Complete resonance assignments of bundlin (BfpA) from the bundle-forming pilus of enteropathogenic Escherichia coli.
Complete resonance assignments of bundlin (BfpA) from the bundle-forming pilus of enteropathogenic Escherichia coli.
复制标题
来自肠致病性大肠杆菌的束形成菌毛的束蛋白 (BfpA) 的完整共振分配。
DOI:
10.1023/b:jnmr.0000032511.89525.64
复制
发表时间:
2004
影响因子:
2.7
通讯作者:
Matthews,Stephen
中科院分区:
文献类型:
--
作者:
Ramboarina,Stéphanie;Fernandes,Paula;Simpson,Peter;Frankel,Gad;Donnenberg,Michael;Matthews,Stephen
Enteropathogenic Escherichia coli (EPEC) causes acute and persistent neonatal diarrhea in developing countries (reviewed in Frankel et al., 1998). The production of a type IVB fimbria in EPEC, known as the bundle-forming pilus (BFP), is required for the formation of large discrete EPEC microcolonies on the surface of epithelial cells–a phenotype characterized as localized adherence (LA)(Donnenberg et al., 1992). In addition, BFP is crucial for EPEC virulence, antigenicity and autoaggregation (Bieber et al., 1998). Bundlin, the product of the bfpA gene, is the pilin protein that constitutes the only known structural subunit of BFP filaments (Donnenberg et al., 1997, Blank et al., 2000). Pre-bundlin contains a hydrophilic leader sequence that is cleaved by a prepilin peptidase BfpP to produce the mature protein. The focus of this communication is the globular ‘head’domain of the bundlin that is encoded by the α1 allele (Blank et al., 2000).