Show simple item record

dc.contributor.authorCheung, Jackie K
dc.contributor.authorAdams, Vicki
dc.contributor.authorD'Souza, Danielle
dc.contributor.authorJames, Meagan
dc.contributor.authorDay, Christopher J
dc.contributor.authorJennings, Michael P
dc.contributor.authorLyras, Dena
dc.contributor.authorRood, Julian
dc.date.accessioned2020-07-16T03:36:48Z
dc.date.available2020-07-16T03:36:48Z
dc.date.issued2020
dc.identifier.issn1438-4221
dc.identifier.doi10.1016/j.ijmm.2020.151398
dc.identifier.urihttp://hdl.handle.net/10072/395505
dc.description.abstractClostridium perfringens is the causative agent of human clostridial myonecrosis; the major toxins involved in this disease are α-toxin and perfringolysin O. The RevSR two-component regulatory system has been shown to be involved in regulating virulence in a mouse myonecrosis model. Previous microarray and RNAseq analysis of a revR mutant implied that factors other than the major toxins may play a role in virulence. The RNAseq data showed that the expression of the gene encoding the EngCP endo α-N-acetylgalactosaminidase (CPE0693) was significantly down-regulated in a revR mutant. Enzymes from this family have been identified in several Gram-positive pathogens and have been postulated to contribute to their virulence. In this study, we constructed an engCP mutant of C. perfringens and showed that it was significantly less virulent than its wild-type parent strain. Virulence was restored by complementation in trans with the wild-type engCP gene. We also demonstrated that purified EngCP was able to hydrolyse α-dystroglycan derived from C2C12 mouse myotubes. However, EngCP had little effect on membrane permeability in mice, suggesting that EngCP may play a role other than the disruption of the structural integrity of myofibres. Glycan array analysis indicated that EngCP could recognise structures containing the monosaccharide N-acetlygalactosamine at 4C, but could recognise structures terminating in galactose, glucose and N-acetylglucosamine under conditions where EngCP was enzymatically active. In conclusion, we have obtained evidence that EngCP is required for virulence in C. perfringens and, although classical exotoxins are important for disease, we have now shown that an O-glycosidase also plays an important role in the disease process.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom151398:1
dc.relation.ispartofpageto151398:12
dc.relation.ispartofissue2
dc.relation.ispartofjournalInternational Journal of Medical Microbiology
dc.relation.ispartofvolume310
dc.subject.fieldofresearchMedical microbiology
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchcode3207
dc.subject.fieldofresearchcode3107
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsVirology
dc.subject.keywordsMyonecrosis
dc.titleThe EngCP endo alpha-N-acetylgalactosaminidase is a virulence factor involved in Clostridium perfringens gas gangrene infections
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationCheung, JK; Adams, V; D'Souza, D; James, M; Day, CJ; Jennings, MP; Lyras, D; Rood, J, The EngCP endo alpha-N-acetylgalactosaminidase is a virulence factor involved in Clostridium perfringens gas gangrene infections, International Journal of Medical Microbiology, 2020, 310 (2)
dcterms.dateAccepted2019-12-15
dcterms.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.date.updated2020-07-16T03:32:39Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2020 The Authors. Published by Elsevier GmbH. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/BY-NC-ND/4.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited.
gro.hasfulltextFull Text
gro.griffith.authorJennings, Michael P.
gro.griffith.authorDay, Christopher J.


Files in this item

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record