Recombinant production and characterization of the carbohydrate recognition domain from Atlantic salmon C-type lectin receptor C (SCLRC)

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TypeArticle
Journal titleProtein Expression and Purification
Volume59
Issue1
Pages3846; # of pages: 9
AbstractThe Atlantic salmon C-type lectin receptor C (SCLRC) locus encodes a potential oligomeric type II receptor. C-type lectins recognize carbohydrates in a Ca2+-dependent manner through structurally conserved, yet functionally diverse, C-type lectin-like domains (CTLDs). Many conserved amino acids in animal CTLDs are present in SCLRC, with the notable exception of an asparagine crucially involved in Ca2+- and carbohydrate-binding, which is tyrosine in SCLRC. SCLRC also contains six cysteines that form three disulfide bonds. Although SCLRC was originally identified as an up-regulated transcript responding to Aeromonas salmonicida infection, the biological role of this protein is still unknown. To study the structure and ligand binding properties of SCLRC, we created a homology model of the 17 kDa CTLD and produced it as an affinity-tagged protein in the periplasm of Escherichia coli by co-expression of proteins that facilitate disulfide bond formation. The recombinant form of SCLRC was characterized by a protease protection assay, a solid-phase carbohydrate-binding assay, and frontal affinity chromatography. On the basis of this characterization, we classify SCLRC as a C-type lectin that binds to mannose and its derivatives.
Publication date
PublisherElsevier
LanguageEnglish
AffiliationNRC Institute for Marine Biosciences; National Research Council Canada; Aquatic and Crop Resource Development
Peer reviewedYes
NRC number42761
1724
NPARC number3538214
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Record identifier2952f037-d05e-44bd-b32b-31add8ec70bd
Record created2009-03-01
Record modified2016-05-09
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