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dc.contributor.authorGeorgousakis, Melina M
dc.contributor.authorHofmann, Andreas
dc.contributor.authorBatzloff, Michael R
dc.contributor.authorMcMillan, David J
dc.contributor.authorSriprakash, Kadaba S
dc.date.accessioned2017-05-03T15:19:44Z
dc.date.available2017-05-03T15:19:44Z
dc.date.issued2009
dc.date.modified2010-12-07T02:55:47Z
dc.identifier.issn0264-410X
dc.identifier.doi10.1016/j.vaccine.2009.08.049
dc.identifier.urihttp://hdl.handle.net/10072/29553
dc.description.abstractA conformationally restricted B cell epitope has been identified as a potential safe vaccine candidate from the major group A streptococcal virulence factor, the M protein. To maintain -helical secondary structure, the minimal epitope is flanked with heterologous sequences to produce the chimeric vaccine candidate called J14. As a strategy toward developing an affordable multivalent GAS vaccine, we have expressed J14 recombinantly with a second GAS protective antigen H12 (rJ14H12).Whenadministered to mice sub-cutaneously, the fusion protein stimulated a strong serum IgG response to the H12 component, but J14 was poorly immunogenic. To increase the immunogenicity of J14 when expressed with the model fusion partner, amino acid modifications were made to the initial recombinant J14 construct to produce rJJo. These changes stabilised the -helical conformation of the recombinant antigen as assessed by circular dichroism. Mice immunised with rJJoH12, the fusion protein incorporating JJo, effectively stimulated a humoral response to both of the included antigens. These data support the feasibility of developing a multivalent vaccine incorporating the conformationally restricted protective antigen J14.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent179403 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeNetherlands
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofpagefrom6799
dc.relation.ispartofpageto6806
dc.relation.ispartofjournalVaccine
dc.relation.ispartofvolume27
dc.rights.retentionY
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchAgricultural, veterinary and food sciences
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchMedical biochemistry - proteins and peptides (incl. medical proteomics)
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode30
dc.subject.fieldofresearchcode32
dc.subject.fieldofresearchcode320506
dc.titleStructural optimisation of a conformational epitope improves antigenicity when expressed as a recombinant fusion protein
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2009 Elsevier. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
gro.date.issued2009
gro.hasfulltextFull Text
gro.griffith.authorHofmann, Andreas
gro.griffith.authorMcMillan, David J.
gro.griffith.authorSriprakash, Kadaba S.


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