Imperial College London
Alternate

DrAlexanderWebb

Faculty of Medicine, Department of Infectious Disease

Research Associate
 
 
 
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Contact

 

+44 (0)20 7594 3058alexander.webb1

 
 
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Location

 

Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Percy:2016:10.1128/JB.00116-16,
author = {Percy, M and Karinou, E and Webb, A and Grundling, A},
doi = {10.1128/JB.00116-16},
journal = {Journal of Bacteriology},
pages = {2029--2042},
title = {Identification of a lipoteichoic acid glycosyltransferase enzyme reveals that GW-domain containing proteins can be retained in the cell wall of Listeria monocytogenes in the absence of lipoteichoic acid or its modifications},
url = {http://dx.doi.org/10.1128/JB.00116-16},
volume = {198},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Listeria monocytogenes is a food-borne Gram-positive bacterial pathogen and many of its virulence factors are either secreted proteins, or proteins covalently or non-covalently-attached to the cell wall. Previous work has indicated that non-covalently-attached proteins with GW domains are retained in the cell wall by binding to the cell wall polymer lipoteichoic acid (LTA). LTA is a glycerolphosphate polymer, which is modified in L. monocytogenes with galactose and D-alanine residues. We identified Lmo0933 as the cytoplasmic glycosyltransferase required for the LTA glycosylation process and renamed the protein GtlA for glycosyltransferase LTA A. Using L. monocytogenes mutants lacking galactose or D-alanine modifications or the complete LTA polymer, we show that GW-domain proteins are still retained within the cell wall, indicating that other cell wall polymers are involved in the retention of GW-domain proteins. Further experiments reveal peptidoglycan as the binding receptor as a purified GW domainfusion protein can bind to L. monocytogenes cells lacking wall teichoic acid (WTA) as well as purified peptidoglycan derived from a wild-type or WTA-negative strain. With this, we not only identified the first enzyme involved in the LTA glycosylation process, but we also provide new insight into the binding mechanism of non-covalently attached cell wall proteins.
AU  - Percy,M
AU  - Karinou,E
AU  - Webb,A
AU  - Grundling,A
DO  - 10.1128/JB.00116-16
EP  - 2042
PY  - 2016///
SN  - 1098-5530
SP  - 2029
TI  - Identification of a lipoteichoic acid glycosyltransferase enzyme reveals that GW-domain containing proteins can be retained in the cell wall of Listeria monocytogenes in the absence of lipoteichoic acid or its modifications
T2  - Journal of Bacteriology
UR  - http://dx.doi.org/10.1128/JB.00116-16
UR  - http://hdl.handle.net/10044/1/32421
VL  - 198
ER  -
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