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dc.contributor.authorZhang, Hengen_NZ
dc.contributor.authorBurrows, J.en_NZ
dc.contributor.authorCard, G.en_NZ
dc.contributor.authorAttwood, Graeme T.en_NZ
dc.contributor.authorWheeler, Thomas T.en_NZ
dc.contributor.authorArcus, Vickery L.en_NZ
dc.date.accessioned2019-11-01T01:34:49Z
dc.date.available2019en_NZ
dc.date.available2019-11-01T01:34:49Z
dc.date.issued2019en_NZ
dc.identifier.citationZhang, H., Burrows, J., Card, G., Attwood, G. T., Wheeler, T. T., & Arcus, V. L. (2019). The three dimensional structure of Bovine Salivary Protein 30b (BSP30b) and its interaction with specific rumen bacteria. PLOS One, 14(4). https://doi.org/10.1371/journal.pone.0206709en
dc.identifier.issn1932-6203en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/13075
dc.description.abstractBovine Salivary Protein 30b (BSP30b) is a member of the tubular lipid-binding (TULIP) superfamily that includes the human bactericidal/permeability-increasing proteins (BPI), lipopolysaccharide binding proteins (LBP) and palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNC). BSP30b is most closely related to the PLUNC family and is predominantly found in bovine saliva. There are four BSP30 isoforms (BSP30a-d) and collectively, they are the most abundant protein component of bovine saliva. The PLUNC family members are proposed to be lipid binding proteins, although in most cases their lipid ligands are unknown. Here, we present the X-ray crystal structure of BSP30b at 2.0 Å resolution. We used a double methionine mutant and Se-Met SAD phasing to solve the structure. The structure adopts a curved cylindrical form with a hydrophobic channel formed by an α/β wrap, which is consistent with the TULIP superfamily. The structure of BSP30b in complex with oleic acid is also presented where the ligand is accommodated within the hydrophobic channel. The electron density for oleic acid suggests that the ligand is only partially occupied in the binding site implying that oleic acid may not be the preferred ligand. GFP-tagged BSP30b binds to the surface of olive oil droplets, as observed under fluorescent microscopy, and acts as a surfactant consistent with its association with decreased susceptibility to bloat in cattle. Bacteria extracted directly from bovine rumen contents indicate that the GFP_BSP30b fusion protein binds to a small number of selected bacterial species in vivo. These results suggest that BSP30b may bind to bacterial lipids from specific species and that this abundant protein may have important biological roles via interacting with rumen bacteria during feeding and rumination.
dc.format.mimetypeapplication/pdf
dc.language.isoenen_NZ
dc.publisherPublic Library of Scienceen_NZ
dc.rights© 2019 Zhang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.subjectScience & Technologyen_NZ
dc.subjectMultidisciplinary Sciencesen_NZ
dc.subjectScience & Technology - Other Topicsen_NZ
dc.subjectNasal Lavage fluiden_NZ
dc.subjectBPIen_NZ
dc.subjectCattleen_NZ
dc.subjectPluncen_NZ
dc.subjectSuperfamilyen_NZ
dc.subjectExpressionen_NZ
dc.subjectSoftwareen_NZ
dc.subjectSplunc1en_NZ
dc.subjectBloaten_NZ
dc.titleThe three dimensional structure of Bovine Salivary Protein 30b (BSP30b) and its interaction with specific rumen bacteriaen_NZ
dc.typeJournal Article
dc.identifier.doi10.1371/journal.pone.0206709en_NZ
dc.relation.isPartOfPLOS Oneen_NZ
pubs.elements-id236945
pubs.issue4en_NZ
pubs.publication-statusPublisheden_NZ
pubs.volume14en_NZ
uow.identifier.article-noARTN e0206709


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