A new Paracoccidioides brasiliensis 70-kDa heat shock protein reacts with sera from paracoccidioidomycosis patients
A cDNA coding for a new member of the 70-kDa heat shock proteins (HSP70) family from the dimorphic and pathogenic fungus, Paracoccidioides brasiliensis, was cloned and characterized. The cDNA-deduced sequence coded for 655-amino acid residues and showed 95% identity to a previously described P. bras...
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| Veröffentlicht in: | Medical mycology (Oxford) 2005-09, Vol.43 (6), p.495-503 |
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| creator | Bisio, Laura C. Silva, Silvana P. Pereira, Ildinete Silva Xavier, Mauro A. S. Venâncio, Emerson J Puccia, Rosana Soares, Célia M. A. Felipe, Maria Sueli S. |
| description | A cDNA coding for a new member of the 70-kDa heat shock proteins (HSP70) family from the dimorphic and pathogenic fungus, Paracoccidioides brasiliensis, was cloned and characterized. The cDNA-deduced sequence coded for 655-amino acid residues and showed 95% identity to a previously described P. brasiliensishsp70 gene. Cytoplasmic and typical nuclear localization signals, which indicate induction upon stress, were identified in the deduced peptide. The complete hsp70 cDNA coding region was cloned into a pGEX 4T-3 plasmid and expressed in Escherichia coli as a glutathione-S-transferase-tagged fusion protein. The recombinant protein reacted with a rabbit polyclonal antibody against HSP70. Western immunoblot experiments demonstrated that sera from paracoccidioidomycosis patients recognized the purified recombinant protein, suggesting an immunological role for this protein in the infectious process. The antigenicity analysis of rHSP70 detected three internal peptides that could act as activators of T-cell proliferation. |
| doi_str_mv | 10.1080/13693780400029478 |
| format | Article |
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The recombinant protein reacted with a rabbit polyclonal antibody against HSP70. Western immunoblot experiments demonstrated that sera from paracoccidioidomycosis patients recognized the purified recombinant protein, suggesting an immunological role for this protein in the infectious process. The antigenicity analysis of rHSP70 detected three internal peptides that could act as activators of T-cell proliferation.</description><identifier>ISSN: 1369-3786</identifier><identifier>EISSN: 1460-2709</identifier><identifier>DOI: 10.1080/13693780400029478</identifier><identifier>PMID: 16320493</identifier><language>eng</language><publisher>UK: Informa UK Ltd</publisher><subject>Amino Acid Sequence ; Antibodies, Fungal - blood ; Antigens, Fungal - chemistry ; Antigens, Fungal - genetics ; Antigens, Fungal - immunology ; Base Sequence ; Escherichia coli ; HSP70 Heat-Shock Proteins - chemistry ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - immunology ; Humans ; Immunoblotting ; Molecular Sequence Data ; Paracoccidioides - immunology ; Paracoccidioides - metabolism ; Paracoccidioides brasiliensis ; Paracoccidioidomycosis - blood ; Paracoccidioidomycosis - immunology ; Protein Structure, Secondary ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Fungal - chemistry ; RNA, Fungal - genetics ; Sequence Alignment ; Sequence Analysis, DNA ; Surface Properties</subject><ispartof>Medical mycology (Oxford), 2005-09, Vol.43 (6), p.495-503</ispartof><rights>2005 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 2005</rights><rights>2005 ISHAM 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-68911c18ed526abefd5e21b200eb5c9346b451879516e19745ac06becb2d54e93</citedby><cites>FETCH-LOGICAL-c380t-68911c18ed526abefd5e21b200eb5c9346b451879516e19745ac06becb2d54e93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/13693780400029478$$EPDF$$P50$$Ginformahealthcare$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/13693780400029478$$EHTML$$P50$$Ginformahealthcare$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,61194,61375</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16320493$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bisio, Laura C.</creatorcontrib><creatorcontrib>Silva, Silvana P.</creatorcontrib><creatorcontrib>Pereira, Ildinete Silva</creatorcontrib><creatorcontrib>Xavier, Mauro A. 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The complete hsp70 cDNA coding region was cloned into a pGEX 4T-3 plasmid and expressed in Escherichia coli as a glutathione-S-transferase-tagged fusion protein. The recombinant protein reacted with a rabbit polyclonal antibody against HSP70. Western immunoblot experiments demonstrated that sera from paracoccidioidomycosis patients recognized the purified recombinant protein, suggesting an immunological role for this protein in the infectious process. 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| identifier | ISSN: 1369-3786 |
| ispartof | Medical mycology (Oxford), 2005-09, Vol.43 (6), p.495-503 |
| issn | 1369-3786 1460-2709 |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Taylor & Francis Journals Complete |
| subjects | Amino Acid Sequence Antibodies, Fungal - blood Antigens, Fungal - chemistry Antigens, Fungal - genetics Antigens, Fungal - immunology Base Sequence Escherichia coli HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - immunology Humans Immunoblotting Molecular Sequence Data Paracoccidioides - immunology Paracoccidioides - metabolism Paracoccidioides brasiliensis Paracoccidioidomycosis - blood Paracoccidioidomycosis - immunology Protein Structure, Secondary Recombinant Proteins - genetics Recombinant Proteins - immunology Reverse Transcriptase Polymerase Chain Reaction RNA, Fungal - chemistry RNA, Fungal - genetics Sequence Alignment Sequence Analysis, DNA Surface Properties |
| title | A new Paracoccidioides brasiliensis 70-kDa heat shock protein reacts with sera from paracoccidioidomycosis patients |
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