Differential antifungal and calcium channel-blocking activity among structurally related plant defensins
Plant defensins are a family of small Cys-rich antifungal proteins that play important roles in plant defense against invading fungi. Structures of several plant defensins share a Cys-stabilized α/β-motif. Structural determinants in plant defensins that govern their antifungal activity and the mecha...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2004-08, Vol.135 (4), p.2055-2067 |
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| creator | Spelbrink, R.G Dilmac, N Allen, A Smith, T.J Shah, D.M Hockerman, G.H |
| description | Plant defensins are a family of small Cys-rich antifungal proteins that play important roles in plant defense against invading fungi. Structures of several plant defensins share a Cys-stabilized α/β-motif. Structural determinants in plant defensins that govern their antifungal activity and the mechanisms by which they inhibit fungal growth remain unclear. Alfalfa (Medicago sativa) seed defensin, MsDef1, strongly inhibits the growth of Fusarium graminearum in vitro, and its antifungal activity is markedly reduced in the presence of Ca2+. By contrast, MtDef2 from Medicago truncatula, which shares 65% amino acid sequence identity with MsDef1, lacks antifungal activity against F. graminearum. Characterization of the in vitro antifungal activity of the chimeras containing portions of the MsDef1 and MtDef2 proteins shows that the major determinants of antifungal activity reside in the carboxy-terminal region (amino acids 31-45) of MsDef1. We further define the active site by demonstrating that the Arg at position 38 of MsDef1 is critical for its antifungal activity. Furthermore, we have found for the first time, to our knowledge, that MsDef1 blocks the mammalian L-type Ca2+ channel in a manner akin to a virally encoded and structurally unrelated antifungal toxin KP4 from Ustilago maydis, whereas structurally similar MtDef2 and the radish (Raphanus sativus) seed defensin Rs-AFP2 fail to block the L-type Ca2+ channel. From these results, we speculate that the two unrelated antifungal proteins, KP4 and MsDef1, have evolutionarily converged upon the same molecular target, whereas the two structurally related antifungal plant defensins, MtDef2 and Rs-AFP2, have diverged to attack different targets in fungi. |
| doi_str_mv | 10.1104/pp.104.040873 |
| format | Article |
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Structures of several plant defensins share a Cys-stabilized α/β-motif. Structural determinants in plant defensins that govern their antifungal activity and the mechanisms by which they inhibit fungal growth remain unclear. Alfalfa (Medicago sativa) seed defensin, MsDef1, strongly inhibits the growth of Fusarium graminearum in vitro, and its antifungal activity is markedly reduced in the presence of Ca2+. By contrast, MtDef2 from Medicago truncatula, which shares 65% amino acid sequence identity with MsDef1, lacks antifungal activity against F. graminearum. Characterization of the in vitro antifungal activity of the chimeras containing portions of the MsDef1 and MtDef2 proteins shows that the major determinants of antifungal activity reside in the carboxy-terminal region (amino acids 31-45) of MsDef1. We further define the active site by demonstrating that the Arg at position 38 of MsDef1 is critical for its antifungal activity. Furthermore, we have found for the first time, to our knowledge, that MsDef1 blocks the mammalian L-type Ca2+ channel in a manner akin to a virally encoded and structurally unrelated antifungal toxin KP4 from Ustilago maydis, whereas structurally similar MtDef2 and the radish (Raphanus sativus) seed defensin Rs-AFP2 fail to block the L-type Ca2+ channel. From these results, we speculate that the two unrelated antifungal proteins, KP4 and MsDef1, have evolutionarily converged upon the same molecular target, whereas the two structurally related antifungal plant defensins, MtDef2 and Rs-AFP2, have diverged to attack different targets in fungi.