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Functional characterization of a subtilisin-like serine protease from .

J. Biol. Chem.. 2019; 
Howell Matthew,Dumitrescu Daniel G,Blankenship Lauren R,Herkert Darby,Hatzios Stavrou
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Monoclonal Antibody Services Membranes were blocked with 3% (w/v) dry milk in TBST prior to incubation with a mouse polyclonal anti-IvaP antibody (GenScript; 1:1000 –1: 2000 dilution) (9), a rabbit polyclonal anti-DDDDK antibody (Abcam ab1162; 1:5,000 dilution), a sheep polyclonal anti-hu- man intelectin-1 antibody (R&D Systems AF4254; 1:2,000 dilu- tion), or one of two mouse monoclonal anti-His antibodies (GenScript A00186 (15 ␮l per 10 ml of TBST) and Invitrogen MA1–21315 (1:1000 dilution)). Get A Quote

Abstract

, the causative agent of the human diarrheal disease cholera, exports numerous enzymes that facilitate its adaptation to both intestinal and aquatic niches. These secreted enzymes can mediate nutrient acquisition, biofilm assembly, and interactions with its host. We recently identified a secreted serine protease, IvaP, that is active in infected rabbits and human choleric stool. IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted end... More

Keywords

bacteria,cholera,host-pathogen interaction,intelectin,lectin,pathogenesis,serine protease,subtil