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Topology of the outer-membrane secretin PilQ from Neisseria meningitidis
Centre for Molecular Biology and Neuroscience, Institute of Microbiology, University of Oslo, Oslo, Norway, Centre for Molecular Biology and Neuroscience, Institute of Microbiology, Rikshospitalet-Radiumhospitalet Medical Centre, Norway.
Centre for Molecular Biology and Neuroscience, Institute of Microbiology, University of Oslo, Oslo, Norway.
Faculty of Life Sciences, The University of Manchester, Sackville Street, Manchester M60 1QD, United Kingdom.
Faculty of Life Sciences, The University of Manchester, Sackville Street, Manchester M60 1QD, United Kingdom.
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2006 (English)In: Microbiology, ISSN 1350-0872, Vol. 152, no 12, 3751-3764 p.Article in journal (Refereed) Published
Abstract [en]

Neisseria meningitidis is the causative agent of epidemic meningococcal meningitis and septicaemia. Type IV pili are surface organelles that mediate a variety of functions, including adhesion, twitching motility, and competence for DNA binding and uptake in transformation. The secretin PilQ is required for type IV pilus expression at the cell surface, and forms a dodecameric cage-like macromolecular complex in the meningococcal outer membrane. PilQ-null mutants are devoid of surface pili, and prevailing evidence suggests that the PilQ complex facilitates extrusion and retraction of type IV pili across the outer membrane. Defining the orientation of the meningococcal PilQ complex in the membrane is a prerequisite for understanding the structure-function relationships of this important protein in pilus biology. In order to begin to define the topology of the PilQ complex in the outer membrane, polyhistidine insertions in N- and C-terminal regions of PilQ were constructed, and their subcellular locations examined. Notably, the insertion epitopes at residues 205 and 678 were located within the periplasm, whereas residue 656 was exposed at the outer surface of the outer membrane. Using electron microscopy with Ni-NTA gold labelling, it was demonstrated that the insertion at residue 205 within the N-terminus mapped to a site on the arm-like features of the 3D structure of the PilQ multimer. Interestingly, mutation of the same region gave rise to an increase in vancomycin permeability through the PilQ complex. The results yield novel information on the PilQ N-terminal location and function in the periplasm, and reveal a complex organization of the membrane-spanning secretin in vivo. © 2006 SGM.

Place, publisher, year, edition, pages
2006. Vol. 152, no 12, 3751-3764 p.
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-50062DOI: 10.1099/mic.0.2006/000315-0OAI: oai:DiVA.org:liu-50062DiVA: diva2:270958
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2011-01-11

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