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.104.040873</identifier><identifier>PMID: 15299136</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>alfalfa ; Amino Acid Sequence ; amino acid sequences ; Amino acids ; Antifungal Agents - pharmacology ; antifungal properties ; antifungal proteins ; Antifungals ; arginine ; Biochemical Processes and Macromolecular Structures ; Biological and medical sciences ; calcium ; calcium channel blockers ; Calcium Channel Blockers - pharmacology ; Calcium channels ; Cysteine ; defensins ; Defensins - genetics ; Defensins - pharmacology ; forage crops ; Fundamental and applied biological sciences. Psychology ; Fungal plant pathogens ; Fungal spores ; Fungi ; Fusarium graminearum ; Gibberella zeae ; Hyphae ; Medicago sativa ; Medicago truncatula ; Models, Molecular ; molecular models ; Molecular Sequence Data ; Neurospora crassa ; Neurospora crassa - drug effects ; Pathology, epidemiology, host-fungus relationships. Damages, economic importance ; Phytopathology. Animal pests. Plant and forest protection ; Pichia pastoris ; plant pathogenic fungi ; plant proteins ; Plant Proteins - genetics ; Plant Proteins - pharmacology ; Plants ; Protein Conformation ; protein structure ; Proteins ; radishes ; Raphanus sativus ; Scorpion Venoms - chemistry ; structure-activity relationships ; Toxins ; Ustilago ; Ustilago maydis</subject><ispartof>Plant physiology (Bethesda), 2004-08, Vol.135 (4), p.2055-2067</ispartof><rights>Copyright 2004 American Society of Plant Biologists</rights><rights>2004 INIST-CNRS</rights><rights>Copyright © 2004, American Society of Plant Biologists 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c558t-33199964d6c4250ffcf0f70e50a631b37985303c40155983e38175684a74baf03</citedby><cites>FETCH-LOGICAL-c558t-33199964d6c4250ffcf0f70e50a631b37985303c40155983e38175684a74baf03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4356562$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4356562$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16040883$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15299136$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Spelbrink, R.G</creatorcontrib><creatorcontrib>Dilmac, N</creatorcontrib><creatorcontrib>Allen, A</creatorcontrib><creatorcontrib>Smith, T.J</creatorcontrib><creatorcontrib>Shah, D.M</creatorcontrib><creatorcontrib>Hockerman, G.H</creatorcontrib><title>Differential antifungal and calcium channel-blocking activity among structurally related plant defensins</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Plant defensins are a family of small Cys-rich antifungal proteins that play important roles in plant defense against invading fungi. Structures of several plant defensins share a Cys-stabilized α/β-motif. Structural determinants in plant defensins that govern their antifungal activity and the mechanisms by which they inhibit fungal growth remain unclear. Alfalfa (Medicago sativa) seed defensin, MsDef1, strongly inhibits the growth of Fusarium graminearum in vitro, and its antifungal activity is markedly reduced in the presence of Ca2+. By contrast, MtDef2 from Medicago truncatula, which shares 65% amino acid sequence identity with MsDef1, lacks antifungal activity against F. graminearum. Characterization of the in vitro antifungal activity of the chimeras containing portions of the MsDef1 and MtDef2 proteins shows that the major determinants of antifungal activity reside in the carboxy-terminal region (amino acids 31-45) of MsDef1. We further define the active site by demonstrating that the Arg at position 38 of MsDef1 is critical for its antifungal activity. Furthermore, we have found for the first time, to our knowledge, that MsDef1 blocks the mammalian L-type Ca2+ channel in a manner akin to a virally encoded and structurally unrelated antifungal toxin KP4 from Ustilago maydis, whereas structurally similar MtDef2 and the radish (Raphanus sativus) seed defensin Rs-AFP2 fail to block the L-type Ca2+ channel. From these results, we speculate that the two unrelated antifungal proteins, KP4 and MsDef1, have evolutionarily converged upon the same molecular target, whereas the two structurally related antifungal plant defensins, MtDef2 and Rs-AFP2, have diverged to attack different targets in fungi.