Thymic stromal lymphopoietin exerts antimicrobial activities.
Identifieur interne : 000901 ( Ncbi/Checkpoint ); précédent : 000900; suivant : 000902Thymic stromal lymphopoietin exerts antimicrobial activities.
Auteurs : Andreas Sonesson [Suède] ; Gopinath Kasetty ; Anders I. Olin ; Martin Malmsten ; Matthias Mörgelin ; Ole E. S Rensen ; Artur SchmidtchenSource :
- Experimental dermatology [ 1600-0625 ] ; 2011.
Descripteurs français
- KwdFr :
- Anti-infectieux (métabolisme), Anti-infectieux (pharmacologie), Candida albicans (), Cytokines (métabolisme), Cytokines (pharmacologie), Données de séquences moléculaires, Escherichia coli (), Fragments peptidiques (pharmacologie), Humains, Leukocyte elastase (métabolisme), Liposomes (métabolisme), Metalloendopeptidases (métabolisme), Peptide hydrolases (métabolisme), Peptides antimicrobiens cationiques (pharmacologie), Perméabilité (), Perméabilité de la membrane cellulaire (), Protéines bactériennes (métabolisme), Protéines recombinantes (pharmacologie), Pseudomonas aeruginosa (), Pseudomonas aeruginosa (enzymologie), Staphylococcus aureus (enzymologie), Staphylococcus epidermidis (), Survie cellulaire (), Séquence d'acides aminés, Tests de sensibilité microbienne.
- MESH :
- enzymologie : Pseudomonas aeruginosa, Staphylococcus aureus.
- métabolisme : Anti-infectieux, Cytokines, Leukocyte elastase, Liposomes, Metalloendopeptidases, Peptide hydrolases, Protéines bactériennes.
- pharmacologie : Anti-infectieux, Cytokines, Fragments peptidiques, Peptides antimicrobiens cationiques, Protéines recombinantes.
- Candida albicans, Données de séquences moléculaires, Escherichia coli, Humains, Perméabilité, Perméabilité de la membrane cellulaire, Pseudomonas aeruginosa, Staphylococcus epidermidis, Survie cellulaire, Séquence d'acides aminés, Tests de sensibilité microbienne.
English descriptors
- KwdEn :
- Amino Acid Sequence, Anti-Infective Agents (metabolism), Anti-Infective Agents (pharmacology), Antimicrobial Cationic Peptides (pharmacology), Bacterial Proteins (metabolism), Candida albicans (drug effects), Cell Membrane Permeability (drug effects), Cell Survival (drug effects), Cytokines (metabolism), Cytokines (pharmacology), Escherichia coli (drug effects), Humans, Leukocyte Elastase (metabolism), Liposomes (metabolism), Metalloendopeptidases (metabolism), Microbial Sensitivity Tests, Molecular Sequence Data, Peptide Fragments (pharmacology), Peptide Hydrolases (metabolism), Permeability (drug effects), Pseudomonas aeruginosa (drug effects), Pseudomonas aeruginosa (enzymology), Recombinant Proteins (pharmacology), Staphylococcus aureus (enzymology), Staphylococcus epidermidis (drug effects).
- MESH :
- chemical , metabolism : Anti-Infective Agents, Bacterial Proteins, Cytokines, Leukocyte Elastase, Liposomes, Metalloendopeptidases, Peptide Hydrolases.
- chemical , pharmacology : Anti-Infective Agents, Antimicrobial Cationic Peptides, Cytokines, Peptide Fragments, Recombinant Proteins.
- drug effects : Candida albicans, Cell Membrane Permeability, Cell Survival, Escherichia coli, Permeability, Pseudomonas aeruginosa, Staphylococcus epidermidis.
- enzymology : Pseudomonas aeruginosa, Staphylococcus aureus.
- Amino Acid Sequence, Humans, Microbial Sensitivity Tests, Molecular Sequence Data.
