Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/6212
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dc.contributor.authorKamaruzaman I.N.A.en_US
dc.contributor.authorStaton G.J.en_US
dc.contributor.authorAinsworth S.en_US
dc.contributor.authorCarter S.D.en_US
dc.contributor.authorEvans N.J.en_US
dc.date.accessioned2024-07-31T08:52:11Z-
dc.date.available2024-07-31T08:52:11Z-
dc.date.issued2024-01-24-
dc.identifier.issn20762607-
dc.identifier.urihttp://hdl.handle.net/123456789/6212-
dc.descriptionWeb of Scienceen_US
dc.description.abstractLeptospirosis is a zoonotic bacterial disease affecting mammalian species worldwide. Cattle are a major susceptible host; infection with pathogenic Leptospira spp. represents a public health risk and results in reproductive failure and reduced milk yield, causing economic losses. The characterisation of outer membrane proteins (OMPs) from disease-causing bacteria dissects pathogenesis and underpins vaccine development. As most leptospire pathogenesis research has focused on Leptospira interrogans, this study aimed to characterise novel OMPs from another important genomospecies, Leptospira borgpetersenii, which has global distribution and is relevant to bovine and human diseases. Several putative L. borgpetersenii OMPs were recombinantly expressed, refolded and purified, and evaluated for function and immunogenicity. Two of these unique, putative OMPs (rLBL0972 and rLBL2618) bound to immobilised fibronectin, laminin and fibrinogen, which, together with structural and functional data, supports their classification as leptospiral adhesins. A third putative OMP (rLBL0375), did not exhibit saturable adhesion ability but, together with rLBL0972 and the included control, OmpL1, demonstrated significant cattle milk IgG antibody reactivity from infected cows. To dissect leptospire host–pathogen interactions further, we expressed alleles of OmpL1 and a novel multi-specific adhesin, rLBL2618, from a variety of genomospecies and surveyed their adhesion ability, with both proteins exhibiting divergences in extracellular matrix component binding specificity across synthesised orthologs. We also observed functional redundancy across different L. borgspetersenii OMPs which, together with diversity in function across genomospecies orthologs, delineates multiple levels of plasticity in adhesion that is potentially driven by immune selection and host adaptation. These data identify novel leptospiral proteins which should be further evaluated as vaccine and/or diagnostic candidates. Moreover, functional redundancy across leptospire surface proteins together with identified adhesion divergence across genomospecies further dissect the complex host–pathogen interactions of a genus responsible for substantial global disease burden.en_US
dc.description.sponsorshipBBSRC New Investigator Award (BB/K009443/1)en_US
dc.description.sponsorshipMinistry of Higher Education (MoHE), Malaysia (KTP901108146086)en_US
dc.description.sponsorshipBactiVac Network MR/R005974/1en_US
dc.description.sponsorshipBBSRC Research Grant BB/W016133/1en_US
dc.language.isoenen_US
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)en_US
dc.relation.ispartofMicroorganismen_US
dc.subjectadhesinsen_US
dc.subjectbovine leptospirosisen_US
dc.subjectouter membrane proteinen_US
dc.titleCharacterisation of Putative Outer Membrane Proteins from Leptospira borgpetersenii Serovar Hardjo-Bovis Identifies Novel Adhesins and Diversity in Adhesion across Genomospecies Orthologsen_US
dc.typeInternationalen_US
dc.identifier.doihttps://doi.org/10.3390/microorganisms12020245-
dc.volume12(2)en_US
dc.description.articleno245en_US
dc.date.seminarstartdate2024-01-24-
dc.description.typeArticleen_US
dc.description.impactfactor4.5en_US
dc.description.quartileQ2en_US
dc.contributor.correspondingauthorintanaina@umk.edu.myen_US
item.languageiso639-1en-
item.openairetypeInternational-
item.grantfulltextopen-
item.fulltextWith Fulltext-
crisitem.author.deptUniversity Malaysia Kelantan, Malaysia-
Appears in Collections:Faculty of Veterinary Medicine - Journal (Scopus/WOS)
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