</description><subject>alfalfa</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Antifungal Agents - pharmacology</subject><subject>antifungal properties</subject><subject>antifungal proteins</subject><subject>Antifungals</subject><subject>arginine</subject><subject>Biochemical Processes and Macromolecular Structures</subject><subject>Biological and medical sciences</subject><subject>calcium</subject><subject>calcium channel blockers</subject><subject>Calcium Channel Blockers - pharmacology</subject><subject>Calcium channels</subject><subject>Cysteine</subject><subject>defensins</subject><subject>Defensins - genetics</subject><subject>Defensins - pharmacology</subject><subject>forage crops</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal plant pathogens</subject><subject>Fungal spores</subject><subject>Fungi</subject><subject>Fusarium graminearum</subject><subject>Gibberella zeae</subject><subject>Hyphae</subject><subject>Medicago sativa</subject><subject>Medicago truncatula</subject><subject>Models, Molecular</subject><subject>molecular models</subject><subject>Molecular Sequence Data</subject><subject>Neurospora crassa</subject><subject>Neurospora crassa - drug effects</subject><subject>Pathology, epidemiology, host-fungus relationships. Damages, economic importance</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Pichia pastoris</subject><subject>plant pathogenic fungi</subject><subject>plant proteins</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - pharmacology</subject><subject>Plants</subject><subject>Protein Conformation</subject><subject>protein structure</subject><subject>Proteins</subject><subject>radishes</subject><subject>Raphanus sativus</subject><subject>Scorpion Venoms - chemistry</subject><subject>structure-activity relationships</subject><subject>Toxins</subject><subject>Ustilago</subject><subject>Ustilago maydis</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkjtvFDEUhUcIRJZASYdgGhDNLNdvu6BA4SlFooDUltdj7zp4Htgzkfbf42FWCTRQnWvdz8f36riqniLYIgT0zThui2yBghTkXrVBjOAGMyrvVxuAUoOU6qx6lPM1ACCC6MPqDDGsFCJ8Ux3eB-9dcv0UTKxNET_3-99lW1sTbZi72h5M37vY7OJgf4R-Xxs7hZswHWvTDeWYpzTbaU4mxmOdXDSTa-sxFre6dd71OfT5cfXAm5jdk5OeV1cfP3y_-Nxcfv305eLdZWMZk1NDCFJKcdpySzED760HL8AxMJygHRFKMgLEUkCMKUkckUgwLqkRdGc8kPPq7eo7zrvOtbZsVubSYwqdSUc9mKD_7vThoPfDjWYYhBDl_qvT_TT8nF2edBeydbFs44Y5a84lIhiWh17_E0RSMEkFFvy_nkhwqQDjAjYraNOQc3L-dm4Eeolbj6NeZI278M__XPaOPuVbgJcnwOSSpk-mtyHfcXwxkovRs5W7ztOQbvuUMM74MteLte3NoM0-FYurb7j8JgBFheCK_ALQsMZt</recordid><startdate>20040801</startdate><enddate>20040801</enddate><creator>Spelbrink, R.G</creator><creator>Dilmac, N</creator><creator>Allen, A</creator><creator>Smith, T.J</creator><creator>Shah, D.M</creator><creator>Hockerman, G.H</creator><general>American Society of Plant Biologists</general><general>American Society of Plant Physiologists</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>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20040801</creationdate><title>Differential antifungal and calcium channel-blocking activity among structurally related plant defensins</title><author>Spelbrink, R.G ; Dilmac, N ; Allen, A ; Smith, T.J ; Shah, D.M ; Hockerman, G.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c558t-33199964d6c4250ffcf0f70e50a631b37985303c40155983e38175684a74baf03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>alfalfa</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Amino acids</topic><topic>Antifungal Agents - pharmacology</topic><topic>antifungal properties</topic><topic>antifungal proteins</topic><topic>Antifungals</topic><topic>arginine</topic><topic>Biochemical Processes and Macromolecular Structures</topic><topic>Biological and medical sciences</topic><topic>calcium</topic><topic>calcium channel blockers</topic><topic>Calcium Channel Blockers - pharmacology</topic><topic>Calcium channels</topic><topic>Cysteine</topic><topic>defensins</topic><topic>Defensins - genetics</topic><topic>Defensins - pharmacology</topic><topic>forage crops</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal plant pathogens</topic><topic>Fungal spores</topic><topic>Fungi</topic><topic>Fusarium graminearum</topic><topic>Gibberella zeae</topic><topic>Hyphae</topic><topic>Medicago sativa</topic><topic>Medicago truncatula</topic><topic>Models, Molecular</topic><topic>molecular models</topic><topic>Molecular Sequence Data</topic><topic>Neurospora crassa</topic><topic>Neurospora crassa - drug effects</topic><topic>Pathology, epidemiology, host-fungus relationships. Damages, economic importance</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Pichia pastoris</topic><topic>plant pathogenic fungi</topic><topic>plant proteins</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - pharmacology</topic><topic>Plants</topic><topic>Protein