Front Cover: Autotransporter Adhesins in Escherichia coli Pathogenesis
نویسندگان
چکیده
منابع مشابه
UpaG, a new member of the trimeric autotransporter family of adhesins in uropathogenic Escherichia coli.
The ability of Escherichia coli to colonize both intestinal and extraintestinal sites is driven by the presence of specific virulence factors, among which are the autotransporter (AT) proteins. Members of the trimeric AT adhesin family are important virulence factors for several gram-negative pathogens and mediate adherence to eukaryotic cells and extracellular matrix (ECM) proteins. In this st...
متن کاملDomain annotation of trimeric autotransporter adhesins—daTAA
MOTIVATION Trimeric autotransporter adhesins (TAAs), such as Yersinia YadA, Neisseria NadA, Moraxella UspAs, Haemophilus Hia and Bartonella BadA, are important pathogenicity factors of proteobacteria. Their high sequence diversity and distinct mosaic-like structure lead to difficulties in the annotation of their sequences. These stem from the large number of short repeats, the presence of compo...
متن کاملPet, an autotransporter enterotoxin from enteroaggregative Escherichia coli.
Enteroaggregative Escherichia coli (EAEC) is an emerging cause of diarrheal illness. Clinical data suggest that diarrhea caused by EAEC is predominantly secretory in nature, but the responsible enterotoxin has not been described. Work from our laboratories has implicated a ca. 108-kDa protein as a heat-labile enterotoxin and cytotoxin, as evidenced by rises in short-circuit current and falls in...
متن کاملHeterobinary adhesins based on the Escherichia coli FimH fimbrial protein.
The FimH adhesin of Escherichia coli type 1 fimbriae confers the ability to bind to D-mannosides by virtue of a receptor-binding domain located in its N-terminal region. This protein was engineered into a heterobifunctional adhesin by introducing a secondary binding site in the C-terminal region. The insertion of histidine clusters into this site resulted in coordination of various metal ions b...
متن کاملGlycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein.
Glycosylation is a common modulation of protein function in eukaryotes and is biologically important. However, in bacteria protein glycosylation is rare, and relatively few bacterial glycoproteins are known. In Escherichia coli only two glycoproteins have been described to date. Here we introduce a novel member to this exclusive group, namely, antigen 43 (Ag43), a self-recognizing autotransport...
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ژورنال
عنوان ژورنال: PROTEOMICS
سال: 2017
ISSN: 1615-9853
DOI: 10.1002/pmic.2017700181