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dc.contributor.authorLin, Chi-Hung
dc.contributor.authorPeterson, Robyn A
dc.contributor.authorGueniche, Audrey
dc.contributor.authorde Beaumais, Segolene Adam
dc.contributor.authorHourblin, Virginie
dc.contributor.authorBreton, Lionel
dc.contributor.authorDalko, Maria
dc.contributor.authorPacker, Nicolle H
dc.date.accessioned2019-08-29T06:12:53Z
dc.date.available2019-08-29T06:12:53Z
dc.date.issued2019
dc.identifier.issn0944-5013
dc.identifier.doi10.1016/j.micres.2018.12.007
dc.identifier.urihttp://hdl.handle.net/10072/386791
dc.description.abstractSweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection. We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose. A fluorescent plate assay was used to determine whether glycans on sweat proteins provide binding epitopes for odour-producing skin commensals Staphylococcus epidermidis and Corynebacterium. Sialic acid and fucose were found to be important binding epitopes for S. epidermidis 3-22-BD-6, a strain recently isolated from human sweat, whereas fucose (but not sialic acid) contributed to the binding of Type strain S. epidermidis ATCC 12228. In contrast, our results indicate that sweat N-glycans do not provide binding epitopes for Corynebacterium. Synthetic sugar mimics of Lewis blood group antigens were investigated as potential inhibitors of the binding of S. epidermidis 3-22-BD-6 to sweat. Pre-incubation of the bacterium with LeB, LeX, LeY and sLeX (pentaose) resulted in a significant reduction in sweat protein adhesion indicating that terminal fucose is a key binding epitope, particularly when linked to a Type 2 chain (Galβ1-4GlcNAc) configuration (LeY). Our results form an impetus for future studies seeking to elucidate the role of glycans in sweat associated malodour, with possible implications for cosmetic and medical fields.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom53
dc.relation.ispartofpageto60
dc.relation.ispartofjournalMicrobiological Research
dc.relation.ispartofvolume220
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchMedical Microbiology
dc.subject.fieldofresearchcode0605
dc.subject.fieldofresearchcode1108
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsMicrobiology
dc.subject.keywordsSweat
dc.subject.keywordsGlycan
dc.titleDifferential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationLin, C-H; Peterson, RA; Gueniche, A; de Beaumais, SA; Hourblin, V; Breton, L; Dalko, M; Packer, NH, Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat, Microbiological Research, 2019, 220, pp. 53-60
dcterms.dateAccepted2018-12-28
dcterms.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.date.updated2019-08-29T06:00:18Z
dc.description.versionAccepted Manuscript (AM)
gro.rights.copyright© 2019 Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International Licence (http://creativecommons.org/licenses/by-nc-nd/4.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited.
gro.hasfulltextFull Text
gro.griffith.authorLin, Chi-Hung
gro.griffith.authorPacker, Nicki


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