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

  1. Author:
    Krishnamoorthy, L.
    Bess, J. W.
    Preston, A. B.
    Nagashima, K.
    Mahal, L. K.

  2. Author Address

    Krishnamoorthy, Lakshmi, Preston, Alex B.; Mahal, Lara K.] Univ Texas Austin, Dept Chem & Biochem, Ctr Syst & Synthet Biol, Austin, TX 78712 USA. [Krishnamoorthy, Lakshmi, Preston, Alex B.; Mahal, Lara K.] Univ Texas Austin, Inst Cellular & Mol Biol, Austin, TX 78712 USA. [Bess, Julian W., Jr.] NCI, AIDS Vaccine Program, Frederick, MD USA. [Nagashima, Kunio] NCI, SAIC Frederick Inc, Image Anal Lab, Frederick, MD USA.
    1. Year: 2009
  2. Journal: Nature Chemical Biology
    1. 5
    2. 4
    3. Pages: 244-250
  4. Type of Article: Article
  1. Abstract:

    HIV-1 is a master at deceiving the immune system and usurping host biosynthetic machinery. Although HIV-1 is coated with host-derived glycoproteins, only glycosylation of viral gp120 has been described. Here we use 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, which suggests 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, thus potentially explaining why eliciting a protective antiviral immune response is difficult.

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External Sources

  1. PMID: 19234452

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