Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.

Type IV pili are polymeric fibers which protrude from the cell surface and play a critical role in adhesion and invasion by pathogenic bacteria. The secretion of pili across the periplasm and outer membrane is mediated by a specialized secretin protein, PilQ, but the way in which this large channel...

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Autores principales:	Jamie-Lee Berry, Marie M Phelan, Richard F Collins, Tomas Adomavicius, Tone Tønjum, Stefan A Frye, Louise Bird, Ray Owens, Robert C Ford, Lu-Yun Lian, Jeremy P Derrick
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c5dfad14645e482ebefde8203a97758d
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spelling	oai:doaj.org-article:c5dfad14645e482ebefde8203a97758d2021-11-18T06:03:58ZStructure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.1553-73661553-737410.1371/journal.ppat.1002923https://doaj.org/article/c5dfad14645e482ebefde8203a97758d2012-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23028322/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Type IV pili are polymeric fibers which protrude from the cell surface and play a critical role in adhesion and invasion by pathogenic bacteria. The secretion of pili across the periplasm and outer membrane is mediated by a specialized secretin protein, PilQ, but the way in which this large channel is formed is unknown. Using NMR, we derived the structures of the periplasmic domains from N. meningitidis PilQ: the N-terminus is shown to consist of two β-domains, which are unique to the type IV pilus-dependent secretins. The structure of the second β-domain revealed an eight-stranded β-sandwich structure which is a novel variant of the HSP20-like fold. The central part of PilQ consists of two α/β fold domains: the structure of the first of these is similar to domains from other secretins, but with an additional α-helix which links it to the second α/β domain. We also determined the structure of the entire PilQ dodecamer by cryoelectron microscopy: it forms a cage-like structure, enclosing a cavity which is approximately 55 Å in internal diameter at its largest extent. Specific regions were identified in the density map which corresponded to the individual PilQ domains: this allowed us to dock them into the cryoelectron microscopy density map, and hence reconstruct the entire PilQ assembly which spans the periplasm. We also show that the C-terminal domain from the lipoprotein PilP, which is essential for pilus assembly, binds specifically to the first α/β domain in PilQ and use NMR chemical shift mapping to generate a model for the PilP:PilQ complex. We conclude that passage of the pilus fiber requires disassembly of both the membrane-spanning and the β-domain regions in PilQ, and that PilP plays an important role in stabilising the PilQ assembly during secretion, through its anchorage in the inner membrane.Jamie-Lee BerryMarie M PhelanRichard F CollinsTomas AdomaviciusTone TønjumStefan A FryeLouise BirdRay OwensRobert C FordLu-Yun LianJeremy P DerrickPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 9, p e1002923 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Jamie-Lee Berry Marie M Phelan Richard F Collins Tomas Adomavicius Tone Tønjum Stefan A Frye Louise Bird Ray Owens Robert C Ford Lu-Yun Lian Jeremy P Derrick Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.
description	Type IV pili are polymeric fibers which protrude from the cell surface and play a critical role in adhesion and invasion by pathogenic bacteria. The secretion of pili across the periplasm and outer membrane is mediated by a specialized secretin protein, PilQ, but the way in which this large channel is formed is unknown. Using NMR, we derived the structures of the periplasmic domains from N. meningitidis PilQ: the N-terminus is shown to consist of two β-domains, which are unique to the type IV pilus-dependent secretins. The structure of the second β-domain revealed an eight-stranded β-sandwich structure which is a novel variant of the HSP20-like fold. The central part of PilQ consists of two α/β fold domains: the structure of the first of these is similar to domains from other secretins, but with an additional α-helix which links it to the second α/β domain. We also determined the structure of the entire PilQ dodecamer by cryoelectron microscopy: it forms a cage-like structure, enclosing a cavity which is approximately 55 Å in internal diameter at its largest extent. Specific regions were identified in the density map which corresponded to the individual PilQ domains: this allowed us to dock them into the cryoelectron microscopy density map, and hence reconstruct the entire PilQ assembly which spans the periplasm. We also show that the C-terminal domain from the lipoprotein PilP, which is essential for pilus assembly, binds specifically to the first α/β domain in PilQ and use NMR chemical shift mapping to generate a model for the PilP:PilQ complex. We conclude that passage of the pilus fiber requires disassembly of both the membrane-spanning and the β-domain regions in PilQ, and that PilP plays an important role in stabilising the PilQ assembly during secretion, through its anchorage in the inner membrane.
format	article
author	Jamie-Lee Berry Marie M Phelan Richard F Collins Tomas Adomavicius Tone Tønjum Stefan A Frye Louise Bird Ray Owens Robert C Ford Lu-Yun Lian Jeremy P Derrick
author_facet	Jamie-Lee Berry Marie M Phelan Richard F Collins Tomas Adomavicius Tone Tønjum Stefan A Frye Louise Bird Ray Owens Robert C Ford Lu-Yun Lian Jeremy P Derrick
author_sort	Jamie-Lee Berry
title	Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.
title_short	Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.
title_full	Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.
title_fullStr	Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.
title_full_unstemmed	Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.
title_sort	structure and assembly of a trans-periplasmic channel for type iv pili in neisseria meningitidis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/c5dfad14645e482ebefde8203a97758d
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Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.

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