作者: H. V. Nielsen , A. L. Flores-Mireles , A. L. Kau , K. A. Kline , J. S. Pinkner
DOI: 10.1128/JB.00451-13
关键词: Enterococcus faecalis 、 Fimbriae Proteins 、 Biochemistry 、 Sortase 、 Biofilm 、 Pilin 、 Fimbria 、 Pilus 、 Biology 、 Protein subunit
摘要: Enterococci commonly cause hospital-acquired infections, such as infective endocarditis and catheter-associated urinary tract infections. In animal models of these a long hairlike extracellular protein fiber known the endocarditis- biofilm-associated (Ebp) pilus is an important virulence factor for Enterococcus faecalis. For Ebp other sortase-assembled pili, pilus-associated sortases are essential formation they create covalent isopeptide bonds between sortase recognition motif pilin-like subunits. However, molecular requirements governing incorporation three subunits (EbpA, EbpB, EbpC) have not been investigated in E. Here, we show that Lys residue within EbpC subunit was necessary polymerization. EbpA into only required its (LPXTG), while EbpB motif. Only would be tip subunit, base require pilin Thus, data support model with at polymer. addition, housekeeping sortase, SrtA, found to process predicted catalytic Cys efficient cell wall anchoring mature pili. defined interactions involved polymerization, minor organization, subcellular compartmentalization faecalis system. These studies advance our understanding unique mechanisms biogenesis.