The antiretroviral lectin cyanovirin-N targets well-known and novel targets on the surface of Entamoeba histolytica trophozoites

Andrea Carpentieri, Daniel M. Ratner, Sudip K. Ghosh, Sulagna Banerjee, G. Guy Bushkin, Jike Cui, Michael Lubrano, Martin Steffen, Catherine E. Costello, Barry O'Keefe, Phillips W. Robbins, John Samuelson

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 (Man5GlcNAc2). Here, we show that glycoproteins with unmodified N-glycans are aggregated and capped on the surface of E. histolytica trophozoites by the antiret- roviral 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.

Original languageEnglish (US)
Pages (from-to)1661-1668
Number of pages8
JournalEukaryotic Cell
Volume9
Issue number11
DOIs
StatePublished - Nov 1 2010
Externally publishedYes

Fingerprint

Trophozoites
Entamoeba histolytica
Lectins
Polysaccharides
Glycoproteins
Concanavalin A
Plant Lectins
Amoebic Dysentery
Amoebic Liver Abscess
Mucins
Phagocytosis
Virulence
Membrane Proteins
Proteins
Peptide Hydrolases
Vaccines
Monoclonal Antibodies
cyanovirin N

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

The antiretroviral lectin cyanovirin-N targets well-known and novel targets on the surface of Entamoeba histolytica trophozoites. / Carpentieri, Andrea; Ratner, Daniel M.; Ghosh, Sudip K.; Banerjee, Sulagna; Bushkin, G. Guy; Cui, Jike; Lubrano, Michael; Steffen, Martin; Costello, Catherine E.; O'Keefe, Barry; Robbins, Phillips W.; Samuelson, John.

In: Eukaryotic Cell, Vol. 9, No. 11, 01.11.2010, p. 1661-1668.

Research output: Contribution to journalArticle

Carpentieri, A, Ratner, DM, Ghosh, SK, Banerjee, S, Bushkin, GG, Cui, J, Lubrano, M, Steffen, M, Costello, CE, O'Keefe, B, Robbins, PW & Samuelson, J 2010, 'The antiretroviral lectin cyanovirin-N targets well-known and novel targets on the surface of Entamoeba histolytica trophozoites', Eukaryotic Cell, vol. 9, no. 11, pp. 1661-1668. https://doi.org/10.1128/EC.00166-10
Carpentieri, Andrea ; Ratner, Daniel M. ; Ghosh, Sudip K. ; Banerjee, Sulagna ; Bushkin, G. Guy ; Cui, Jike ; Lubrano, Michael ; Steffen, Martin ; Costello, Catherine E. ; O'Keefe, Barry ; Robbins, Phillips W. ; Samuelson, John. / The antiretroviral lectin cyanovirin-N targets well-known and novel targets on the surface of Entamoeba histolytica trophozoites. In: Eukaryotic Cell. 2010 ; Vol. 9, No. 11. pp. 1661-1668.
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