PhytAMP: a database dedicated to antimicrobial plant peptides
Identifieur interne : 000064 ( Main/Exploration ); précédent : 000063; suivant : 000065PhytAMP: a database dedicated to antimicrobial plant peptides
Auteurs : Riadh Hammami [Tunisie, France, Canada] ; Jeannette Ben Hamida [Tunisie] ; Gérard Vergoten [France] ; Ismail Fliss [Canada]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 2008.
Descripteurs français
- KwdFr :
- Anti-infectieux (classification), Anti-infectieux (composition chimique), Anti-infectieux (pharmacologie), Bases de données factuelles (MeSH), Interface utilisateur (MeSH), Peptides antimicrobiens cationiques (classification), Peptides antimicrobiens cationiques (composition chimique), Peptides antimicrobiens cationiques (pharmacologie), Phylogenèse (MeSH), Plantes (métabolisme).
- MESH :
- classification : Anti-infectieux, Peptides antimicrobiens cationiques.
- composition chimique : Anti-infectieux, Peptides antimicrobiens cationiques.
- métabolisme : Plantes.
- pharmacologie : Anti-infectieux, Peptides antimicrobiens cationiques.
- Bases de données factuelles, Interface utilisateur, Phylogenèse.
English descriptors
- KwdEn :
- Anti-Infective Agents (chemistry), Anti-Infective Agents (classification), Anti-Infective Agents (pharmacology), Antimicrobial Cationic Peptides (chemistry), Antimicrobial Cationic Peptides (classification), Antimicrobial Cationic Peptides (pharmacology), Databases, Factual (MeSH), Phylogeny (MeSH), Plants (metabolism), User-Computer Interface (MeSH).
- MESH :
- chemical , chemistry : Anti-Infective Agents, Antimicrobial Cationic Peptides.
- chemical , classification : Anti-Infective Agents, Antimicrobial Cationic Peptides.
- chemical , pharmacology : Anti-Infective Agents, Antimicrobial Cationic Peptides.
- metabolism : Plants.
- Databases, Factual, Phylogeny, User-Computer Interface.
Abstract
Plants produce small cysteine-rich antimicrobial peptides as an innate defense against pathogens. Based on amino acid sequence homology, these peptides were classified mostly as α-defensins, thionins, lipid transfer proteins, cyclotides, snakins and hevein-like. Although many antimicrobial plant peptides are now well characterized, much information is still missing or is unavailable to potential users. The compilation of such information in one centralized resource, such as a database would therefore facilitate the study of the potential these peptide structures represent, for example, as alternatives in response to increasing antibiotic resistance or for increasing plant resistance to pathogens by genetic engineering. To achieve this goal, we developed a new database, PhytAMP, which contains valuable information on antimicrobial plant peptides, including taxonomic, microbiological and physicochemical data. Information is very easy to extract from this database and allows rapid prediction of structure/function relationships and target organisms and hence better exploitation of plant peptide biological activities in both the pharmaceutical and agricultural sectors. PhytAMP may be accessed free of charge at
Url:
DOI: 10.1093/nar/gkn655
PubMed: 18836196
PubMed Central: 2686510
Affiliations:
Links toward previous steps (curation, corpus...)
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Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>Plants produce small cysteine-rich antimicrobial peptides as an innate defense against pathogens. Based on amino acid sequence homology, these peptides were classified mostly as α-defensins, thionins, lipid transfer proteins, cyclotides, snakins and hevein-like. Although many antimicrobial plant peptides are now well characterized, much information is still missing or is unavailable to potential users. The compilation of such information in one centralized resource, such as a database would therefore facilitate the study of the potential these peptide structures represent, for example, as alternatives in response to increasing antibiotic resistance or for increasing plant resistance to pathogens by genetic engineering. To achieve this goal, we developed a new database, PhytAMP, which contains valuable information on antimicrobial plant peptides, including taxonomic, microbiological and physicochemical data. Information is very easy to extract from this database and allows rapid prediction of structure/function relationships and target organisms and hence better exploitation of plant peptide biological activities in both the pharmaceutical and agricultural sectors. PhytAMP may be accessed free of charge at <ext-link ext-link-type="uri" xlink:href="http://phytamp.pfba-lab.org">http://phytamp.pfba-lab.org</ext-link>
.</p>
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</TEI>
<affiliations><list><country><li>Canada</li>
<li>France</li>
<li>Tunisie</li>
</country>
</list>
<tree><country name="Tunisie"><noRegion><name sortKey="Hammami, Riadh" sort="Hammami, Riadh" uniqKey="Hammami R" first="Riadh" last="Hammami">Riadh Hammami</name>
</noRegion>
<name sortKey="Ben Hamida, Jeannette" sort="Ben Hamida, Jeannette" uniqKey="Ben Hamida J" first="Jeannette" last="Ben Hamida">Jeannette Ben Hamida</name>
</country>
<country name="France"><noRegion><name sortKey="Hammami, Riadh" sort="Hammami, Riadh" uniqKey="Hammami R" first="Riadh" last="Hammami">Riadh Hammami</name>
</noRegion>
<name sortKey="Vergoten, Gerard" sort="Vergoten, Gerard" uniqKey="Vergoten G" first="Gérard" last="Vergoten">Gérard Vergoten</name>
</country>
<country name="Canada"><noRegion><name sortKey="Hammami, Riadh" sort="Hammami, Riadh" uniqKey="Hammami R" first="Riadh" last="Hammami">Riadh Hammami</name>
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<name sortKey="Fliss, Ismail" sort="Fliss, Ismail" uniqKey="Fliss I" first="Ismail" last="Fliss">Ismail Fliss</name>
</country>
</tree>
</affiliations>
</record>
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