Computer-assisted prediction of HLA-DR binding and experimental analysis for human promiscuous Th1-cell peptides in the 24 kDa secreted lipoprotein (LppX) of Mycobacterium tuberculosis.
Identifieur interne : 002415 ( PubMed/Corpus ); précédent : 002414; suivant : 002416Computer-assisted prediction of HLA-DR binding and experimental analysis for human promiscuous Th1-cell peptides in the 24 kDa secreted lipoprotein (LppX) of Mycobacterium tuberculosis.
Auteurs : R. Al-Attiyah ; A S MustafaSource :
- Scandinavian journal of immunology [ 0300-9475 ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antigens, Bacterial (immunology), BCG Vaccine, Computer Simulation, Epitope Mapping (methods), Epitopes, T-Lymphocyte (chemistry), HLA-DR Antigens (immunology), HLA-DR Antigens (metabolism), Humans, Molecular Sequence Data, Mycobacterium tuberculosis (immunology), Peptides (immunology), Peptides (metabolism), Sequence Homology, Th1 Cells (immunology), Th1 Cells (metabolism).
- MESH :
- chemical , chemistry : Epitopes, T-Lymphocyte.
- chemical , immunology : Antigens, Bacterial, HLA-DR Antigens, Peptides.
- chemical , metabolism : HLA-DR Antigens, Peptides.
- immunology : Mycobacterium tuberculosis, Th1 Cells.
- metabolism : Th1 Cells.
- methods : Epitope Mapping.
- Amino Acid Sequence, Animals, BCG Vaccine, Computer Simulation, Humans, Molecular Sequence Data, Sequence Homology.
Abstract
The secreted 24 kDa lipoprotein (LppX) is an antigen that is specific for Mycobacterium tuberculosis complex and M. leprae. The present study was carried out to identify the promiscuous T helper 1 (Th1)-cell epitopes of the M. tuberculosis LppX (MT24, Rv2945c) antigen by using 15 overlapping synthetic peptides (25 mers overlapping by 10 residues) covering the sequence of the complete protein. The analysis of Rv2945c sequence for binding to 51 alleles of nine serologically defined HLA-DR molecules, by using a virtual matrix-based prediction program (propred), showed that eight of the 15 peptides of Rv2945c were predicted to bind promiscuously to >/=10 alleles from more than or equal to three serologically defined HLA-DR molecules. The Th1-cell reactivity of all the peptides was assessed in antigen-induced proliferation and interferon-gamma (IFN-gamma)-secretion assays with peripheral blood mononuclear cells (PBMCs) from 37 bacille Calmette-Guérin (BCG)-vaccinated healthy subjects. The results showed that 17 of the 37 donors, which represented an HLA-DR-heterogeneous group, responded to one or more peptides of Rv2945c in the Th1-cell assays. Although each peptide stimulated PBMCs from one or more donors in the above assays, the best positive responses (12/17 (71%) responders) were observed with the peptide p14 (aa 196-220). This suggested a highly promiscuous presentation of p14 to Th1 cells. In addition, the sequence of p14 is completely identical among the LppX of M. tuberculosis, M. bovis and M. leprae, which further supports the usefulness of Rv2945c and p14 in the subunit vaccine design against both tuberculosis and leprosy.
