Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis

Aspergillus species are common airborne fungi that have been identified as causative agents of extrinsic bronchial asthma. More than 10 allergens from A. fumigatus have been recently characterized by cDNA cloning. The objective of this study is to identify A. fumigatus allergens through immunoblot a...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Clinical and experimental allergy 2001-02, Vol.31 (2), p.295-302
Hauptverfasser: Shen, H.-D., Lin, W.-L., Tam, M. F., Chou, H., Wang, C.-W., Tsai, J.-J., Wang, S.-R., Han, S.-H.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 302
container_issue 2
container_start_page 295
container_title Clinical and experimental allergy
container_volume 31
creator Shen, H.-D.
Lin, W.-L.
Tam, M. F.
Chou, H.
Wang, C.-W.
Tsai, J.-J.
Wang, S.-R.
Han, S.-H.
description Aspergillus species are common airborne fungi that have been identified as causative agents of extrinsic bronchial asthma. More than 10 allergens from A. fumigatus have been recently characterized by cDNA cloning. The objective of this study is to identify A. fumigatus allergens through immunoblot analysis using sera from asthmatic patients. IgE‐binding components of A. fumigatus and IgE cross‐reactivity among allergens of different prevalent airborne fungal species were analysed by immunoblot and immunoblot inhibition, respectively, using sera from asthmatic patients. The N‐terminal amino acid sequences of major allergens identified were determined by Edman degradation. Among two batches (70 and 41 sera) of asthmatic sera tested, 19 (27%) and 14 (34%), respectively, have IgE immunoblot reactivity towards components of A. fumigatus. A 34‐kDa protein that reacts with IgE antibodies in 15 (79%) and 11 (79%) of the 19 and 14 positive samples, respectively, may be considered a major allergen of A. fumigatus. The N‐terminal amino acid sequences of the 34 kDa major allergen and the 30.5 and 30 kDa IgE‐binding components of A. fumigatus showed sequence identity to that of the vacuolar serine proteinase from A. fumigatus. The results from immunoblot inhibition show IgE cross‐reactivity among major allergens of A. fumigatus, P. notatum and P. oxalicum. Results obtained suggest that the 34 kDa major allergen of A. fumigatus may be a vacuolar serine proteinase. There is IgE cross‐reactivity among serine proteinase allergens of A. fumigatus, P. notatum and P. oxalicum.
doi_str_mv 10.1046/j.1365-2222.2001.01026.x
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76972972</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17895719</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5556-438ebd626a1fb9ee05a0c6bf4ff051216cbc61e9233a2eb93a0fec87b07389a63</originalsourceid><addsrcrecordid>eNqNkcGO0zAQhiMEYsvCKyALJG4JdlI78YFDVZayUrUcWMTRmrjjysWJi51A-yS8Ls62KhIXsCzNSPP9Mx7_WUYYLRidi7e7glWC52U6RUkpKyijpSgOj7LZpfA4m1HJ53ndyPlV9izGHaW04rJ5ml0xVnImKjbLft1usB-ssRoG63viDfkBevQOAokYbI9kH_yAtoeIBCIB0sHOBwLOYdjig2IR9ym3zo2RmLGzWxhS1h6J7bqx963zw2D7LYF-Q-7yAUOX2jkCKXgC2m7SqO8j9jpNSIVjtPF59sSAi_jiHK-zLx9u7pcf8_Wn1e1ysc4151zk86rBdiNKAcy0EpFyoFq0Zm4M5axkQrdaMJRlVUGJrayAGtRN3dK6aiSI6jp7c-qbtkxPiIPqbNToHPTox6hqIesy3X-CLP0zr5lM4Ku_wJ0fQ1orMVJKWjdsGtucIB18jAGN2gfbQTgqRtVksdqpyUk1Oakmi9WDxeqQpC_P_ce2w80f4dnTBLw-AxA1OBOg1zZeOFlTQZtEvTtRP63D43-PV8ubxZQlfX7S2zjg4aKH8E2Juqq5-nq3Uqu1vC_ff2ap2W8af9Lw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>199907816</pqid></control><display><type>article</type><title>Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Shen, H.-D. ; Lin, W.-L. ; Tam, M. F. ; Chou, H. ; Wang, C.-W. ; Tsai, J.-J. ; Wang, S.-R. ; Han, S.-H.</creator><creatorcontrib>Shen, H.-D. ; Lin, W.-L. ; Tam, M. F. ; Chou, H. ; Wang, C.-W. ; Tsai, J.-J. ; Wang, S.-R. ; Han, S.-H.