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Modulation of HIV and SIV neutralization sensitivity by DC-SIGN and mannose-binding lectin

  1. Author:
    Marzi, A.
    Mitchell, D. A.
    Chaipan, C.
    Fisch, T.
    Doms, R. W.
    Carrington, M.
    Desrosiers, R. C.
    Pohlmann, S.
  2. Author Address

    Hannover Med Sch, Inst Virol, D-30625 Hannover, Germany. Univ Hosp Erlangen, Inst Clin & Mol Virol, D-91054 Erlangen, Germany. Univ Erlangen Nurnberg, Nikolaus Fiebiger Ctr Mol Med, D-91054 Erlangen, Germany. Warwick Med Sch, Clin Sci Res Inst, Coventry CV2 2DX, W Midlands, England. Univ Penn, Dept Microbiol, Philadelphia, PA 19104 USA. SAIC Frederick Inc, NCI, Lab Genom Divers, Ft Detrick, MD 21702 USA. Harvard Univ, Sch Med, New England Reg Primate Res Ctr, Southborough, MA 01772 USA.;Pohlmann, S, Hannover Med Sch, Inst Virol, OE 5230,Carl Neuberg Str 1, D-30625 Hannover, Germany.;poehlmann.stefan@mh-harinover.de
    1. Year: 2007
    2. Date: Nov
  1. Journal: Virology
    1. 368
    2. 2
    3. Pages: 322-330
  2. Type of Article: Article
  3. ISSN: 0042-6822
  1. Abstract:

    The C-type lectin DC-SIGN binds to oligosaccharides on the human and simian immunodeficiency virus (HIV, SIV) envelope glycoproteins and promotes infection of susceptible cells. Here, we show that DC-SIGN recognizes glycans involved in SIV sensitivity to neutralizing antibodies and that binding to DC-SIGN confers neutralization resistance to an otherwise sensitive SIV variant. Moreover, we provide evidence that mannosebinding lectin (MBL) can interfere with HIV-1 neutralization by the carbohydrate-specific antibody 2GI2. (c) 2007 Elsevier Inc. All rights reserved.

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External Sources

  1. DOI: 10.1016/j.virol.2007.07.004
  2. WOS: 000250891400012

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