Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete Phytophthora infestans, a Causative Agent of Potato Late Blight Disease.
Identifieur interne : 000096 ( Main/Exploration ); précédent : 000095; suivant : 000097Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete Phytophthora infestans, a Causative Agent of Potato Late Blight Disease.
Auteurs : Eugene A. Rogozhin [Russie] ; Alexey S. Vasilchenko [Russie] ; Anna S. Barashkova [Russie] ; Alexey N. Smirnov [Russie] ; Sergey K. Zavriev [Russie] ; Vladimir P. Demushkin [Russie]Source :
- Plants (Basel, Switzerland) [ 2223-7747 ] ; 2020.
Abstract
We report the inhibitory effect of peptide extracts obtained from seven medicinal plants against a causative agent of late blight disease Phytophthora infestans. We find that all the extracts possess inhibitory activity toward the zoospores output, zoosporangium germination, and the development of P. infestans on potato disc tubers at different quantitative levels. Based on the biological effects detected, an extract of common horsetail (Equisetum arvense) biomass is recognized as the most effective and is selected for further structural analysis. We perform a combination of amino acid analysis and MALDI-TOF mass spectrometry, which reveal the presence of Asn/Asp- and Gln/Glu-rich short peptides with molecular masses in the range of 500-900 Da and not exceeding 1500 Da as the maximum. Analytical anion-exchange HPLC is successfully applied for separation of the peptide extract from common horsetail (E. arvense). We collect nine dominant components that are combined in two groups with differences in retention times. The N-terminal amino acid sequence of the prevalent compounds after analytical ion-exchange HPLC allows us to identify them as peptide fragments of functionally active proteins associated with photosynthesis, aquatic transport, and chitin binding. The anti-oomycete effects may be associated with the conversion of ribulose-1,5-bisphosphate carboxylase/oxygenase to produce a number of biologically active anionic peptides with possible regulatory functions. These data inform our knowledge regarding biologically active peptide fragments; they are the components of programmed or induced proteolysis of plant proteins and can realize secondary antimicrobial functions.
DOI: 10.3390/plants9101294
PubMed: 33007947
PubMed Central: PMC7599828
Affiliations:
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Rogozhin</name><affiliation wicri:level="1"><nlm:affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>Gause Institute of New Antibiotics, 119021 Moscow, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Gause Institute of New Antibiotics, 119021 Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>All-Russian Institute of Plant Protection, 196608 St.-Petersburg-Pushkin, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>All-Russian Institute of Plant Protection, 196608 St.-Petersburg-Pushkin</wicri:regionArea><wicri:noRegion>196608 St.-Petersburg-Pushkin</wicri:noRegion></affiliation></author><author><name sortKey="Vasilchenko, Alexey S" sort="Vasilchenko, Alexey S" uniqKey="Vasilchenko A" first="Alexey S" last="Vasilchenko">Alexey S. Vasilchenko</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Biological and Agricultural Biology (X-Bio) Tyumen State University, Russian Federation, 625003 Tyumen, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Biological and Agricultural Biology (X-Bio) Tyumen State University, Russian Federation, 625003 Tyumen</wicri:regionArea><wicri:noRegion>625003 Tyumen</wicri:noRegion></affiliation></author><author><name sortKey="Barashkova, Anna S" sort="Barashkova, Anna S" uniqKey="Barashkova A" first="Anna S" last="Barashkova">Anna S. Barashkova</name><affiliation wicri:level="1"><nlm:affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>Institute of Biological and Agricultural Biology (X-Bio) Tyumen State University, Russian Federation, 625003 Tyumen, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Biological and Agricultural Biology (X-Bio) Tyumen State University, Russian Federation, 625003 Tyumen</wicri:regionArea><wicri:noRegion>625003 Tyumen</wicri:noRegion></affiliation></author><author><name sortKey="Smirnov, Alexey N" sort="Smirnov, Alexey N" uniqKey="Smirnov A" first="Alexey N" last="Smirnov">Alexey N. Smirnov</name><affiliation wicri:level="1"><nlm:affiliation>Timiryazev Russian State Agrarian University, 127550 Moscow, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Timiryazev Russian