Thymic stromal lymphopoietin exerts antimicrobial activities.
Identifieur interne : 002419 ( Main/Exploration ); précédent : 002418; suivant : 002420Thymic 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:
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Le document en format XML
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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. 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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 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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)
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