CORE
🇺🇦
make metadata, not war
Services
Services overview
Explore all CORE services
Access to raw data
API
Dataset
FastSync
Content discovery
Recommender
Discovery
OAI identifiers
OAI Resolver
Managing content
Dashboard
Bespoke contracts
Consultancy services
Support us
Support us
Membership
Sponsorship
Community governance
Advisory Board
Board of supporters
Research network
About
About us
Our mission
Team
Blog
FAQs
Contact us
Functional significance of active site residues in the enzymatic component of the Clostridium difficile binary toxin
Authors
Arnold
Barth
+22 more
Barth
Barth
Biasini
Davies
Gerding
Guex
Gülke
Holbourn
Kiefer
Mauss
Nagahama
Perelle
Perelle
Popoff
Roberts
Roberts
Salentin
Schwan
Sundriyal
Sundriyal
Tsuge
Vandekerckhove
Publication date
11 August 2016
Publisher
'Elsevier BV'
Doi
Cite
Abstract
© 2016 Clostridium difficile binary toxin (CDT) is an ADP-ribosyltransferase which is linked to enhanced pathogenesis of C. difficile strains. CDT has dual function: domain a (CDTa) catalyses the ADP-ribosylation of actin (enzymatic component), whereas domain b (CDTb) transports CDTa into the cytosol (transport component). Understanding the molecular mechanism of CDT is necessary to assess its role in C. difficile infection. Identifying amino acids that are essential to CDTa function may aid drug inhibitor design to control the severity of C. difficile infections. Here we report mutations of key catalytic residues within CDTa and their effect on CDT cytotoxicity. Rather than an all-or-nothing response, activity of CDTa mutants vary with the type of amino acid substitution; S345A retains cytotoxicity whereas S345Y was sufficient to render CDT non-cytotoxic. Thus CDTa cytotoxicity levels are directly linked to ADP-ribosyltransferase activity
Similar works
Full text
Open in the Core reader
Download PDF
Available Versions
Elsevier - Publisher Connector
See this paper in CORE
Go to the repository landing page
Download from data provider
Last time updated on 05/05/2017
Crossref
See this paper in CORE
Go to the repository landing page
Download from data provider
info:doi/10.1016%2Fj.bbrep.201...
Last time updated on 01/04/2019
E-space: Manchester Metropolitan University's Research Repository
See this paper in CORE
Go to the repository landing page
Download from data provider
oai:e-space.mmu.ac.uk:625170
Last time updated on 26/03/2020
Supporting member
OPUS
See this paper in CORE
Go to the repository landing page
Download from data provider
oai:purehost.bath.ac.uk:public...
Last time updated on 02/01/2019