</creatorcontrib><description>Aspergillus species are common airborne fungi that have been identified as causative agents of extrinsic bronchial asthma. More than 10 allergens from A. fumigatus have been recently characterized by cDNA cloning. The objective of this study is to identify A. fumigatus allergens through immunoblot analysis using sera from asthmatic patients. IgE‐binding components of A. fumigatus and IgE cross‐reactivity among allergens of different prevalent airborne fungal species were analysed by immunoblot and immunoblot inhibition, respectively, using sera from asthmatic patients. The N‐terminal amino acid sequences of major allergens identified were determined by Edman degradation. Among two batches (70 and 41 sera) of asthmatic sera tested, 19 (27%) and 14 (34%), respectively, have IgE immunoblot reactivity towards components of A. fumigatus. A 34‐kDa protein that reacts with IgE antibodies in 15 (79%) and 11 (79%) of the 19 and 14 positive samples, respectively, may be considered a major allergen of A. fumigatus. The N‐terminal amino acid sequences of the 34 kDa major allergen and the 30.5 and 30 kDa IgE‐binding components of A. fumigatus showed sequence identity to that of the vacuolar serine proteinase from A. fumigatus. The results from immunoblot inhibition show IgE cross‐reactivity among major allergens of A. fumigatus, P. notatum and P. oxalicum. Results obtained suggest that the 34 kDa major allergen of A. fumigatus may be a vacuolar serine proteinase. There is IgE cross‐reactivity among serine proteinase allergens of A. fumigatus, P. notatum and P. oxalicum.</description><identifier>ISSN: 0954-7894</identifier><identifier>EISSN: 1365-2222</identifier><identifier>DOI: 10.1046/j.1365-2222.2001.01026.x</identifier><identifier>PMID: 11251631</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science, Ltd</publisher><subject>A. fumigatus ; Adolescent ; Adult ; Aged ; allergens ; Allergens - chemistry ; Allergens - immunology ; Allergic diseases ; Antigens, Fungal - chemistry ; Antigens, Fungal - immunology ; Aspergillus fumigatus ; Aspergillus fumigatus - enzymology ; Aspergillus fumigatus - immunology ; Asthma - immunology ; Biological and medical sciences ; Cross Reactions ; Electrophoresis, Gel, Two-Dimensional ; Humans ; immunoblot ; Immunoblotting ; Immunoglobulin E - immunology ; Immunopathology ; Medical sciences ; Middle Aged ; N-terminal amino acid sequence ; Penicillium - immunology ; Respiratory and ent allergic diseases ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - immunology ; Vacuoles - enzymology</subject><ispartof>Clinical and experimental allergy, 2001-02, Vol.31 (2), p.295-302</ispartof><rights>2001 INIST-CNRS</rights><rights>Copyright Blackwell Scientific Publications Ltd. Feb 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5556-438ebd626a1fb9ee05a0c6bf4ff051216cbc61e9233a2eb93a0fec87b07389a63</citedby><cites>FETCH-LOGICAL-c5556-438ebd626a1fb9ee05a0c6bf4ff051216cbc61e9233a2eb93a0fec87b07389a63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1365-2222.2001.01026.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-2222.2001.01026.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=970608$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11251631$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shen, H.-D.</creatorcontrib><creatorcontrib>Lin, W.-L.</creatorcontrib><creatorcontrib>Tam, M. F.</creatorcontrib><creatorcontrib>Chou, H.</creatorcontrib><creatorcontrib>Wang, C.-W.</creatorcontrib><creatorcontrib>Tsai, J.-J.</creatorcontrib><creatorcontrib>Wang, S.-R.</creatorcontrib><creatorcontrib>Han, S.-H.</creatorcontrib><title>Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis</title><title>Clinical and experimental allergy</title><addtitle>Clin Exp Allergy</addtitle><description>Aspergillus species are common airborne fungi that have been identified as causative agents of extrinsic bronchial asthma. More than 10 allergens from A. fumigatus have been recently characterized by cDNA cloning. The objective of this study is to identify A. fumigatus allergens through immunoblot analysis using sera from asthmatic patients. IgE‐binding components of A. fumigatus and IgE cross‐reactivity among allergens of different prevalent airborne fungal species were analysed by immunoblot and immunoblot inhibition, respectively, using sera from asthmatic patients. The N‐terminal amino acid sequences of major allergens identified were determined by Edman degradation. Among two batches (70 and 41 sera) of asthmatic sera tested, 19 (27%) and 14 (34%), respectively, have IgE immunoblot reactivity towards components of A. fumigatus. A 34‐kDa protein that reacts with IgE antibodies in 15 (79%) and 11 (79%) of the 19 and 14 positive samples, respectively, may be considered a major allergen of A. fumigatus. The N‐terminal amino acid sequences of the 34 kDa major allergen and the 30.5 and 30 kDa IgE‐binding components of A. fumigatus showed sequence identity to that of the vacuolar serine proteinase from A. fumigatus. The results from immunoblot inhibition show IgE cross‐reactivity among major allergens of A. fumigatus, P. notatum and P. oxalicum. Results obtained suggest that the 34 kDa major allergen of A. fumigatus may be a vacuolar serine proteinase. There is IgE cross‐reactivity among serine proteinase allergens of A. fumigatus, P. notatum and P. oxalicum.