Effects of tunicamycin on glycoprotein antigens of Aspergillus fumigatus

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorHearn, Veronica M.
dc.creatorShimizu, M.
dc.date2014-05-27T11:18:09Z
dc.date2016-10-25T18:14:09Z
dc.date2014-05-27T11:18:09Z
dc.date2016-10-25T18:14:09Z
dc.date1996-12-01
dc.date.accessioned2017-04-06T00:48:27Z
dc.date.available2017-04-06T00:48:27Z
dc.identifierMicrobios, v. 85, n. 345, p. 239-250, 1996.
dc.identifier0026-2633
dc.identifierhttp://hdl.handle.net/11449/64943
dc.identifierhttp://acervodigital.unesp.br/handle/11449/64943
dc.identifier2-s2.0-0029704305
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/8699966
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/886712
dc.descriptionTunicamycin, 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.
dc.languageeng
dc.relationMicrobios
dc.rightsinfo:eu-repo/semantics/closedAccess
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 fumigatus
dc.typeOtro


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