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

Autor: Graham Simmons, George Lin, Frédéric Baribaud, Drew Weissman, Stefan Pöhlmann, Paul Bates, Beth S. Haggarty, George J. Leslie, James A. Hoxie, Houping Ni, Robert W. Doms
Rok vydání: 2003
Předmět:
Zdroj: Journal of Virology. 77:1337-1346
ISSN: 1098-5514
0022-538X
DOI: 10.1128/jvi.77.2.1337-1346.2003
Popis: 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 N -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 N -glycans will efficiently interact with DC-SIGN(R), whereas those with solely complex N -glycans will not. Thus, the virus-producing cell type is an important factor in dictating both N -glycan status and virus interactions with DC-SIGN(R), which may impact virus tropism and transmissibility in vivo.
Databáze: OpenAIRE