Abstract
Thymic stromal lymphopoietin (TSLP) is an interleukin-7-like cytokine expressed by epithelial cells and reported to be involved in allergic diseases and atopic eczema. The presence of several predicted α-helical regions in TSPL, a structure characterizing many classical antimicrobial peptides (AMPs), prompted us to investigate whether TSLP exerts antimicrobial activities. Recombinant human TSLP exerted antimicrobial activity, particularly against Gram-negative bacteria. Using synthetic overlapping peptide 20-mers of TSLP, it was demonstrated that the antimicrobial effect is primarily mediated by the C-terminal region of the protein. MKK34 (MKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLK), a peptide spanning a C-terminal α-helical region in TSLP, showed potent antimicrobial activities, in physiological salt conditions and in the presence of human plasma. Fluorescent studies of peptide-treated bacteria, electron microscopy and liposome leakage models showed that MKK34 exerted membrane-disrupting effects comparable to those of the classical AMP LL-37. Moreover, TSLP was degraded into multiple fragments by staphylococcal V8 proteinase. One major antimicrobial degradation fragment was found to encompass the C-terminal antimicrobial region defined by the MKK34 peptide. We here describe a novel antimicrobial role for TSLP. The antimicrobial activity is primarily mediated by the C-terminal part of the protein. In combination with the previously known cytokine function of TSLP, our result indicates dual functions of the molecule and a previously unknown role in host defense.
DOI: 10.1111/j.1600-0625.2011.01391.x
PubMed: 22092577
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001E35
- to stream PubMed, to step Curation: 001E35
- to stream PubMed, to step Checkpoint: 001D30
- to stream Ncbi, to step Merge: 000901
- to stream Ncbi, to step Curation: 000901
Links to Exploration step
pubmed:22092577Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Thymic stromal lymphopoietin exerts antimicrobial activities.</title>
<author><name sortKey="Sonesson, Andreas" sort="Sonesson, Andreas" uniqKey="Sonesson A" first="Andreas" last="Sonesson">Andreas Sonesson</name>
<affiliation wicri:level="1"><nlm:affiliation>Divisions of Dermatology and Venereology Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden. andreas.sonesson@med.lu.se</nlm:affiliation>
<country xml:lang="fr">Suède</country>
<wicri:regionArea>Divisions of Dermatology and Venereology Infection Medicine, Department of Clinical Sciences, Lund University, Lund</wicri:regionArea>
<wicri:noRegion>Lund</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kasetty, Gopinath" sort="Kasetty, Gopinath" uniqKey="Kasetty G" first="Gopinath" last="Kasetty">Gopinath Kasetty</name>
</author>
<author><name sortKey="Olin, Anders I" sort="Olin, Anders I" uniqKey="Olin A" first="Anders I" last="Olin">Anders I. Olin</name>
</author>
<author><name sortKey="Malmsten, Martin" sort="Malmsten, Martin" uniqKey="Malmsten M" first="Martin" last="Malmsten">Martin Malmsten</name>
</author>
<author><name sortKey="Morgelin, Matthias" sort="Morgelin, Matthias" uniqKey="Morgelin M" first="Matthias" last="Mörgelin">Matthias Mörgelin</name>
</author>
<author><name sortKey="S Rensen, Ole E" sort="S Rensen, Ole E" uniqKey="S Rensen O" first="Ole E" last="S Rensen">Ole E. S Rensen</name>
</author>
<author><name sortKey="Schmidtchen, Artur" sort="Schmidtchen, Artur" uniqKey="Schmidtchen A" first="Artur" last="Schmidtchen">Artur Schmidtchen</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2011">2011</date>
<idno type="RBID">pubmed:22092577</idno>
<idno type="pmid">22092577</idno>
<idno type="doi">10.1111/j.1600-0625.2011.01391.x</idno>
<idno type="wicri:Area/PubMed/Corpus">001E35</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001E35</idno>
<idno type="wicri:Area/PubMed/Curation">001E35</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001E35</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001D30</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001D30</idno>
<idno type="wicri:Area/Ncbi/Merge">000901</idno>
<idno type="wicri:Area/Ncbi/Curation">000901</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000901</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Thymic stromal lymphopoietin exerts antimicrobial activities.</title>
<author><name sortKey="Sonesson, Andreas" sort="Sonesson, Andreas" uniqKey="Sonesson A" first="Andreas" last="Sonesson">Andreas Sonesson</name>
