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dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorWohlschlager, Thereseen_US
dc.contributor.authorTiralongo, Evelinen_US
dc.contributor.authorKiefel, Miltonen_US
dc.date.accessioned2017-04-24T11:32:12Z
dc.date.available2017-04-24T11:32:12Z
dc.date.issued2009en_US
dc.date.modified2010-09-01T08:06:59Z
dc.identifier.issn13500872en_US
dc.identifier.doi10.1099/mic.0.026997-0en_AU
dc.identifier.urihttp://hdl.handle.net/10072/30107
dc.description.abstractInfection by Aspergillus fumigatus, which causes the life-threatening disease invasive aspergillosis, begins with the inhalation of conidia that adhere to and germinate in the lung. Previous studies have shown that A. fumigatus conidia express high levels of the negatively charged 9-carbon sugar sialic acid, and that sialic acid appears to mediate the binding of A. fumigatus conidia to basal lamina proteins. However, despite the ability of sialic acid to inhibit adherence of A. fumigatus conidia, the exact mechanism by which this binding occurs remains unresolved. Utilizing various free sialic acids and other carbohydrates, sialic acid derivatives, sialoglycoconjugates, glycoproteins, -keto acid related compounds and amino acids we have found that the binding of A. fumigatus conidia to type IV collagen and fibrinogen was inhibited by (i) glycoproteins (in a sialic acid-independent manner), and (ii) free sialic acids, glucuronic acid and -keto acid related compounds. However, inhibition by the latter was found to be the result of a shift in pH from neutral (pH 7.4) to acidic (less than pH 4.6) induced by the relatively high concentrations of free sialic acids, glucuronic acid and -keto acid related compounds used in the binding assays. This suggests that previous reports describing inhibition of A. fumigatus conidia binding by free sialic acid may actually be due to a pH shift similar to that shown here. As previously reported, we found that A. fumigatus conidia express only N-acetylneuraminic acid, the most common sialic acid found in nature. However, A. fumigatus appears to do so by an alternative mechanism to that seen in other organisms. We report here that A. fumigatus (i) does not incorporate sialic acid obtained from the environment, (ii) does not synthesize and incorporate sialic acid from exogenous N-acetylmannosamine, and (iii) lacks homologues of known sialic acid biosynthesizing enzymes.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.format.extent1042117 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherThe Society for General Microbiologyen_US
dc.publisher.placeUKen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom3100en_US
dc.relation.ispartofpageto3109en_US
dc.relation.ispartofissue9en_US
dc.relation.ispartofjournalMicrobiologyen_US
dc.relation.ispartofvolume155en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchMycologyen_US
dc.subject.fieldofresearchMedical Biochemistry: Carbohydratesen_US
dc.subject.fieldofresearchcode060505en_US
dc.subject.fieldofresearchcode110102en_US
dc.titleInhibition of Aspergillus fumigatus conidia binding to extracellular matrix proteins by sialic acids: a pH effect?en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.rights.copyrightCopyright 2009 Society for General Microbiology (SGM). This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal website for access to the definitive, published version.en_AU
gro.date.issued2009
gro.hasfulltextFull Text


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