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dc.contributor.authorSmeesters, Pierre R
dc.contributor.authorMcMillan, David J
dc.contributor.authorSriprakash, Kadaba S
dc.date.accessioned2017-05-03T11:48:40Z
dc.date.available2017-05-03T11:48:40Z
dc.date.issued2010
dc.date.modified2011-02-23T08:56:16Z
dc.identifier.issn0966-842X
dc.identifier.doi10.1016/j.tim.2010.02.007
dc.identifier.urihttp://hdl.handle.net/10072/36507
dc.description.abstractInteraction of the M-protein of group A Streptococcus (GAS) with its numerous host binding partners might assist the bacteria in evading host immune responses. Although the extensive diversity of this protein has been highlighted by different GAS typing schemes, most of the structural and functional information has been obtained from a limited number of types. Increasing numbers of epidemiological, clinical and biological reports suggest that the structure and function of the M protein is less conserved than previously thought. This review focuses on the known interactions between M proteins and host ligand proteins, emphasizing that our understanding of this well-studied molecule is fragmented.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_AU
dc.publisherElsevier
dc.publisher.placeUnited Kingdom
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom275
dc.relation.ispartofpageto282
dc.relation.ispartofissue6
dc.relation.ispartofjournalTrends in Microbiology
dc.relation.ispartofvolume18
dc.rights.retentionY
dc.subject.fieldofresearchMedical Microbiology not elsewhere classified
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchMedical Microbiology
dc.subject.fieldofresearchcode110899
dc.subject.fieldofresearchcode0605
dc.subject.fieldofresearchcode1108
dc.titleThe streptococcal M protein: a highly versatile molecule
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2010
gro.hasfulltextNo Full Text
gro.griffith.authorMcMillan, David J.
gro.griffith.authorSriprakash, Kadaba S.


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