</description><subject>A. fumigatus</subject><subject>Adolescent</subject><subject>Adult</subject><subject>Aged</subject><subject>allergens</subject><subject>Allergens - chemistry</subject><subject>Allergens - immunology</subject><subject>Allergic diseases</subject><subject>Antigens, Fungal - chemistry</subject><subject>Antigens, Fungal - immunology</subject><subject>Aspergillus fumigatus</subject><subject>Aspergillus fumigatus - enzymology</subject><subject>Aspergillus fumigatus - immunology</subject><subject>Asthma - immunology</subject><subject>Biological and medical sciences</subject><subject>Cross Reactions</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Humans</subject><subject>immunoblot</subject><subject>Immunoblotting</subject><subject>Immunoglobulin E - immunology</subject><subject>Immunopathology</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>N-terminal amino acid sequence</subject><subject>Penicillium - immunology</subject><subject>Respiratory and ent allergic diseases</subject><subject>Sequence Analysis, Protein</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - immunology</subject><subject>Vacuoles - enzymology</subject><issn>0954-7894</issn><issn>1365-2222</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcGO0zAQhiMEYsvCKyALJG4JdlI78YFDVZayUrUcWMTRmrjjysWJi51A-yS8Ls62KhIXsCzNSPP9Mx7_WUYYLRidi7e7glWC52U6RUkpKyijpSgOj7LZpfA4m1HJ53ndyPlV9izGHaW04rJ5ml0xVnImKjbLft1usB-ssRoG63viDfkBevQOAokYbI9kH_yAtoeIBCIB0sHOBwLOYdjig2IR9ym3zo2RmLGzWxhS1h6J7bqx963zw2D7LYF-Q-7yAUOX2jkCKXgC2m7SqO8j9jpNSIVjtPF59sSAi_jiHK-zLx9u7pcf8_Wn1e1ysc4151zk86rBdiNKAcy0EpFyoFq0Zm4M5axkQrdaMJRlVUGJrayAGtRN3dK6aiSI6jp7c-qbtkxPiIPqbNToHPTox6hqIesy3X-CLP0zr5lM4Ku_wJ0fQ1orMVJKWjdsGtucIB18jAGN2gfbQTgqRtVksdqpyUk1Oakmi9WDxeqQpC_P_ce2w80f4dnTBLw-AxA1OBOg1zZeOFlTQZtEvTtRP63D43-PV8ubxZQlfX7S2zjg4aKH8E2Juqq5-nq3Uqu1vC_ff2ap2W8af9Lw</recordid><startdate>200102</startdate><enddate>200102</enddate><creator>Shen, H.-D.</creator><creator>Lin, W.-L.</creator><creator>Tam, M. F.</creator><creator>Chou, H.</creator><creator>Wang, C.-W.</creator><creator>Tsai, J.-J.</creator><creator>Wang, S.-R.</creator><creator>Han, S.-H.</creator><general>Blackwell Science, Ltd</general><general>Blackwell</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>200102</creationdate><title>Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis</title><author>Shen, H.-D. ; Lin, W.-L. ; Tam, M. F. ; Chou, H. ; Wang, C.-W. ; Tsai, J.-J. ; Wang, S.-R. ; Han, S.-H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5556-438ebd626a1fb9ee05a0c6bf4ff051216cbc61e9233a2eb93a0fec87b07389a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>A. fumigatus</topic><topic>Adolescent</topic><topic>Adult</topic><topic>Aged</topic><topic>allergens</topic><topic>Allergens - chemistry</topic><topic>Allergens - immunology</topic><topic>Allergic diseases</topic><topic>Antigens, Fungal - chemistry</topic><topic>Antigens, Fungal - immunology</topic><topic>Aspergillus fumigatus</topic><topic>Aspergillus fumigatus - enzymology</topic><topic>Aspergillus fumigatus - immunology</topic><topic>Asthma - immunology</topic><topic>Biological and medical sciences</topic><topic>Cross Reactions</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Humans</topic><topic>immunoblot</topic><topic>Immunoblotting</topic><topic>Immunoglobulin E - immunology</topic><topic>Immunopathology</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>N-terminal amino acid sequence</topic><topic>Penicillium - immunology</topic><topic>Respiratory and ent allergic diseases</topic><topic>Sequence Analysis, Protein</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - immunology</topic><topic>Vacuoles - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shen, H.-D.