ArticleBMC structural biology2013
Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold.
Article in BMC structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Structural characterization of the Sel1-like repeat protein LceB from Legionella pneumophila.Protein science : a publication of the Protein Society · 2024Article
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- Characterization of the Pseudomonas aeruginosa T6SS PldB immunity proteins PA5086, PA5087 and PA5088 explains a novel stockpiling mechanism.Acta crystallographica. Section F, Structural biology communications · 2020Article
- TOR dynamically regulates plant cell-cell transport.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Klebsiella pneumoniae type VI secretion system-mediated microbial competition is PhoPQ controlled and reactive oxygen species dependent.PLoS pathogens · 2020Article
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- Inhibition of proteasome rescues a pathogenic variant of respiratory chain assembly factor COA7.EMBO molecular medicine · 2019Article
- Peptides for Infectious Diseases: From Probe Design to Diagnostic Microarrays.Antibodies (Basel, Switzerland) · 2019Review
- Identification and Characterization of msf, a Novel Virulence Factor in Haemophilus influenzae.PloS one · 2016Article
- Molecular modeling and computational analyses suggests that the Sinorhizobium meliloti periplasmic regulator protein ExoR adopts a superhelical fold and is controlled by a unique mechanism of proteolysis.Protein science : a publication of the Protein Society · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L.Acta crystallographica. Section F, Structural biology communications · 2014Article
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12 authors.
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Abstract
backgroundIncreasing rates of antimicrobial resistance among uropathogens led, among other efforts, to the application of subtractive reverse vaccinology for the identification of antigens present in extraintestinal pathogenic E. coli (ExPEC) strains but absent or variable in non-pathogenic strains, in a quest for a broadly protective Escherichia coli vaccine. The protein coded by locus c5321 from CFT073 E. coli was identified as one of nine potential vaccine candidates against ExPEC and was able to confer protection with an efficacy of 33% in a mouse model of sepsis. c5321 (known also as EsiB) lacks functional annotation and structurally belongs to the Sel1-like repeat (SLR) family. Herein, as part of the general characterization of this potential antigen, we have focused on its structural properties.
resultsWe report the 1.74 Å-resolution crystal structure of c5321 from CFT073 E. coli determined by Se-Met SAD phasing. The structure is composed of 11 SLR units in a topological organisation that highly resembles that found in HcpC from Helicobacter pylori, with the main difference residing in how the super-helical fold is stabilised. The stabilising effect of disulfide bridges in HcpC is replaced in c5321 by a strengthening of the inter-repeat hydrophobic core. A metal-ion binding site, uncharacteristic of SLR proteins, is detected between SLR units 3 and 4 in the region of the inter-repeat hydrophobic core. Crystal contacts are observed between the C-terminal tail of one molecule and the C-terminal amphipathic groove of a neighbouring one, resembling interactions between ligand and proteins containing tetratricopeptide-like repeats.
conclusionsThe structure of antigen c5321 presents a mode of stabilization of the SLR fold different from that observed in close homologs of known structure. The location of the metal-ion binding site and the observed crystal contacts suggest a potential role in regulation of conformational flexibility and interaction with yet unidentified target proteins, respectively. These findings open new perspectives in both antigen design and for the identification of a functional role for this protective antigen.
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