<affiliation wicri:level="1"><nlm:affiliation>Divisions of Dermatology and Venereology Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden. andreas.sonesson@med.lu.se</nlm:affiliation>
<country xml:lang="fr">Suède</country>
<wicri:regionArea>Divisions of Dermatology and Venereology Infection Medicine, Department of Clinical Sciences, Lund University, Lund</wicri:regionArea>
<wicri:noRegion>Lund</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kasetty, Gopinath" sort="Kasetty, Gopinath" uniqKey="Kasetty G" first="Gopinath" last="Kasetty">Gopinath Kasetty</name>
</author>
<author><name sortKey="Olin, Anders I" sort="Olin, Anders I" uniqKey="Olin A" first="Anders I" last="Olin">Anders I. Olin</name>
</author>
<author><name sortKey="Malmsten, Martin" sort="Malmsten, Martin" uniqKey="Malmsten M" first="Martin" last="Malmsten">Martin Malmsten</name>
</author>
<author><name sortKey="Morgelin, Matthias" sort="Morgelin, Matthias" uniqKey="Morgelin M" first="Matthias" last="Mörgelin">Matthias Mörgelin</name>
</author>
<author><name sortKey="S Rensen, Ole E" sort="S Rensen, Ole E" uniqKey="S Rensen O" first="Ole E" last="S Rensen">Ole E. S Rensen</name>
</author>
<author><name sortKey="Schmidtchen, Artur" sort="Schmidtchen, Artur" uniqKey="Schmidtchen A" first="Artur" last="Schmidtchen">Artur Schmidtchen</name>
</author>
</analytic>
<series><title level="j">Experimental dermatology</title>
<idno type="eISSN">1600-0625</idno>
<imprint><date when="2011" type="published">2011</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Anti-Infective Agents (metabolism)</term>
<term>Anti-Infective Agents (pharmacology)</term>
<term>Antimicrobial Cationic Peptides (pharmacology)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Candida albicans (drug effects)</term>
<term>Cell Membrane Permeability (drug effects)</term>
<term>Cell Survival (drug effects)</term>
<term>Cytokines (metabolism)</term>
<term>Cytokines (pharmacology)</term>
<term>Escherichia coli (drug effects)</term>
<term>Humans</term>
<term>Leukocyte Elastase (metabolism)</term>
<term>Liposomes (metabolism)</term>
<term>Metalloendopeptidases (metabolism)</term>
<term>Microbial Sensitivity Tests</term>
<term>Molecular Sequence Data</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Peptide Hydrolases (metabolism)</term>
<term>Permeability (drug effects)</term>
<term>Pseudomonas aeruginosa (drug effects)</term>
<term>Pseudomonas aeruginosa (enzymology)</term>
<term>Recombinant Proteins (pharmacology)</term>
<term>Staphylococcus aureus (enzymology)</term>
<term>Staphylococcus epidermidis (drug effects)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Anti-infectieux (métabolisme)</term>
<term>Anti-infectieux (pharmacologie)</term>
<term>Candida albicans ()</term>
<term>Cytokines (métabolisme)</term>
<term>Cytokines (pharmacologie)</term>
<term>Données de séquences moléculaires</term>
<term>Escherichia coli ()</term>
<term>Fragments peptidiques (pharmacologie)</term>
<term>Humains</term>
<term>Leukocyte elastase (métabolisme)</term>
<term>Liposomes (métabolisme)</term>
<term>Metalloendopeptidases (métabolisme)</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Peptides antimicrobiens cationiques (pharmacologie)</term>
<term>Perméabilité ()</term>
<term>Perméabilité de la membrane cellulaire ()</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Protéines recombinantes (pharmacologie)</term>
<term>Pseudomonas aeruginosa ()</term>
<term>Pseudomonas aeruginosa (enzymologie)</term>
<term>Staphylococcus aureus (enzymologie)</term>
<term>Staphylococcus epidermidis ()</term>
<term>Survie cellulaire ()</term>
<term>Séquence d'acides aminés</term>
<term>Tests de sensibilité microbienne</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anti-Infective Agents</term>
<term>Bacterial Proteins</term>
<term>Cytokines</term>
<term>Leukocyte Elastase</term>
<term>Liposomes</term>
<term>Metalloendopeptidases</term>
<term>Peptide Hydrolases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-Infective Agents</term>
<term>Antimicrobial Cationic Peptides</term>
<term>Cytokines</term>
<term>Peptide Fragments</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Candida albicans</term>
<term>Cell Membrane Permeability</term>
<term>Cell Survival</term>
<term>Escherichia coli</term>
<term>Permeability</term>
<term>Pseudomonas aeruginosa</term>
<term>Staphylococcus epidermidis</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Pseudomonas aeruginosa</term>