</creatorcontrib><creatorcontrib>Lin, W.-L.</creatorcontrib><creatorcontrib>Tam, M. F.</creatorcontrib><creatorcontrib>Chou, H.</creatorcontrib><creatorcontrib>Wang, C.-W.</creatorcontrib><creatorcontrib>Tsai, J.-J.</creatorcontrib><creatorcontrib>Wang, S.-R.</creatorcontrib><creatorcontrib>Han, S.-H.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Clinical and experimental allergy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shen, H.-D.</au><au>Lin, W.-L.</au><au>Tam, M. F.</au><au>Chou, H.</au><au>Wang, C.-W.</au><au>Tsai, J.-J.</au><au>Wang, S.-R.</au><au>Han, S.-H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis</atitle><jtitle>Clinical and experimental allergy</jtitle><addtitle>Clin Exp Allergy</addtitle><date>2001-02</date><risdate>2001</risdate><volume>31</volume><issue>2</issue><spage>295</spage><epage>302</epage><pages>295-302</pages><issn>0954-7894</issn><eissn>1365-2222</eissn><abstract>Aspergillus species are common airborne fungi that have been identified as causative agents of extrinsic bronchial asthma. More than 10 allergens from A. fumigatus have been recently characterized by cDNA cloning. The objective of this study is to identify A. fumigatus allergens through immunoblot analysis using sera from asthmatic patients. IgE‐binding components of A. fumigatus and IgE cross‐reactivity among allergens of different prevalent airborne fungal species were analysed by immunoblot and immunoblot inhibition, respectively, using sera from asthmatic patients. The N‐terminal amino acid sequences of major allergens identified were determined by Edman degradation. Among two batches (70 and 41 sera) of asthmatic sera tested, 19 (27%) and 14 (34%), respectively, have IgE immunoblot reactivity towards components of A. fumigatus. A 34‐kDa protein that reacts with IgE antibodies in 15 (79%) and 11 (79%) of the 19 and 14 positive samples, respectively, may be considered a major allergen of A. fumigatus. The N‐terminal amino acid sequences of the 34 kDa major allergen and the 30.5 and 30 kDa IgE‐binding components of A. fumigatus showed sequence identity to that of the vacuolar serine proteinase from A. fumigatus. The results from immunoblot inhibition show IgE cross‐reactivity among major allergens of A. fumigatus, P. notatum and P. oxalicum. Results obtained suggest that the 34 kDa major allergen of A. fumigatus may be a vacuolar serine proteinase. There is IgE cross‐reactivity among serine proteinase allergens of A. fumigatus, P. notatum and P. oxalicum.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science, Ltd</pub><pmid>11251631</pmid><doi>10.1046/j.1365-2222.2001.01026.x</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0954-7894
ispartof Clinical and experimental allergy, 2001-02, Vol.31 (2), p.295-302
issn 0954-7894
1365-2222
language eng
recordid cdi_proquest_miscellaneous_76972972
source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects A. fumigatus
Adolescent
Adult
Aged
allergens
Allergens - chemistry
Allergens - immunology
Allergic diseases
Antigens, Fungal - chemistry
Antigens, Fungal - immunology
Aspergillus fumigatus
Aspergillus fumigatus - enzymology
Aspergillus fumigatus - immunology
Asthma - immunology
Biological and medical sciences
Cross Reactions
Electrophoresis, Gel, Two-Dimensional
Humans
immunoblot
Immunoblotting
Immunoglobulin E - immunology
Immunopathology
Medical sciences
Middle Aged
N-terminal amino acid sequence
Penicillium - immunology
Respiratory and ent allergic diseases
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Serine Endopeptidases - chemistry
Serine Endopeptidases - immunology
Vacuoles - enzymology
title Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-06T12%3A10%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20vacuolar%20serine%20proteinase%20as%20a%20major%20allergen%20of%20Aspergillus%20fumigatus%20by%20immunoblotting%20and%20N-terminal%20amino%20acid%20sequence%20analysis&rft.jtitle=Clinical%20and%20experimental%20allergy&rft.au=Shen,%20H.-D.&rft.date=2001-02&rft.volume=31&rft.issue=2&rft.spage=295&rft.epage=302&rft.pages=295-302&rft.issn=0954-7894&rft.eissn=1365-2222&rft_id=info:doi/10.1046/j.1365-2222.2001.01026.x&rft_dat=%3Cproquest_cross%3E17895719%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=199907816&rft_id=info:pmid/11251631&rfr_iscdi=true