Quantitative lipoproteomics in Clostridium difficile reveals a role for lipoproteins in sporulation
File(s)
Published version
Author(s)
Charlton, T
Kovacs-Simon, A
Michell, S
Fairweather, N
Tate, E
Type
Journal Article
Abstract
Bacterial lipoproteins are surface exposed, anchored to the membrane by S
diacylglyceryl modification of the N-terminal cysteine thiol. They play important roles in
many essential cellular processes and in bacterial pathogenesis. For example,
Clostridium difficile is a Gram-positive anaerobe that causes severe gastrointestinal
disease, however, its lipoproteome remains poorly characterized. Here we describe the
application of metabolic tagging with alkyne-tagged lipid analogues, in combination
with quantitative proteomics, to profile protein lipidation across diverse C. difficile
strains and on inactivation of specific components of the lipoprotein biogenesis
pathway. These studies provide the first comprehensive map of the C. difficile
lipoproteome, demonstrate the existence of two active lipoprotein signal peptidases
and provide insights into lipoprotein function, implicating the lipoproteome in
transmission of this pathogen.
diacylglyceryl modification of the N-terminal cysteine thiol. They play important roles in
many essential cellular processes and in bacterial pathogenesis. For example,
Clostridium difficile is a Gram-positive anaerobe that causes severe gastrointestinal
disease, however, its lipoproteome remains poorly characterized. Here we describe the
application of metabolic tagging with alkyne-tagged lipid analogues, in combination
with quantitative proteomics, to profile protein lipidation across diverse C. difficile
strains and on inactivation of specific components of the lipoprotein biogenesis
pathway. These studies provide the first comprehensive map of the C. difficile
lipoproteome, demonstrate the existence of two active lipoprotein signal peptidases
and provide insights into lipoprotein function, implicating the lipoproteome in
transmission of this pathogen.
Date Issued
2015-11-19
Date Acceptance
2015-10-01
Citation
Chemistry & Biology, 2015, 22
ISSN
1074-5521
Publisher
Elsevier (Cell Press)
Journal / Book Title
Chemistry & Biology
Volume
22
Copyright Statement
© 2015 The Authors. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/)
Identifier
http://www.cell.com/chemistry-biology/abstract/S1074-5521(15)00408-1
Publication Status
Published