ArticlePLoS pathogens2014
Structure of CfaA suggests a new family of chaperones essential for assembly of class 5 fimbriae.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- A bipartite bacterial virulence factor targets the complement system and neutrophil activation.The EMBO journal · 2025Article
- Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.PLoS pathogens · 2020Article
- Classical chaperone-usher (CU) adhesive fimbriome: uropathogenic Escherichia coli (UPEC) and urinary tract infections (UTIs).Folia microbiologica · 2020Review
- Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.The Journal of biological chemistry · 2018Article
- Off-pathway assembly of fimbria subunits is prevented by chaperone CfaA of CFA/I fimbriae from enterotoxigenic E. coli.Molecular microbiology · 2016Article
- Binding of CFA/I Pili of Enterotoxigenic Escherichia coli to Asialo-GM1 Is Mediated by the Minor Pilin CfaE.Infection and immunity · 2016Article
- Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.PLoS pathogens · 2015Article
- Purification, crystallization and preliminary X-ray diffraction analysis of the Escherichia coli common pilus chaperone EcpB.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Structure and function of enterotoxigenic Escherichia coli fimbriae from differing assembly pathways.Molecular microbiology · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Adhesive pili on the surface of pathogenic bacteria comprise polymerized pilin subunits and are essential for initiation of infections. Pili assembled by the chaperone-usher pathway (CUP) require periplasmic chaperones that assist subunit folding, maintain their stability, and escort them to the site of bioassembly. Until now, CUP chaperones have been classified into two families, FGS and FGL, based on the short and long length of the subunit-interacting loops between its F1 and G1 β-strands, respectively. CfaA is the chaperone for assembly of colonization factor antigen I (CFA/I) pili of enterotoxigenic E. coli (ETEC), a cause of diarrhea in travelers and young children. Here, the crystal structure of CfaA along with sequence analyses reveals some unique structural and functional features, leading us to propose a separate family for CfaA and closely related chaperones. Phenotypic changes resulting from mutations in regions unique to this chaperone family provide insight into their function, consistent with involvement of these regions in interactions with cognate subunits and usher proteins during pilus assembly.
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