HIV-1 Envelope Glycan Composition as a Key Determinant of Efficient Virus Transmission via DC-SIGN and Resistance to Inhibitory Lectins—Jan 2019

Carbohydrate-recognizing lectins interact with HIV-1 envelope (Env) oligomannose-, hybrid-, and complex-type glycans. This study studied the role of glycan heterogeneity in HIV-1 trans-infection by the host mannose-binding lectin DC-SIGN. HIV-1 strains differed in glycan content and trans-infection via DC-SIGN and antiviral lectin sensitivity. DC-SIGN-mediated virus capture increased when Env glycans displayed only the oligomannose type, but degradation decreased virus trans-infection, which was mitigated by integration with hybrid-type glycans. Env signal peptide (SP) amino acid modifications altered Env glycan content, affecting DC-SIGN-dependent trans-infection and virus sensitivity to antiviral lectins. Thus, SP variation and glycosylation that give HIV-1 Env different oligosaccharides determine virus fitness and phenotypic variety.

Jan, M., Upadhyay, C., & Hioe, C. E. (2019). HIV-1 Envelope Glycan Composition as a Key Determinant of Efficient Virus Transmission via DC-SIGN and Resistance to Inhibitory Lectins. iScience, 21, 413–427. https://doi.org/10.1016/j.isci.2019.10.030

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Functional Antibody Response Against V1V2 and V3 of HIV gp120 in the VAX003 and VAX004 Vaccine Trials—Balasubramanian 2018

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Heterogeneity in glycan composition on the surface of HIV-1 envelope determines virus sensitivity to lectins—JAN 2018