Involvement of Extracellular Matrix and Integrin-like Proteins on Conidial Adhesion and Appressorium Differentiation in Magnaporthe oryzae
Conidial adhesion and appressorium formation of Magnaporthe oryzae on the rice surface are important early events in the infection process. As an initiative step to understand the mechanisms underlying these cellular processes at a biochemical level, the effect of a human fibronectin antibody (HFA)...
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Veröffentlicht in: | Journal of microbiology and biotechnology 2007-07, Vol.17 (7), p.1198-1203 |
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creator | Bae, C.Y. (Seoul National University, Seoul, Republic of Korea) Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr Choi, W.B. (Dong-Eui University, Busan, Republic of Korea) Lee, Y.H. (Seoul National University, Seoul, Republic of Korea) |
description | Conidial adhesion and appressorium formation of Magnaporthe oryzae on the rice surface are important early events in the infection process. As an initiative step to understand the mechanisms underlying these cellular processes at a biochemical level, the effect of a human fibronectin antibody (HFA) and RGD peptides on conidial adhesion and appressorium formation was evaluated. HFA inhibited conidial adhesion and appressorium formation in a dosage-dependent manner. RGD peptides also inhibited these cellular events. Conidial adhesion and appressorium formation inhibited by RGD peptides were restored by chemicals involved in the cyclic AMP-dependent signaling pathway. |
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(Seoul National University, Seoul, Republic of Korea) ; Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr ; Choi, W.B. (Dong-Eui University, Busan, Republic of Korea) ; Lee, Y.H. (Seoul National University, Seoul, Republic of Korea)</creator><creatorcontrib>Bae, C.Y. (Seoul National University, Seoul, Republic of Korea) ; Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr ; Choi, W.B. (Dong-Eui University, Busan, Republic of Korea) ; Lee, Y.H. (Seoul National University, Seoul, Republic of Korea)</creatorcontrib><description>Conidial adhesion and appressorium formation of Magnaporthe oryzae on the rice surface are important early events in the infection process. As an initiative step to understand the mechanisms underlying these cellular processes at a biochemical level, the effect of a human fibronectin antibody (HFA) and RGD peptides on conidial adhesion and appressorium formation was evaluated. HFA inhibited conidial adhesion and appressorium formation in a dosage-dependent manner. RGD peptides also inhibited these cellular events. Conidial adhesion and appressorium formation inhibited by RGD peptides were restored by chemicals involved in the cyclic AMP-dependent signaling pathway.</description><identifier>ISSN: 1017-7825</identifier><identifier>PMID: 18051333</identifier><language>eng</language><publisher>Seoul: Korean Society for Applied Microbiology</publisher><subject>Antibodies - pharmacology ; appressorium formation ; Biological and medical sciences ; Biotechnology ; Cell Adhesion ; conidial adhesion ; extracellular matrix ; Extracellular Matrix - metabolism ; fibronectin ; Fibronectins - pharmacology ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - metabolism ; Fungal Structures - physiology ; integrin ; Integrins - physiology ; Magnaporthe - chemistry ; Magnaporthe - cytology ; Magnaporthe oryzae ; Oligopeptides - pharmacology ; PROTEINAS ; PROTEINE ; PROTEINS ; Signal Transduction ; signaling pathway ; Spores, Fungal - physiology ; Surface Properties ; Time Factors</subject><ispartof>Journal of microbiology and biotechnology, 2007-07, Vol.17 (7), p.1198-1203</ispartof><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18965475$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18051333$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bae, C.Y. (Seoul National University, Seoul, Republic of Korea)</creatorcontrib><creatorcontrib>Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr</creatorcontrib><creatorcontrib>Choi, W.B. (Dong-Eui University, Busan, Republic of Korea)</creatorcontrib><creatorcontrib>Lee, Y.H. (Seoul National University, Seoul, Republic of Korea)</creatorcontrib><title>Involvement of Extracellular Matrix and Integrin-like Proteins on Conidial Adhesion and Appressorium Differentiation in Magnaporthe oryzae</title><title>Journal of microbiology and biotechnology</title><addtitle>J Microbiol Biotechnol</addtitle><description>Conidial adhesion and appressorium formation of Magnaporthe oryzae on the rice surface are important early events in the infection process. As an initiative step to understand the mechanisms underlying these cellular processes at a biochemical level, the effect of a human fibronectin antibody (HFA) and RGD peptides on conidial adhesion and appressorium formation was evaluated. HFA inhibited conidial adhesion and appressorium formation in a dosage-dependent manner. RGD peptides also inhibited these cellular events. Conidial adhesion and appressorium formation inhibited by RGD peptides were restored by chemicals involved in the cyclic AMP-dependent signaling pathway.