Imperial College London
Portrait Picture

ProfessorAnneDell

Faculty of Natural Sciences, Department of Life Sciences

Professor of Carbohydrate Bichemistry
 
 
 
//

Contact

 

a.dell

 
 
//

Location

 

101BSir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Richards:2018:10.1074/jbc.RA118.004530,
author = {Richards, E and Bouché, L and Panico, M and Arbeloa, A and Vinogradov, E and Morris, H and Wren, B and Logan, SM and Dell, A and Fairweather, NF},
doi = {10.1074/jbc.RA118.004530},
journal = {Journal of Biological Chemistry},
pages = {18123--18137},
title = {The S-layer protein of a Clostridium difficile SLCT-11 strain displays a complex glycan required for normal cell growth and morphology.},
url = {http://dx.doi.org/10.1074/jbc.RA118.004530},
volume = {293},
year = {2018}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Clostridium difficile is a bacterial pathogen that causes major health challenges worldwide. It has a well-characterized surface (S)-layer, a para-crystalline proteinaceous layer surrounding the cell wall. In many bacterial and archaeal species, the S-layer is glycosylated, but no such modifications have been demonstrated in C. difficile. Here, we show that a C. difficilestrain of S-layer cassette type 11, Ox247, has a complex glycan attached via an O-linkage to Thr-38 of the S-layer low-molecular-weight subunit. Using mass spectrometry and NMR, we fully characterized this glycan. We present evidence that it is composed of three domains: (i) a core peptide-linked tetrasaccharide with the sequence -4-α-Rha-3-α-Rha-3-α-Rha-3-β-Gal-peptide, (ii) a repeating pentasaccharide with the sequence -4-β-Rha-4-α-Glc-3-β-Rha-4-(α-Rib-3-)β-Rha-, and (iii) a non-reducing end-terminal 2,3 cyclophosphoryl-rhamnose attached to a ribose-branched sub-terminal rhamnose residue. The Ox247 genome contains a 24 kb locus containing genes for synthesis and protein attachment of this glycan. Mutations in genes within this locus altered or completely abrogated formation of this glycan, and their phenotypes suggested that this S-layer modification may affect sporulation, cell length, and biofilm formation of C. difficile. In summary, our findings indicate that the S-layer protein of SLCT-11 strains displays a complex glycan and suggest that this glycan is required for C. difficilesporulation and control of cell shape, a discovery with implications for the development of antimicrobials targeting the S-layer.
AU  - Richards,E
AU  - Bouché,L
AU  - Panico,M
AU  - Arbeloa,A
AU  - Vinogradov,E
AU  - Morris,H
AU  - Wren,B
AU  - Logan,SM
AU  - Dell,A
AU  - Fairweather,NF
DO  - 10.1074/jbc.RA118.004530
EP  - 18137
PY  - 2018///
SN  - 0021-9258
SP  - 18123
TI  - The S-layer protein of a Clostridium difficile SLCT-11 strain displays a complex glycan required for normal cell growth and morphology.
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.RA118.004530
UR  - https://www.ncbi.nlm.nih.gov/pubmed/30275012
UR  - http://hdl.handle.net/10044/1/65604
VL  - 293
ER  -
Download