Conformation</topic><topic>protein structure</topic><topic>Proteins</topic><topic>radishes</topic><topic>Raphanus sativus</topic><topic>Scorpion Venoms - chemistry</topic><topic>structure-activity relationships</topic><topic>Toxins</topic><topic>Ustilago</topic><topic>Ustilago maydis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spelbrink, R.G</creatorcontrib><creatorcontrib>Dilmac, N</creatorcontrib><creatorcontrib>Allen, A</creatorcontrib><creatorcontrib>Smith, T.J</creatorcontrib><creatorcontrib>Shah, D.M</creatorcontrib><creatorcontrib>Hockerman, G.H</creatorcontrib><collection>AGRIS</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>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Spelbrink, R.G</au><au>Dilmac, N</au><au>Allen, A</au><au>Smith, T.J</au><au>Shah, D.M</au><au>Hockerman, G.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential antifungal and calcium channel-blocking activity among structurally related plant defensins</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2004-08-01</date><risdate>2004</risdate><volume>135</volume><issue>4</issue><spage>2055</spage><epage>2067</epage><pages>2055-2067</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>Plant defensins are a family of small Cys-rich antifungal proteins that play important roles in plant defense against invading fungi. Structures of several plant defensins share a Cys-stabilized α/β-motif. Structural determinants in plant defensins that govern their antifungal activity and the mechanisms by which they inhibit fungal growth remain unclear. Alfalfa (Medicago sativa) seed defensin, MsDef1, strongly inhibits the growth of Fusarium graminearum in vitro, and its antifungal activity is markedly reduced in the presence of Ca2+. By contrast, MtDef2 from Medicago truncatula, which shares 65% amino acid sequence identity with MsDef1, lacks antifungal activity against F. graminearum. Characterization of the in vitro antifungal activity of the chimeras containing portions of the MsDef1 and MtDef2 proteins shows that the major determinants of antifungal activity reside in the carboxy-terminal region (amino acids 31-45) of MsDef1. We further define the active site by demonstrating that the Arg at position 38 of MsDef1 is critical for its antifungal activity. Furthermore, we have found for the first time, to our knowledge, that MsDef1 blocks the mammalian L-type Ca2+ channel in a manner akin to a virally encoded and structurally unrelated antifungal toxin KP4 from Ustilago maydis, whereas structurally similar MtDef2 and the radish (Raphanus sativus) seed defensin Rs-AFP2 fail to block the L-type Ca2+ channel. From these results, we speculate that the two unrelated antifungal proteins, KP4 and MsDef1, have evolutionarily converged upon the same molecular target, whereas the two structurally related antifungal plant defensins, MtDef2 and Rs-AFP2, have diverged to attack different targets in fungi.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>15299136</pmid><doi>10.1104/pp.104.040873</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | alfalfa Amino Acid Sequence amino acid sequences Amino acids Antifungal Agents - pharmacology antifungal properties antifungal proteins Antifungals arginine Biochemical Processes and Macromolecular Structures Biological and medical sciences calcium calcium channel blockers Calcium Channel Blockers - pharmacology Calcium channels Cysteine defensins Defensins - genetics Defensins - pharmacology forage crops Fundamental and applied biological sciences. Psychology Fungal plant pathogens Fungal spores Fungi Fusarium graminearum Gibberella zeae Hyphae Medicago sativa Medicago truncatula Models, Molecular molecular models Molecular Sequence Data Neurospora crassa Neurospora crassa - drug effects Pathology, epidemiology, host-fungus relationships. Damages, economic importance Phytopathology. Animal pests. Plant and forest protection Pichia pastoris plant pathogenic fungi plant proteins Plant Proteins - genetics Plant Proteins - pharmacology Plants Protein Conformation protein structure Proteins radishes Raphanus sativus Scorpion Venoms - chemistry structure-activity relationships Toxins Ustilago Ustilago maydis |
| title | Differential antifungal and calcium channel-blocking activity among structurally related plant defensins |
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