Multiple Structures Disclose the Secretins' Secrets

Filloux, Alain; Voulhoux, Romé

doi:10.1128/jb.00702-17

Cited by 15 publications

(17 citation statements)

References 16 publications

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“…In contrast, the PilQ secretin adopts a complex, multidomain oligomeric assembly which spans the outer membrane and part of the periplasm. Using recent structures derived from related secretins 51 , a model for the transmembrane portion of PilQ was generated; a previous NMR study generated structural models for the KH-like α/β domains and β domain which constitute the portion within the periplasm 52 . Sequence variation mapped to two parts of the transmembrane region, specifically the cap and periplasmic gate, which closes off the internal chamber within the oligomer 51 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Here, we used a generalized refolding protocol which was successful previously 11–13 , although it is imperfect: we have not been able to develop a refolding protocol which successfully reconstitutes the dodecameric PilQ assembly, for example. PilQ is a member of the secretin family, a group of iOMPs which are challenging to isolate and study 51 . The fact that our recombinant PilQ sample shows a well-defined peak in the Sypro Orange fluorescence assay suggests that some conformational epitopes are retained, however (Supplementary Fig.…”

Section: Discussionmentioning

confidence: 99%

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Immunogenicity profiling of protein antigens from capsular group B Neisseria meningitidis

Awanye

Chang

Wheeler

et al. 2019

Sci Rep

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Outer membrane vesicle (OMV)- based vaccines have been used to provide strain-specific protection against capsular group B Neisseria meningitidis infections, but the full breadth of the immune response against the components of the OMV has not been established. Sera from adults vaccinated with an OMV vaccine were used to screen 91 outer membrane proteins (OMPs) incorporated in an antigen microarray panel. Antigen-specific IgG levels were quantified pre-vaccination, and after 12 and 18 weeks. These results were compared with IgG levels from mice vaccinated with the same OMV vaccine. The repertoires of highly responding antigens in humans and mice overlapped, but were not identical. The highest responding antigens to human IgG comprised four integral OMPs (PorA, PorB, OpcA and PilQ), a protein which promotes the stability of PorA and PorB (RmpM) and two lipoproteins (BamC and GNA1162). These observations will assist in evaluating the role of minor antigen components within OMVs in providing protection against meningococcal infection. In addition, the relative dominance of responses to integral OMPs in humans emphasizes the importance of this subclass and points to the value of maintaining conformational epitopes from integral membrane proteins in vaccine formulations.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Immunogenicity profiling of protein antigens from capsular group B Neisseria meningitidis

Awanye

Chang

Wheeler

et al. 2019

Sci Rep

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“… 2013 ; Worrall et al. 2016 ; Filloux and Voulhoux 2018 ). T3SS secretins consist of three N-terminal N-domains (N0, N1 and N3) that protrude deeply into the periplasm, a C-domain that forms the outer membrane portal, and an S-domain through which a cognate pilotin binds the secretin and mediates its targeting and assembly (Worrall et al.…”

Section: Structure Of the Injectisomementioning

confidence: 99%

Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells

Wagner

Grin

Malmsheimer

et al. 2018

FEMS Microbiology Letters

155

134

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Virulence-associated type III secretion systems (T3SS) serve the injection of bacterial effector proteins into eukaryotic host cells. They are able to secrete a great diversity of substrate proteins in order to modulate host cell function, and have evolved to sense host cell contact and to inject their substrates through a translocon pore in the host cell membrane. T3SS substrates contain an N-terminal signal sequence and often a chaperone-binding domain for cognate T3SS chaperones. These signals guide the substrates to the machine where substrates are unfolded and handed over to the secretion channel formed by the transmembrane domains of the export apparatus components and by the needle filament. Secretion itself is driven by the proton motive force across the bacterial inner membrane. The needle filament measures 20–150 nm in length and is crowned by a needle tip that mediates host-cell sensing. Secretion through T3SS is a highly regulated process with early, intermediate and late substrates. A strict secretion hierarchy is required to build an injectisome capable of reaching, sensing and penetrating the host cell membrane, before host cell-acting effector proteins are deployed. Here, we review the recent progress on elucidating the assembly, structure and function of T3SS injectisomes.

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“…Secretins and their cognate pilotins create outer-membrane channels in various secretion and pilus systems. Secretin oligomers have a unique double-layered b-barrel architecture (Filloux and Voulhoux, 2018;Worrall et al, 2016). The outer b-barrel forms a large vestibule that passes though the outer membrane (Worrall et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP

et al. 2021

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Multiple Structures Disclose the Secretins' Secrets

Cited by 15 publications

References 16 publications

Immunogenicity profiling of protein antigens from capsular group B Neisseria meningitidis

Immunogenicity profiling of protein antigens from capsular group B Neisseria meningitidis

Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells

CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP

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