State Agrarian University, 127550 Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Zavriev, Sergey K" sort="Zavriev, Sergey K" uniqKey="Zavriev S" first="Sergey K" last="Zavriev">Sergey K. Zavriev</name><affiliation wicri:level="1"><nlm:affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Demushkin, Vladimir P" sort="Demushkin, Vladimir P" uniqKey="Demushkin V" first="Vladimir P" last="Demushkin">Vladimir P. Demushkin</name><affiliation wicri:level="1"><nlm:affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author></analytic><series><title level="j">Plants (Basel, Switzerland)</title><idno type="ISSN">2223-7747</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report the inhibitory effect of peptide extracts obtained from seven medicinal plants against a causative agent of late blight disease <i>Phytophthora infestans.</i> We find that all the extracts possess inhibitory activity toward the zoospores output, zoosporangium germination, and the development of <i>P. infestans</i> on potato disc tubers at different quantitative levels. Based on the biological effects detected, an extract of common horsetail (<i>Equisetum arvense</i>) biomass is recognized as the most effective and is selected for further structural analysis. We perform a combination of amino acid analysis and MALDI-TOF mass spectrometry, which reveal the presence of Asn/Asp- and Gln/Glu-rich short peptides with molecular masses in the range of 500-900 Da and not exceeding 1500 Da as the maximum. Analytical anion-exchange HPLC is successfully applied for separation of the peptide extract from common horsetail (<i>E. arvense</i>). We collect nine dominant components that are combined in two groups with differences in retention times. The <i>N</i>-terminal amino acid sequence of the prevalent compounds after analytical ion-exchange HPLC allows us to identify them as peptide fragments of functionally active proteins associated with photosynthesis, aquatic transport, and chitin binding. The anti-oomycete effects may be associated with the conversion of ribulose-1,5-bisphosphate carboxylase/oxygenase to produce a number of biologically active anionic peptides with possible regulatory functions. These data inform our knowledge regarding biologically active peptide fragments; they are the components of programmed or induced proteolysis of plant proteins and can realize secondary antimicrobial functions.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">33007947</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>03</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2223-7747</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>10</Issue><PubDate><Year>2020</Year><Month>Sep</Month><Day>30</Day></PubDate></JournalIssue><Title>Plants (Basel, Switzerland)</Title><ISOAbbreviation>Plants (Basel)</ISOAbbreviation></Journal><ArticleTitle>Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete <i>Phytophthora infestans,</i> a Causative Agent of Potato Late Blight Disease.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E1294</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/plants9101294</ELocationID><Abstract><AbstractText>We report the inhibitory effect of peptide extracts obtained from seven medicinal plants against a causative agent of late blight disease <i>Phytophthora infestans.</i> We find that all the extracts possess inhibitory activity toward the zoospores output, zoosporangium germination, and the development of <i>P. infestans</i> on potato disc tubers at different quantitative levels. Based on the biological effects detected, an extract of common horsetail (<i>Equisetum arvense</i>) biomass is recognized as the most effective and is selected for further structural analysis. We perform a combination of amino acid analysis and MALDI-TOF mass spectrometry, which reveal the presence of Asn/Asp- and Gln/Glu-rich short peptides with molecular masses in the range of 500-900 Da and not exceeding 1500 Da as the maximum. Analytical anion-exchange HPLC is successfully applied for separation of the peptide extract from common horsetail (<i>E. arvense</i>). We collect nine dominant components that are combined in two groups with differences in retention times. The <i>N</i>-terminal amino acid sequence of the prevalent compounds after analytical ion-exchange HPLC allows us to identify them as peptide fragments of functionally active proteins associated with photosynthesis, aquatic transport, and chitin binding. The anti-oomycete effects may be associated with the