Structural highlights
Publication Abstract from PubMedColonization factor CFA/I defines the major adhesive fimbriae of enterotoxigenic Escherichia coli and mediates bacterial attachment to host intestinal epithelial cells. The CFA/I fimbria consists of a tip-localized minor adhesive subunit, CfaE, and thousands of copies of the major subunit CfaB polymerized into an ordered helical rod. Biosynthesis of CFA/I fimbriae requires the assistance of the periplasmic chaperone CfaA and outer membrane usher CfaC. Although the CfaE subunit is proposed to initiate the assembly of CFA/I fimbriae, how it performs this function remains elusive. Here, we report the establishment of an in vitro assay for CFA/I fimbria assembly and show that stabilized CfaA-CfaB and CfaA-CfaE binary complexes together with CfaC are sufficient to drive fimbria formation. The presence of both CfaA-CfaE and CfaC accelerates fimbria formation, while the absence of either component leads to linearized CfaB polymers in vitro. We further report the crystal structure of the stabilized CfaA-CfaE complex, revealing features unique for biogenesis of Class 5 fimbriae. Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.,He LH, Wang H, Liu Y, Kang M, Li T, Li CC, Tong AP, Zhu YB, Song YJ, Savarino SJ, Prouty MG, Xia D, Bao R PLoS Pathog. 2020 Oct 2;16(10):e1008848. doi: 10.1371/journal.ppat.1008848., eCollection 2020 Oct. PMID:33007034[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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