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Inhibitory role of CXCR4 glycan in CD4-independent X4-tropic human immunodeficiency virus type 1 infection and its abrogation in CD4-dependent infection

¹ Department of AIDS Research, Institute of Tropical Medicine, Nagasaki University, Nagasaki, Japan
² Laboratory of Viral Genomics, Center for Pathogen Genomics, National Institute of Infectious Diseases, Tokyo, Japan
³ Department of Immunology, Graduate School and Faculty of Medicine, University of the Ryukyus, Okinawa, Japan
⁴ AIDS Research Center, National Institute of Infectious Diseases, Tokyo, Japan
⁵ Department of Molecular Virology, Tokyo Medical and Dental University, Tokyo, Japan

Correspondence
Yoshinao Kubo
yoshinao{at}net.nagasaki-u.ac.jp

CXCR4 functions as an infection receptor of X4 human immunodeficiency virus type 1 (HIV-1) . CXCR4 is glycosylated at the N-terminal extracellular region, which is important for viral envelope (Env) protein binding. We compared the effects of CXCR4 glycan on the CD4-dependent and –independent infections in human cells by X4 viruses. We found that transduction mediated by Env proteins of CD4-independent HIV-1 strains increased up to 5.5-fold in cells expressing unglycosylated CXCR4, suggesting that the CXCR4 glycan inhibits CD4-independent X4 virus infection. Co-expression of CD4 on the target cell surface or pre-incubation of virus particles with soluble CD4 abrogates the glycan-mediated inhibition of X4 virus infection, suggesting that interaction of Env protein with CD4 counteracts the inhibition. These findings indicate that it will be advantageous for X4 HIV-1 to remain CD4-dependent. A structural model that explains the glycan-mediated inhibition is discussed.

Supplementary material is available with the online version of this paper.