HIV-1 and microvesicles from T-cells share a common glycome, arguing for a common origin

HIV-1 is a master at deceiving the immune system, usurping host biosynthetic machinery. Although HIV-1 is coated with host-derived glycoproteins only glycosylation of viral gp120 has been described. Herein we utilize lectin microarray technology to analyze the glycome of intact HIV-1 virions. We show that the glycan coat of human T-cell line-derived HIV-1 matches that of native immunomodulatory microvesicles. The carbohydrate composition of both virus and microvesicles is cell-line dependent, suggesting a mechanism to rapidly camouflage the virus within the host. In addition, binding of both virus and microvesicles to antiviral lectins is enriched over the host cell, raising concern about targeting these glycans for therapeutics. This work also sheds light on the binding of HIV-1 to galectin-1, an important human immune lectin. Overall, our work strongly supports the theory that HIV-1 co-opts the exocytic pathway of microvesicles, potentially explaining why eliciting a protective antiviral immune response is difficult.