody , cxcr4 , viral envelope , receptor , peptide , binding site , human immunodeficiency virus (hiv) , lentivirus , immunology , viral disease , chemokine , biochemistry
Abstract Increased temperature enhances the infectivity of human immunodeficiency virus type 1 (HIV‐1), and this enhancement is inhibited by anti‐CXCR4 peptide T140, implying that multiple‐site binding is required to proceed to infection. Here, we tested whether the augmented infectivity induced by increased temperature could account for the heterogeneity of envelope molecules in the effectiveness of anti‐V3 neutralization and anti‐CXCR4 blocking. Pseudoviruses with the X4 envelope which were infectious at room temperature (RT) were more resistant to both anti‐V3 neutralizing antibody 0.5β and T140 than viruses infectious at 37 C and 40 C. Viruses infectious to cells treated with T140 were also resistant to 0.5β. Based on the hypothesis that the HIV‐1 viruses were carrying heterogeneity of functional and nonfunctional gp120 and required the formation of sufficient multiple‐site binding of functional gp120 with receptors to proceed to infection, viruses with many functional gp120 which were infectious at RT and infectious to cells with reduced numbers of CXCR4 by T140 treatment were resistant to 0.5β. Although viruses with many functional gp120 are a minority (less than 5%) of the infectious HIV‐1 fraction, they are regarded as able to escape from neutralizing antibodies and coreceptor antagonists.