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The Antiretroviral Lectin Cyanovirin-N Targets Well-Known and Novel Targets on the Surface of Entamoeba histolytica Trophozoites

  1. Author:
    Carpentieri, A.
    Ratner, D. M.
    Ghosh, S. K.
    Banerjee, S.
    Bushkin, G. G.
    Cui, J. K.
    Lubrano, M.
    Steffen, M.
    Costello, C. E.
    O'Keefe, B.
    Robbins, P. W.
    Samuelson, J.

  2. Author Address

    [Carpentieri, Andrea; Ratner, Daniel M.; Ghosh, Sudip K.; Banerjee, Sulagna; Bushkin, G. Guy; Cui, Jike; Lubrano, Michael; Robbins, Phillips W.; Samuelson, John] Boston Univ, Dept Mol & Cell Biol, Goldman Sch Dent Med, Boston, MA 02118 USA. [Steffen, Martin] Boston Univ, Dept Pathol & Lab Med, Sch Med, Boston, MA 02118 USA. [Costello, Catherine E.] Boston Univ, Dept Biochem, Med Ctr, Boston, MA 02118 USA. [O'Keefe, Barry] NCI Frederick, Mol Targets Dev Program, Ctr Canc Res, Frederick, MD 21702 USA.;Samuelson, J, Boston Univ, Dept Mol & Cell Biol, Goldman Sch Dent Med, 72 E Concord St,Evans 425, Boston, MA 02118 USA.;jsamuels@bu.edu
    1. Year: 2010
    2. Date: Nov
  2. Journal: Eukaryotic Cell
    1. 9
    2. 11
    3. Pages: 1661-1668
  4. Type of Article: Article
  5. ISSN: 1535-9778
  1. Abstract:

    Entamoeba histolytica, the protist that causes amebic dysentery and liver abscess, has a truncated Asn-linked glycan (N-glycan) precursor composed of seven sugars (Man(5)GlcNAc(2)). Here, we show that glycoproteins with unmodified N-glycans are aggregated and capped on the surface of E. histolytica trophozoites by the antiretroviral lectin cyanovirin-N and then replenished from large intracellular pools. Cyanovirin-N cocaps the Gal/GalNAc adherence lectin, as well as glycoproteins containing O-phosphodiester-linked glycans recognized by an anti-proteophosphoglycan monoclonal antibody. Cyanovirin-N inhibits phagocytosis by E. histolytica trophozoites of mucin-coated beads, a surrogate assay for amebic virulence. For technical reasons, we used the plant lectin concanavalin A rather than cyanovirin-N to enrich secreted and membrane proteins for mass spectrometric identification. E. histolytica glycoproteins with occupied N-glycan sites include Gal/GalNAc lectins, proteases, and 17 previously hypothetical proteins. The latter glycoproteins, as well as 50 previously hypothetical proteins enriched by concanavalin A, may be vaccine targets as they are abundant and unique. In summary, the antiretroviral lectin cyanovirin-N binds to well-known and novel targets on the surface of E. histolytica that are rapidly replenished from large intracellular pools.

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External Sources

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  2. DOI: 10.1128/ec.00166-10
  3. View record in Web of Science®
  4. WOS: 000283727500002

Library Notes

  1. Fiscal Year: FY2010-2011
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