Specificity analysis of the C-type lectin from rattlesnake venom, and its selectivity towards Gal- or GalNAc-terminated glycoproteins

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DOIResolve DOI: http://doi.org/10.1007/s10719-011-9342-5
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TypeArticle
Journal titleGlycoconjugate Journal
Volume28
Issue6
Pages427435; # of pages: 9
Subjectrattlesnake venom lectin; Crotalus atrox; C-type lectin; glycan array; lectin subsites; avidity
AbstractThe rattlesnake (Crotalus atrox) venom lectin is a readily-prepared decameric C-type lectin, specific for Gal and GalNAc. Glycan microarray analysis showed it reacted with a wide range of glycans, chiefly recognizing sets of compounds with Galβ1-4GlcNAc (LacNAc), α-Gal or α-GalNAc non-reducing termini. Its array profile was therefore distinctly different from those of four previously studied mammalian C-type lectins with the same Gal/GalNAc monosaccharide specificity, and it was more broadly reactive than several Gal- or GalNAc-specific plant lectins commonly used for glycan blotting. Though a general reactivity towards glycoproteins might be expected from the avidity conferred by its high valence, it showed a marked preference for glycoproteins with multiple glycans, terminated by Gal or GalNAc. Thus its ten closely-spaced sites each with a K(D) for GalNAc of ~2 mM appeared to make RSVL more selective than the four more widely-spaced sites of soybean agglutinin, with a ten-fold better K(D) for GalNAc.
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NPARC number19254212
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Record identifier714d6dfc-f3ef-4d97-bcae-c38bb52a6324
Record created2012-03-08
Record modified2016-05-09
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