conversion of ribulose-1,5-bisphosphate carboxylase/oxygenase to produce a number of biologically active anionic peptides with possible regulatory functions. These data inform our knowledge regarding biologically active peptide fragments; they are the components of programmed or induced proteolysis of plant proteins and can realize secondary antimicrobial functions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rogozhin</LastName><ForeName>Eugene A</ForeName><Initials>EA</Initials><Identifier Source="ORCID">0000-0003-0659-9547</Identifier><AffiliationInfo><Affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Gause Institute of New Antibiotics, 119021 Moscow, Russia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>All-Russian Institute of Plant Protection, 196608 St.-Petersburg-Pushkin, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vasilchenko</LastName><ForeName>Alexey S</ForeName><Initials>AS</Initials><Identifier Source="ORCID">0000-0001-9970-4881</Identifier><AffiliationInfo><Affiliation>Institute of Biological and Agricultural Biology (X-Bio) Tyumen State University, Russian Federation, 625003 Tyumen, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barashkova</LastName><ForeName>Anna S</ForeName><Initials>AS</Initials><AffiliationInfo><Affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institute of Biological and Agricultural Biology (X-Bio) Tyumen State University, Russian Federation, 625003 Tyumen, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Smirnov</LastName><ForeName>Alexey N</ForeName><Initials>AN</Initials><AffiliationInfo><Affiliation>Timiryazev Russian State Agrarian University, 127550 Moscow, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zavriev</LastName><ForeName>Sergey K</ForeName><Initials>SK</Initials><AffiliationInfo><Affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Demushkin</LastName><ForeName>Vladimir P</ForeName><Initials>VP</Initials><AffiliationInfo><Affiliation>Shemyakin and Ovchinnikov Institite of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>19-76-30005</GrantID><Agency>Russian Science Foundation</Agency><Country></Country></Grant><Grant><GrantID>18-34-20058</GrantID><Agency>Russian Foundation for Basic Research</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Plants (Basel)</MedlineTA><NlmUniqueID>101596181</NlmUniqueID><ISSNLinking>2223-7747</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Phytophthora infestans</Keyword><Keyword MajorTopicYN="N">amino acid composition</Keyword><Keyword MajorTopicYN="N">anti-oomycete activity</Keyword><Keyword MajorTopicYN="N">liquid chromatography</Keyword><Keyword MajorTopicYN="N">medicinal plants</Keyword><Keyword MajorTopicYN="N">peptide fragments</Keyword><Keyword MajorTopicYN="N">protein hydrolysis</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>09</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>09</Month><Day>22</Day></PubMedPubDate><PubMedPubDate 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IdType="pubmed">20969798</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><country name="Russie"><region name="District fédéral central"><name sortKey="Rogozhin, Eugene A" sort="Rogozhin, Eugene A" uniqKey="Rogozhin E" first="Eugene A" last="Rogozhin">Eugene A. Rogozhin</name></region><name sortKey="Barashkova, Anna S" sort="Barashkova, Anna S" uniqKey="Barashkova A" first="Anna S" last="Barashkova">Anna S. Barashkova</name><name sortKey="Barashkova, Anna S" sort="Barashkova, Anna S" uniqKey="Barashkova A" first="Anna S" last="Barashkova">Anna S. Barashkova</name><name sortKey="Demushkin, Vladimir P" sort="Demushkin, Vladimir P" uniqKey="Demushkin V" first="Vladimir P" last="Demushkin">Vladimir P. Demushkin</name><name sortKey="Rogozhin, Eugene A" sort="Rogozhin, Eugene A" uniqKey="Rogozhin E" first="Eugene A" last="Rogozhin">Eugene A. Rogozhin</name><name sortKey="Rogozhin, Eugene A" sort="Rogozhin, Eugene A" uniqKey="Rogozhin E" first="Eugene A" last="Rogozhin">Eugene A. Rogozhin</name><name sortKey="Smirnov, Alexey N" sort="Smirnov, Alexey N" uniqKey="Smirnov A" first="Alexey N" last="Smirnov">Alexey N. Smirnov</name><name sortKey="Vasilchenko, Alexey S" sort="Vasilchenko, Alexey S" uniqKey="Vasilchenko A" first="Alexey S" last="Vasilchenko">Alexey S. Vasilchenko</name><name sortKey="Zavriev, Sergey K" sort="Zavriev, Sergey K" uniqKey="Zavriev S" first="Sergey K" last="Zavriev">Sergey K. Zavriev</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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