DOI: 10.1111/j.0300-9475.2004.01349.x
PubMed: 14723617
Links to Exploration step
pubmed:14723617Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Computer-assisted prediction of HLA-DR binding and experimental analysis for human promiscuous Th1-cell peptides in the 24 kDa secreted lipoprotein (LppX) of Mycobacterium tuberculosis.</title><author><name sortKey="Al Attiyah, R" sort="Al Attiyah, R" uniqKey="Al Attiyah R" first="R" last="Al-Attiyah">R. Al-Attiyah</name><affiliation><nlm:affiliation>Department of Microbiology, Faculty of Medicine, Kuwait University, Safat, Kuwait. alattiyah@hsc.kuniv.edu.kw</nlm:affiliation></affiliation></author><author><name sortKey="Mustafa, A S" sort="Mustafa, A S" uniqKey="Mustafa A" first="A S" last="Mustafa">A S Mustafa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:14723617</idno><idno type="pmid">14723617</idno><idno type="doi">10.1111/j.0300-9475.2004.01349.x</idno><idno type="wicri:Area/PubMed/Corpus">002415</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002415</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Computer-assisted prediction of HLA-DR binding and experimental analysis for human promiscuous Th1-cell peptides in the 24 kDa secreted lipoprotein (LppX) of Mycobacterium tuberculosis.</title><author><name sortKey="Al Attiyah, R" sort="Al Attiyah, R" uniqKey="Al Attiyah R" first="R" last="Al-Attiyah">R. Al-Attiyah</name><affiliation><nlm:affiliation>Department of Microbiology, Faculty of Medicine, Kuwait University, Safat, Kuwait. alattiyah@hsc.kuniv.edu.kw</nlm:affiliation></affiliation></author><author><name sortKey="Mustafa, A S" sort="Mustafa, A S" uniqKey="Mustafa A" first="A S" last="Mustafa">A S Mustafa</name></author></analytic><series><title level="j">Scandinavian journal of immunology</title><idno type="ISSN">0300-9475</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antigens, Bacterial (immunology)</term><term>BCG Vaccine</term><term>Computer Simulation</term><term>Epitope Mapping (methods)</term><term>Epitopes, T-Lymphocyte (chemistry)</term><term>HLA-DR Antigens (immunology)</term><term>HLA-DR Antigens (metabolism)</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mycobacterium tuberculosis (immunology)</term><term>Peptides (immunology)</term><term>Peptides (metabolism)</term><term>Sequence Homology</term><term>Th1 Cells (immunology)</term><term>Th1 Cells (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Epitopes, T-Lymphocyte</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Bacterial</term><term>HLA-DR Antigens</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>HLA-DR Antigens</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Mycobacterium tuberculosis</term><term>Th1 Cells</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Th1 Cells</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Epitope Mapping</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>BCG Vaccine</term><term>Computer Simulation</term><term>Humans</term><term>Molecular Sequence Data</term><term>Sequence Homology</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The secreted 24 kDa lipoprotein (LppX) is an antigen that is specific for Mycobacterium tuberculosis complex and M. leprae. The present study was carried out to identify the promiscuous T helper 1 (Th1)-cell epitopes of the M. tuberculosis LppX (MT24, Rv2945c) antigen by using 15 overlapping synthetic peptides (25 mers overlapping by 10 residues) covering the sequence of the complete protein. The analysis of Rv2945c sequence for binding to 51 alleles of nine serologically defined HLA-DR molecules, by using a virtual matrix-based prediction program (propred), showed that eight of the 15 peptides of Rv2945c were predicted to bind promiscuously to >/=10 alleles from more than or equal to three serologically defined HLA-DR molecules. The Th1-cell reactivity of all the peptides was assessed in antigen-induced proliferation and interferon-gamma (IFN-gamma)-secretion assays with peripheral blood mononuclear cells (PBMCs) from 37 bacille Calmette-Guérin (BCG)-vaccinated healthy subjects. The results showed that 17 of the 37 donors, which represented an HLA-DR-heterogeneous group, responded to one or more peptides of Rv2945c in the Th1-cell assays. Although each peptide stimulated PBMCs from one or more donors in the above assays, the best positive responses (12/17 (71%) responders) were observed with the peptide p14 (aa 196-220). This suggested a highly promiscuous presentation of p14 to Th1 cells. In addition, the sequence of p14 is completely identical among the LppX of M. tuberculosis, M. bovis and M. leprae, which further supports the usefulness of Rv2945c and p14 in the subunit vaccine design against both tuberculosis and leprosy.