Differential N-Linked Glycosylation of Human Immunodeficiency Virus and Ebola Virus Envelope Glycoproteins Modulates Interactions with DC-SIGN and DC-SIGNR

説明

<jats:title>ABSTRACT</jats:title> <jats:p> The C-type lectins DC-SIGN and DC-SIGNR [collectively referred to as DC-SIGN(R)] bind and transmit human immunodeficiency virus (HIV) and simian immunodeficiency virus to T cells via the viral envelope glycoprotein (Env). Other viruses containing heavily glycosylated glycoproteins (GPs) fail to interact with DC-SIGN(R), suggesting some degree of specificity in this interaction. We show here that DC-SIGN(R) selectively interact with HIV Env and Ebola virus GPs containing more high-mannose than complex carbohydrate structures. Modulation of <jats:italic>N</jats:italic> -glycans on Env or GP through production of viruses in different primary cells or in the presence of the mannosidase I inhibitor deoxymannojirimycin dramatically affected DC-SIGN(R) infectivity enhancement. Further, murine leukemia virus, which typically does not interact efficiently with DC-SIGN(R), could do so when produced in the presence of deoxymannojirimycin. We predict that other viruses containing GPs with a large proportion of high-mannose <jats:italic>N</jats:italic> -glycans will efficiently interact with DC-SIGN(R), whereas those with solely complex <jats:italic>N</jats:italic> -glycans will not. Thus, the virus-producing cell type is an important factor in dictating both <jats:italic>N</jats:italic> -glycan status and virus interactions with DC-SIGN(R), which may impact virus tropism and transmissibility in vivo. </jats:p>

収録刊行物

  • Journal of Virology

    Journal of Virology 77 (2), 1337-1346, 2003-01-15

    American Society for Microbiology

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