</description><subject>Antibodies - pharmacology</subject><subject>appressorium formation</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cell Adhesion</subject><subject>conidial adhesion</subject><subject>extracellular matrix</subject><subject>Extracellular Matrix - metabolism</subject><subject>fibronectin</subject><subject>Fibronectins - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungal Structures - physiology</subject><subject>integrin</subject><subject>Integrins - physiology</subject><subject>Magnaporthe - chemistry</subject><subject>Magnaporthe - cytology</subject><subject>Magnaporthe oryzae</subject><subject>Oligopeptides - pharmacology</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Signal Transduction</subject><subject>signaling pathway</subject><subject>Spores, Fungal - physiology</subject><subject>Surface Properties</subject><subject>Time Factors</subject><issn>1017-7825</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpN0MlOwzAQBuAcQLQsjwDyBW6RvMRZjlXZKopACM7RNBm3hsQOtlMVHoGnJlWLxGmk0ad_NP9BNGaUZXGWczmKjr1_pzRlPE-PohHLqWRCiHH0MzNr26yxRROIVeRmExxU2DR9A448QnB6Q8DUZGYCLp02caM_kDw7G1AbT6whU2t0raEhk3qFXg-brZ90nUPvrdN9S661UuiGExrCFmgzRC8NdNaFFRLrvr4BT6NDBY3Hs_08id5ub16n9_H86W42ncxjxVMW4lxxhgzSRAJwTOqM5VVe14VKCoCUFVJkalHJRHBYSESmipQpLhhFqbBKuDiJrna5nbOfPfpQttpvXwaDtvdlWlBW0FwM8GIP-0WLddk53YL7Kv_aG8DlHoCvoFEOTKX9P1ekMsnk4M53ToEtYWjRlw8vnNKcUpqwQvwCo-GDeg</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Bae, C.Y. (Seoul National University, Seoul, Republic of Korea)</creator><creator>Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr</creator><creator>Choi, W.B. (Dong-Eui University, Busan, Republic of Korea)</creator><creator>Lee, Y.H. (Seoul National University, Seoul, Republic of Korea)</creator><general>Korean Society for Applied Microbiology</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20070701</creationdate><title>Involvement of Extracellular Matrix and Integrin-like Proteins on Conidial Adhesion and Appressorium Differentiation in Magnaporthe oryzae</title><author>Bae, C.Y. (Seoul National University, Seoul, Republic of Korea) ; Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr ; Choi, W.B. (Dong-Eui University, Busan, Republic of Korea) ; Lee, Y.H. (Seoul National University, Seoul, Republic of Korea)</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f261t-8f21e1a645aa2e4d718c8dd9f49aa619537fbc5432ab5ee1f961f2310e5fec423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Antibodies - pharmacology</topic><topic>appressorium formation</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cell Adhesion</topic><topic>conidial adhesion</topic><topic>extracellular matrix</topic><topic>Extracellular Matrix - metabolism</topic><topic>fibronectin</topic><topic>Fibronectins - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungal Structures - physiology</topic><topic>integrin</topic><topic>Integrins - physiology</topic><topic>Magnaporthe - chemistry</topic><topic>Magnaporthe - cytology</topic><topic>Magnaporthe oryzae</topic><topic>Oligopeptides - pharmacology</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Signal Transduction</topic><topic>signaling pathway</topic><topic>Spores, Fungal - physiology</topic><topic>Surface Properties</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bae, C.Y. (Seoul National University, Seoul, Republic of Korea)</creatorcontrib><creatorcontrib>Kim, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: sokim@snu.ac.kr</creatorcontrib><creatorcontrib>Choi, W.B. (Dong-Eui University, Busan, Republic of Korea)</creatorcontrib><creatorcontrib>Lee, Y.H. 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(Seoul National University, Seoul, Republic of Korea)</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of Extracellular Matrix and Integrin-like Proteins on Conidial Adhesion and Appressorium Differentiation in Magnaporthe oryzae</atitle><jtitle>Journal of microbiology and biotechnology</jtitle><addtitle>J Microbiol Biotechnol</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>17</volume><issue>7</issue><spage>1198</spage><epage>1203</epage><pages>1198-1203</pages><issn>1017-7825</issn><abstract>Conidial adhesion and appressorium formation of Magnaporthe oryzae on the rice surface are important early events in the infection process. As an initiative step to understand the mechanisms underlying these cellular processes at a biochemical level, the effect of a human fibronectin antibody (HFA) and RGD peptides on conidial adhesion and appressorium formation was evaluated. HFA inhibited conidial adhesion and appressorium formation in a dosage-dependent manner. RGD peptides also inhibited these cellular events. Conidial adhesion and appressorium formation inhibited by RGD peptides were restored by chemicals involved in the cyclic AMP-dependent signaling pathway.</abstract><cop>Seoul</cop><pub>Korean Society for Applied Microbiology</pub><pmid>18051333</pmid><tpages>6</tpages></addata></record> |
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subjects | Antibodies - pharmacology appressorium formation Biological and medical sciences Biotechnology Cell Adhesion conidial adhesion extracellular matrix Extracellular Matrix - metabolism fibronectin Fibronectins - pharmacology Fundamental and applied biological sciences. Psychology Fungal Proteins - metabolism Fungal Structures - physiology integrin Integrins - physiology Magnaporthe - chemistry Magnaporthe - cytology Magnaporthe oryzae Oligopeptides - pharmacology PROTEINAS PROTEINE PROTEINS Signal Transduction signaling pathway Spores, Fungal - physiology Surface Properties Time Factors |
title | Involvement of Extracellular Matrix and Integrin-like Proteins on Conidial Adhesion and Appressorium Differentiation in Magnaporthe oryzae |
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