<term>Staphylococcus aureus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pseudomonas aeruginosa</term>
<term>Staphylococcus aureus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Anti-infectieux</term>
<term>Cytokines</term>
<term>Leukocyte elastase</term>
<term>Liposomes</term>
<term>Metalloendopeptidases</term>
<term>Peptide hydrolases</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Anti-infectieux</term>
<term>Cytokines</term>
<term>Fragments peptidiques</term>
<term>Peptides antimicrobiens cationiques</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Humans</term>
<term>Microbial Sensitivity Tests</term>
<term>Molecular Sequence Data</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Candida albicans</term>
<term>Données de séquences moléculaires</term>
<term>Escherichia coli</term>
<term>Humains</term>
<term>Perméabilité</term>
<term>Perméabilité de la membrane cellulaire</term>
<term>Pseudomonas aeruginosa</term>
<term>Staphylococcus epidermidis</term>
<term>Survie cellulaire</term>
<term>Séquence d'acides aminés</term>
<term>Tests de sensibilité microbienne</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Thymic stromal lymphopoietin (TSLP) is an interleukin-7-like cytokine expressed by epithelial cells and reported to be involved in allergic diseases and atopic eczema. The presence of several predicted α-helical regions in TSPL, a structure characterizing many classical antimicrobial peptides (AMPs), prompted us to investigate whether TSLP exerts antimicrobial activities. Recombinant human TSLP exerted antimicrobial activity, particularly against Gram-negative bacteria. Using synthetic overlapping peptide 20-mers of TSLP, it was demonstrated that the antimicrobial effect is primarily mediated by the C-terminal region of the protein. MKK34 (MKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLK), a peptide spanning a C-terminal α-helical region in TSLP, showed potent antimicrobial activities, in physiological salt conditions and in the presence of human plasma. Fluorescent studies of peptide-treated bacteria, electron microscopy and liposome leakage models showed that MKK34 exerted membrane-disrupting effects comparable to those of the classical AMP LL-37. Moreover, TSLP was degraded into multiple fragments by staphylococcal V8 proteinase. One major antimicrobial degradation fragment was found to encompass the C-terminal antimicrobial region defined by the MKK34 peptide. We here describe a novel antimicrobial role for TSLP. The antimicrobial activity is primarily mediated by the C-terminal part of the protein. In combination with the previously known cytokine function of TSLP, our result indicates dual functions of the molecule and a previously unknown role in host defense.</div>
</front>
</TEI>
<affiliations><list><country><li>Suède</li>
</country>
</list>
<tree><noCountry><name sortKey="Kasetty, Gopinath" sort="Kasetty, Gopinath" uniqKey="Kasetty G" first="Gopinath" last="Kasetty">Gopinath Kasetty</name>
<name sortKey="Malmsten, Martin" sort="Malmsten, Martin" uniqKey="Malmsten M" first="Martin" last="Malmsten">Martin Malmsten</name>
<name sortKey="Morgelin, Matthias" sort="Morgelin, Matthias" uniqKey="Morgelin M" first="Matthias" last="Mörgelin">Matthias Mörgelin</name>
<name sortKey="Olin, Anders I" sort="Olin, Anders I" uniqKey="Olin A" first="Anders I" last="Olin">Anders I. Olin</name>
<name sortKey="S Rensen, Ole E" sort="S Rensen, Ole E" uniqKey="S Rensen O" first="Ole E" last="S Rensen">Ole E. S Rensen</name>
<name sortKey="Schmidtchen, Artur" sort="Schmidtchen, Artur" uniqKey="Schmidtchen A" first="Artur" last="Schmidtchen">Artur Schmidtchen</name>
</noCountry>
<country name="Suède"><noRegion><name sortKey="Sonesson, Andreas" sort="Sonesson, Andreas" uniqKey="Sonesson A" first="Andreas" last="Sonesson">Andreas Sonesson</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000901 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Checkpoint/biblio.hfd -nk 000901 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= Ncbi |étape= Checkpoint |type= RBID |clé= pubmed:22092577 |texte= Thymic stromal lymphopoietin exerts antimicrobial activities. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Checkpoint/RBID.i -Sk "pubmed:22092577" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Checkpoint/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
This area was generated with Dilib version V0.6.33. |