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dc.contributor.authorSmeesters, Pierre R.en_US
dc.contributor.authorMcMillan, Daviden_US
dc.contributor.authorSriprakash, Kadabaen_US
dc.date.accessioned2017-05-03T11:48:40Z
dc.date.available2017-05-03T11:48:40Z
dc.date.issued2010en_US
dc.date.modified2011-02-23T08:56:16Z
dc.identifier.issn1878-4380en_US
dc.identifier.doi10.1016/j.tim.2010.02.007en_AU
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.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom275en_US
dc.relation.ispartofpageto282en_US
dc.relation.ispartofissue6en_US
dc.relation.ispartofjournalTrends in Microbiologyen_US
dc.relation.ispartofvolume18en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchMedical Microbiology not elsewhere classifieden_US
dc.subject.fieldofresearchcode110899en_US
dc.titleThe streptococcal M protein: a highly versatile moleculeen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2010
gro.hasfulltextNo Full Text


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