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Full-Text Articles in Medicine and Health Sciences
Dmbt1 Inhibition Of Pseudomonas Aeruginosa Twitching Motility Involves Its N-Glycosylation And Cannot Be Conferred By The Scavenger Receptor Cysteine-Rich Bacteria-Binding Peptide Domain., Jianfang Li, Stephanie J Wan, Matteo M E Metruccio, Sophia Ma, Kamran Nazmi, Floris J Bikker, David J. Evans, Suzanne M J Fleiszig
Dmbt1 Inhibition Of Pseudomonas Aeruginosa Twitching Motility Involves Its N-Glycosylation And Cannot Be Conferred By The Scavenger Receptor Cysteine-Rich Bacteria-Binding Peptide Domain., Jianfang Li, Stephanie J Wan, Matteo M E Metruccio, Sophia Ma, Kamran Nazmi, Floris J Bikker, David J. Evans, Suzanne M J Fleiszig
Faculty Publications & Research of the TUC College of Pharmacy
The scavenging capacity of glycoprotein DMBT1 helps defend mucosal epithelia against microbes. DMBT1 binding to multiple bacterial species involves its conserved Scavenger Receptor Cysteine-Rich (SRCR) domains, localized to a 16-mer consensus sequence peptide, SRCRP2. Previously, we showed that DMBT1 bound Pseudomonas aeruginosa pili, and inhibited twitching motility, a pilus-mediated movement important for virulence. Here, we determined molecular characteristics required for twitching motility inhibition. Heat-denatured DMBT1 lost capacity to inhibit twitching motility and showed reduced pili binding (~40%). Size-exclusion chromatography of Lys-C-digested native DMBT1 showed that only high-Mw fractions retained activity, suggesting involvement of the N-terminal containing repeated SRCR domains with …