Imperial College London

DrVladimirPelicic

Faculty of MedicineDepartment of Medicine

Reader in Molecular Bacteriology & Infection
 
 
 
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Contact

 

+44 (0)20 7594 2080v.pelicic Website

 
 
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Location

 

3.20Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Carbonnelle:2006:10.1111/j.1365-2958.2006.05341.x,
author = {Carbonnelle, E and Helaine, S and Nassif, X and Pelicic, V},
doi = {10.1111/j.1365-2958.2006.05341.x},
journal = {Mol Microbiol},
pages = {1510--1522},
title = {A systematic genetic analysis in Neisseria meningitidis defines the Pil proteins required for assembly, functionality, stabilization and export of type IV pili.},
url = {http://dx.doi.org/10.1111/j.1365-2958.2006.05341.x},
volume = {61},
year = {2006}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Although type IV pili (Tfp) are among the commonest virulence factors in bacteria, their biogenesis by complex machineries of 12-15 proteins, and thereby their function remains poorly understood. Interestingly, some of these proteins were reported to merely antagonize the retraction of the fibres powered by PilT, because piliation could be restored in their absence by a mutation in the pilT gene. The recent identification of the 15 Pil proteins dedicated to Tfp biogenesis in Neisseria meningitidis offered us the unprecedented possibility to define their exact contribution in this process. We therefore systematically introduced a pilT mutation into the corresponding non-piliated mutants and characterized them for the rescue of Tfp and Tfp-mediated virulence phenotypes. We found that in addition to the pilin, the main constituent of Tfp, only six Pil proteins were required for the actual assembly of the fibres, because apparently normal fibres were restored in the remaining mutants. Restored fibres were surface-exposed, except in the pilQ/T mutant in which they were trapped in the periplasm, suggesting that the PilQ secretin was the sole Pil component necessary for their emergence on the surface. Importantly, although in most mutants the restored Tfp were not functional, the pilG/T and pilH/T mutants could form bacterial aggregates and adhere to human cells efficiently, suggesting that Tfp stabilization and functional maturation are two discrete steps. These findings have numerous implications for understanding Tfp biogenesis/function and provide a useful groundwork for the characterization of the precise function of each Pil protein in this process.
AU - Carbonnelle,E
AU - Helaine,S
AU - Nassif,X
AU - Pelicic,V
DO - 10.1111/j.1365-2958.2006.05341.x
EP - 1522
PY - 2006///
SN - 0950-382X
SP - 1510
TI - A systematic genetic analysis in Neisseria meningitidis defines the Pil proteins required for assembly, functionality, stabilization and export of type IV pili.
T2 - Mol Microbiol
UR - http://dx.doi.org/10.1111/j.1365-2958.2006.05341.x
UR - https://www.ncbi.nlm.nih.gov/pubmed/16968224
UR - http://hdl.handle.net/10044/1/26765
VL - 61
ER -