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dc.contributor.authorAtack, John M
dc.contributor.authorDay, Christopher J
dc.contributor.authorPoole, Jessica
dc.contributor.authorBrockman, Kenneth L
dc.contributor.authorBakaletz, Lauren O
dc.contributor.authorBarenkamp, Stephen J
dc.contributor.authorJennings, Michael P
dc.date.accessioned2019-07-04T12:41:19Z
dc.date.available2019-07-04T12:41:19Z
dc.date.issued2018
dc.identifier.issn0006-291X
dc.identifier.doi10.1016/j.bbrc.2018.06.126
dc.identifier.urihttp://hdl.handle.net/10072/381692
dc.description.abstractNon-typeable Haemophilus influenzae (NTHi) is a human-adapted bacterial pathogen, responsible for infections of the human respiratory tract. This pathogen expresses a range of adhesins that mediate binding to host cells. Most NTHi strains can express the related adhesins HMW1 and HMW2. Expression of HMW proteins is phase-variable: changes in the length of simple-sequence repeats located in the encoding genes promoter regions results in changes in expression levels of these adhesins. HMW expression is also controlled by epigenetic regulation. HMW1 has been previously demonstrated to bind α 2–3 sialyl-lactosamine, but affinity of this interaction has not been investigated. The host receptor(s) for HMW2 is currently unknown. We hypothesized that host glycans may act as receptors for HMW2-mediated adherence. We examined the glycan-binding activity of HMW2 using glycan arrays and Surface Plasmon Resonance (SPR). These studies demonstrate that HMW2 binds 2–6 linked N-acetylneuraminic acid with high affinity. HMW2 did not bind glycan structures containing the non-human form of sialic acid, N-glycolylneuraminic acid. Thus, the specificity of HMW1 and HMW2 have complementary lectin activities that may allow NTHi distinct niches in the human host.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeUnited Kingdom
dc.relation.ispartofpagefrom1103
dc.relation.ispartofpageto1107
dc.relation.ispartofissue2
dc.relation.ispartofjournalBiochemical and Biophysical Research Communications
dc.relation.ispartofvolume503
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics not elsewhere classified
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics
dc.subject.fieldofresearchcode110199
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0601
dc.subject.fieldofresearchcode1101
dc.subject.keywordsHaemophilus influenzae
dc.subject.keywordsHuman respiratory tract
dc.subject.keywordsHost cells
dc.subject.keywordsProteins
dc.subject.keywordsGlycans
dc.titleThe HMW2 adhesin of non-typeable Haemophilus influenzae is a human-adapted lectin that mediates high-affinity binding to 2-6 linked N-acetylneuraminic acid glycans
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomics
gro.hasfulltextNo Full Text
gro.griffith.authorJennings, Michael P.
gro.griffith.authorDay, Christopher J.
gro.griffith.authorAtack, John M.
gro.griffith.authorPoole, Jessica


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