Imperial College London

Emeritus Professor Howard R. Morris FRS

Faculty of Natural SciencesDepartment of Life Sciences

Senior Research Investigator
 
 
 
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Contact

 

+44 (0)20 7594 5221h.morris

 
 
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Assistant

 

Miss Cathy Thomas +44 (0)20 7594 5220

 
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Location

 

103Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Bouché:2016:10.1074/jbc.M116.749481,
author = {Bouché, L and Panico, M and Hitchen, P and Binet, D and Sastre, F and Faulds-Pain, A and Valiente, E and Vinogradov, E and Aubry, A and Fulton, K and Twine, S and Logan, SM and Wren, BW and Dell, A and Morris, HR},
doi = {10.1074/jbc.M116.749481},
journal = {Journal of Biological Chemistry},
pages = {25439--25449},
title = {The Type B flagellin of hypervirulent Clostridium difficile is modified with novel sulphonated Peptidylamido-glycans},
url = {http://dx.doi.org/10.1074/jbc.M116.749481},
volume = {291},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Glycosylation of flagellins is a well recognized property of many bacterial species. In this study we describe the structural characterization of novel flagellar glycans from a number of hypervirulent strains of C. difficile. We used mass spectrometry (nano LC- MS and MS/MS analysis) to identify a number of putative glycopeptides which carried a variety of glycoform substitutions each of which was linked through an initial HexNAc residue to Ser or Thr. Detailed analysis of a LLDGSSTEIR glycopeptide released by tryptic digestion, which carried two variant structures, revealed that the glycopeptide contained, in addition to carbohydrate moieties, a novel structural entity. A variety of Electrospray-MS strategies using Q-TOF technology were used to define this entity, including positive- and negative-ion collisionally activated decomposition (CAD) MS/MS which produced unique fragmentation patterns, and high resolution accurate mass measurement to allow derivation of atomic compositions, leading to the suggestion of a Taurine-containing peptidylamido-glycan structure. Finally NMR analysis of flagellin glycopeptides provided complementary information. The glycan portion of the modification was assigned as α-Fuc3N-(1→3)-α-Rha-(1→2)-α-Rha3OMe-(1→3)-β-GlcNAc-(1→)Ser and the novel capping moiety was shown to be comprised of Taurine, Alanine, and Glycine. This is the first report of a novel O-linked sulphonated peptidylamido-glycan moiety decorating a flagellin protein.
AU - Bouché,L
AU - Panico,M
AU - Hitchen,P
AU - Binet,D
AU - Sastre,F
AU - Faulds-Pain,A
AU - Valiente,E
AU - Vinogradov,E
AU - Aubry,A
AU - Fulton,K
AU - Twine,S
AU - Logan,SM
AU - Wren,BW
AU - Dell,A
AU - Morris,HR
DO - 10.1074/jbc.M116.749481
EP - 25449
PY - 2016///
SN - 1083-351X
SP - 25439
TI - The Type B flagellin of hypervirulent Clostridium difficile is modified with novel sulphonated Peptidylamido-glycans
T2 - Journal of Biological Chemistry
UR - http://dx.doi.org/10.1074/jbc.M116.749481
UR - http://hdl.handle.net/10044/1/42394
VL - 291
ER -