Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.

Pili of pathogenic Neisseria are major virulence factors associated with adhesion, twitching motility, auto-aggregation, and DNA transformation. Pili of N. meningitidis are subject to several different post-translational modifications. Among these pilin modifications, the presence of phosphorylcholi...

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Autores principales: Freda E-C Jen, Matthew J Warren, Benjamin L Schulz, Peter M Power, W Edward Swords, Jeffery N Weiser, Michael A Apicella, Jennifer L Edwards, Michael P Jennings
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Publicado: Public Library of Science (PLoS) 2013
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Acceso en línea:https://doaj.org/article/ba46c9c302e347529caa330cdba32102
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spelling oai:doaj.org-article:ba46c9c302e347529caa330cdba321022021-11-18T06:05:37ZDual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.1553-73661553-737410.1371/journal.ppat.1003377https://doaj.org/article/ba46c9c302e347529caa330cdba321022013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23696740/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Pili of pathogenic Neisseria are major virulence factors associated with adhesion, twitching motility, auto-aggregation, and DNA transformation. Pili of N. meningitidis are subject to several different post-translational modifications. Among these pilin modifications, the presence of phosphorylcholine (ChoP) and a glycan on the pilin protein are phase-variable (subject to high frequency, reversible on/off switching of expression). In this study we report the location of two ChoP modifications on the C-terminus of N. meningitidis pilin. We show that the surface accessibility of ChoP on pili is affected by phase variable changes to the structure of the pilin-linked glycan. We identify for the first time that the platelet activating factor receptor (PAFr) is a key, early event receptor for meningococcal adherence to human bronchial epithelial cells and tissue, and that synergy between the pilin-linked glycan and ChoP post-translational modifications is required for pili to optimally engage PAFr to mediate adherence to human airway cells.Freda E-C JenMatthew J WarrenBenjamin L SchulzPeter M PowerW Edward SwordsJeffery N WeiserMichael A ApicellaJennifer L EdwardsMichael P JenningsPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 5, p e1003377 (2013)
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
Freda E-C Jen
Matthew J Warren
Benjamin L Schulz
Peter M Power
W Edward Swords
Jeffery N Weiser
Michael A Apicella
Jennifer L Edwards
Michael P Jennings
Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
description Pili of pathogenic Neisseria are major virulence factors associated with adhesion, twitching motility, auto-aggregation, and DNA transformation. Pili of N. meningitidis are subject to several different post-translational modifications. Among these pilin modifications, the presence of phosphorylcholine (ChoP) and a glycan on the pilin protein are phase-variable (subject to high frequency, reversible on/off switching of expression). In this study we report the location of two ChoP modifications on the C-terminus of N. meningitidis pilin. We show that the surface accessibility of ChoP on pili is affected by phase variable changes to the structure of the pilin-linked glycan. We identify for the first time that the platelet activating factor receptor (PAFr) is a key, early event receptor for meningococcal adherence to human bronchial epithelial cells and tissue, and that synergy between the pilin-linked glycan and ChoP post-translational modifications is required for pili to optimally engage PAFr to mediate adherence to human airway cells.
format article
author Freda E-C Jen
Matthew J Warren
Benjamin L Schulz
Peter M Power
W Edward Swords
Jeffery N Weiser
Michael A Apicella
Jennifer L Edwards
Michael P Jennings
author_facet Freda E-C Jen
Matthew J Warren
Benjamin L Schulz
Peter M Power
W Edward Swords
Jeffery N Weiser
Michael A Apicella
Jennifer L Edwards
Michael P Jennings
author_sort Freda E-C Jen
title Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
title_short Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
title_full Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
title_fullStr Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
title_full_unstemmed Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
title_sort dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/ba46c9c302e347529caa330cdba32102
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