Imperial College London
Alternate

Prof Steve Matthews

Faculty of Natural Sciences, Department of Life Sciences

Professor of Chemical and Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5315s.j.matthews Website

 
 
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Location

 

602Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Berry:2019:10.1074/jbc.RA118.006917,
author = {Berry, J and Gurung, I and Anonsen, JH and Spielman, I and Harper, E and Hall, A and Goosens, V and Raynaud, C and Koomey, M and Biais, N and Matthews, S and Pelicic, V},
doi = {10.1074/jbc.RA118.006917},
journal = {Journal of Biological Chemistry},
pages = {6796--6808},
title = {Global biochemical and structural analysis of the type IV pilus from the Gram-positive bacterium Streptococcus sanguinis},
url = {http://dx.doi.org/10.1074/jbc.RA118.006917},
volume = {294},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Type IV pili (Tfp) are functionally versatile filaments, widespread in prokaryotes, that belong to a large class of filamentous nanomachines known as type IV filaments (Tff). Although Tfp have been extensively studied in several Gram-negative pathogens where they function as key virulence factors, many aspects of their biology remain poorly understood. Here, we performed a global biochemical and structural analysis of Tfp in a recently emerged Gram-positive model, Streptococcus sanguinis. In particular, we focused on the five pilins and pilin-like proteins involved in Tfp biology in S. sanguinis. We found that the two major pilins, PilE1 and PilE2, (i) follow widely conserved principles for processing by the prepilin peptidase PilD and for assembly into filaments; (ii) display only one of the post-translational modifications frequently found in pilins, i.e. a methylated N-terminus; (iii) are found in the same hetero-polymeric filaments; and (iv) are not functionally equivalent. The 3D structure of PilE1, solved by NMR, revealed a classical pilin fold with a highly unusual flexible C-terminus. Intriguingly, PilE1 more closely resembles pseudopilins forming shorter Tff than bona fide Tfp-forming major pilins, underlining the evolutionary relatedness among different Tff. Finally, we show that S. sanguinis Tfp contain a low abundance of three additional proteins processed by PilD, the minor pilins PilA, PilB, and PilC. These findings provide the first global biochemical and structural picture of a Gram-positive Tfp and have fundamental implications for our understanding of a widespread class of filamentous nanomachines.
AU  - Berry,J
AU  - Gurung,I
AU  - Anonsen,JH
AU  - Spielman,I
AU  - Harper,E
AU  - Hall,A
AU  - Goosens,V
AU  - Raynaud,C
AU  - Koomey,M
AU  - Biais,N
AU  - Matthews,S
AU  - Pelicic,V
DO  - 10.1074/jbc.RA118.006917
EP  - 6808
PY  - 2019///
SN  - 0021-9258
SP  - 6796
TI  - Global biochemical and structural analysis of the type IV pilus from the Gram-positive bacterium Streptococcus sanguinis
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.RA118.006917
UR  - http://hdl.handle.net/10044/1/68668
VL  - 294
ER  -
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