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14723617</PMID><DateCompleted><Year>2004</Year><Month>03</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0300-9475</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>1</Issue><PubDate><Year>2004</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Scandinavian journal of immunology</Title><ISOAbbreviation>Scand. J. Immunol.</ISOAbbreviation></Journal><ArticleTitle>Computer-assisted prediction of HLA-DR binding and experimental analysis for human promiscuous Th1-cell peptides in the 24 kDa secreted lipoprotein (LppX) of Mycobacterium tuberculosis.</ArticleTitle><Pagination><MedlinePgn>16-24</MedlinePgn></Pagination><Abstract><AbstractText>The secreted 24 kDa lipoprotein (LppX) is an antigen that is specific for Mycobacterium tuberculosis complex and M. leprae. The present study was carried out to identify the promiscuous T helper 1 (Th1)-cell epitopes of the M. tuberculosis LppX (MT24, Rv2945c) antigen by using 15 overlapping synthetic peptides (25 mers overlapping by 10 residues) covering the sequence of the complete protein. The analysis of Rv2945c sequence for binding to 51 alleles of nine serologically defined HLA-DR molecules, by using a virtual matrix-based prediction program (propred), showed that eight of the 15 peptides of Rv2945c were predicted to bind promiscuously to >/=10 alleles from more than or equal to three serologically defined HLA-DR molecules. The Th1-cell reactivity of all the peptides was assessed in antigen-induced proliferation and interferon-gamma (IFN-gamma)-secretion assays with peripheral blood mononuclear cells (PBMCs) from 37 bacille Calmette-Guérin (BCG)-vaccinated healthy subjects. The results showed that 17 of the 37 donors, which represented an HLA-DR-heterogeneous group, responded to one or more peptides of Rv2945c in the Th1-cell assays. Although each peptide stimulated PBMCs from one or more donors in the above assays, the best positive responses (12/17 (71%) responders) were observed with the peptide p14 (aa 196-220). This suggested a highly promiscuous presentation of p14 to Th1 cells. In addition, the sequence of p14 is completely identical among the LppX of M. tuberculosis, M. bovis and M. leprae, which further supports the usefulness of Rv2945c and p14 in the subunit vaccine design against both tuberculosis and leprosy.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Al-Attiyah</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Faculty of Medicine, Kuwait University, Safat, Kuwait. alattiyah@hsc.kuniv.edu.kw</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mustafa</LastName><ForeName>A S</ForeName><Initials>AS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Scand J Immunol</MedlineTA><NlmUniqueID>0323767</NlmUniqueID><ISSNLinking>0300-9475</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000942">Antigens, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001500">BCG Vaccine</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018984">Epitopes, T-Lymphocyte</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006684">HLA-DR Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>144058-44-6</RegistryNumber><NameOfSubstance UI="C072681">Mycobacterium tuberculosis antigens</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000942" MajorTopicYN="N">Antigens, Bacterial</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001500" MajorTopicYN="N">BCG Vaccine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003198" MajorTopicYN="N">Computer Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018604" MajorTopicYN="Y">Epitope Mapping</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018984" MajorTopicYN="N">Epitopes, T-Lymphocyte</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006684" MajorTopicYN="N">HLA-DR Antigens</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009169" MajorTopicYN="N">Mycobacterium tuberculosis</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017385" MajorTopicYN="N">Sequence Homology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018417" MajorTopicYN="N">Th1 Cells</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>1</Month><Day>16</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>3</Month><Day>11</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>1</Month><Day>16</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14723617</ArticleId><ArticleId IdType="pii">1349</ArticleId><ArticleId IdType="doi">10.1111/j.0300-9475.2004.01349.x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002415 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002415 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:14723617
|texte= Computer-assisted prediction of HLA-DR binding and experimental analysis for human promiscuous Th1-cell peptides in the 24 kDa secreted lipoprotein (LppX) of Mycobacterium tuberculosis.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:14723617" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |