Regulation of a novel adhesin Csp1 in Clostridium difficile

• Main Authors: Tung-ShengLin, 林東昇
• Other Authors: I-Hsiu Huang
• Format: Others
• Language: en_US
• Published: 2015
• Online Access: http://ndltd.ncl.edu.tw/handle/24xnw4

碩士 === 國立成功大學 === 微生物及免疫學研究所 === 103 === Clostridium difficile is a Gram positive, spore forming obligate anaerobic bacteria, causive agent of the antibiotic associated diarrhea. C. difficile infection (CDI) is caused by host microflora disruption through broad-spectrum antibiotics. The emergence of hypervirulent C. difficile strains resulting in high morbidity and mortality has occurred in many countries. The C. difficile secrets toxins TcdA, TcdB and binary toxin CDT. TcdA and TcdB are responsible for gastrointestinal inflammation, epithelial cell tight junction lose and apoptosis. Before infection, the pathogens need to attach to the host cell first. In C. difficile, surface protein are responsible for interaction with host cell and extracellular matrix of vertebrates. Csp1, a potential cell wall protein anchored on cell wall by sortase, and a putative collagen binding adhesin. Zmp1, a metalloprotease which can cleave Csp1 in vitro. c-di-GMP, a second messenger molecules modulate C. difficile motility, biofilm and toxin. In our study, we focus on Csp1 regulation between Zmp1 and c-di-GMP. Our results showed that in the absence of metalloprotease, Csp1 localization is increased on the cell wall, c-di-GMP enhance the quantity of Csp1 , and the PPKTG motif is needed for recognization by sortase. In summary, our results demonstrated the localization and regulation of a novel adhesin Csp1 by Zmp1 and c-di-GMP.