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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/64943
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dc.contributor.authorHearn, Veronica M.-
dc.contributor.authorShimizu, M.-
dc.date.accessioned2014-05-27T11:18:09Z-
dc.date.accessioned2016-10-25T18:14:09Z-
dc.date.available2014-05-27T11:18:09Z-
dc.date.available2016-10-25T18:14:09Z-
dc.date.issued1996-12-01-
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/8699966-
dc.identifier.citationMicrobios, v. 85, n. 345, p. 239-250, 1996.-
dc.identifier.issn0026-2633-
dc.identifier.urihttp://hdl.handle.net/11449/64943-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/64943-
dc.description.abstractTunicamycin, which inhibits N-glycosylation of proteins, was used as a tool to determine the type of linkage which occurs in glycoprotein antigens of Aspergillus fumigatus. When A. fumigatus extracts were electrophoretically separated and blotted then probed with anti-Aspergillus patients' sera, differences in antigenic profiles were noted when tunicamycin-treated samples were compared with controls. Tunicamycin had no detectable effect on the cellular proteinases of A. fumigatus, most of which are glycosylated. Some enzymatic components were lacking when extracellular proteinases were compared with those of control samples. The major catalase component of A. fumigatus is a concanavalin A (Con A)-binding glycoprotein. In cultures grown in the presence of tunicamycin, partiallydeglycosylated catalase components were obtained which could be distinguished from the native catalase by their altered mobilities in polyacrylamide gels. The effect of deglycosylation on catalase antigens was monitored using an antiserum raised to a ConA-binding fraction of A fumigatus mycelium. These antibodies bound both to the native glycoprotein and the partially deglycosylated material. These latter two were largely unaffected when incubated with an antiserum raised to a non-ConA-binding fraction of A. fumigatus which is essentially carbohydrate free. The ability to produce partially-glycosylated antigens of A. fumigatus offers a model to study the effect of basic structural modifications on both the enzymatic and antigenic activities of these molecules.en
dc.format.extent239-250-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectAntigens-
dc.subjectAspergillus fumigatus-
dc.subjectEnzymes-
dc.subjectN-glycosylation-
dc.subjectTunicamycin-
dc.subjectantiinfective agent-
dc.subjectcatalase-
dc.subjectfungus antigen-
dc.subjectglycoprotein-
dc.subjectproteinase-
dc.subjecttunicamycin-
dc.subjectanimal-
dc.subjectdrug effect-
dc.subjectenzymology-
dc.subjecthuman-
dc.subjectimmunology-
dc.subjectmetabolism-
dc.subjectpolyacrylamide gel electrophoresis-
dc.subjectrabbit-
dc.subjectAnimals-
dc.subjectAnti-Bacterial Agents-
dc.subjectAntigens, Fungal-
dc.subjectCatalase-
dc.subjectElectrophoresis, Polyacrylamide Gel-
dc.subjectEndopeptidases-
dc.subjectGlycoproteins-
dc.subjectHumans-
dc.subjectRabbits-
dc.titleEffects of tunicamycin on glycoprotein antigens of Aspergillus fumigatusen
dc.typeoutro-
dc.contributor.institutionMycology Reference Laboratory-
dc.contributor.institutionUniversity of Leeds-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationMycology Reference Laboratory, 61 Colindale Avenue, London NW9 5HT-
dc.description.affiliationDepartment of Microbiology University of Leeds, Leeds LS2 9JT, Yorkshire-
dc.description.affiliationUniversidade Estadual Paulista Faculdade de Odontologia Campus de Sao Jose Dos Campos, C. P. 314 Sao Jose Dos Campos, Estado de Sao Paulo-
dc.description.affiliationUnespUniversidade Estadual Paulista Faculdade de Odontologia Campus de Sao Jose Dos Campos, C. P. 314 Sao Jose Dos Campos, Estado de Sao Paulo-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofMicrobios-
dc.identifier.scopus2-s2.0-0029704305-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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