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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2001-10-4
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pubmed:abstractText |
We report for the first time the immunoadjuvant effects of lipoconjugation of peptide antigens in an in vitro system by using CD4+ T-cells. The lipopeptides obtained by conjugating a palmitoyl moiety at the N(alpha)-terminal of Gln(74) or at the epsilon-NH(2) of Lys(75) of GpMBP(74-85) induced increased T-cell responsiveness compared to the native nonlipidated peptide. On the other hand, lipoderivatives of GpMBP(82-98) did not increase the T-cell response, demonstrating that the superagonist inducing effect of lipoconjugation is epitope-specific. Digestion of the two native peptides with cathepsin D and L, both implicated in antigen processing, and with a complete lysosomal fraction of a EBV-transformed B cell line shows that GpMBP(74-85) is resistant to cellular proteases, while GpMBP(82-98) is easily digested by these enzymes. These results suggest that the first prerequisite for increasing the T-cell response by lipoconjugation is the stability of the native peptide to peptidases, providing an important insight into the understanding of the immunoadjuvant effect of lipoderivative antigens.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Basic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-2623
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pubmed:author |
pubmed-author:BalleriniCC,
pubmed-author:BeckHH,
pubmed-author:BiagioliTT,
pubmed-author:ChelliMM,
pubmed-author:DeenDD,
pubmed-author:GinanneschiMM,
pubmed-author:KalbacherHH,
pubmed-author:MassacesiLL,
pubmed-author:MazzantiBB,
pubmed-author:NardiEE,
pubmed-author:PapiniA MAM,
pubmed-author:TraggiaiEE,
pubmed-author:VergelliMM
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3504-10
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11585454-Animals,
pubmed-meshheading:11585454-CD4-Positive T-Lymphocytes,
pubmed-meshheading:11585454-Cathepsin D,
pubmed-meshheading:11585454-Cathepsin L,
pubmed-meshheading:11585454-Cathepsins,
pubmed-meshheading:11585454-Cell Division,
pubmed-meshheading:11585454-Cysteine Endopeptidases,
pubmed-meshheading:11585454-Epitopes,
pubmed-meshheading:11585454-Female,
pubmed-meshheading:11585454-Lipoproteins,
pubmed-meshheading:11585454-Lysosomes,
pubmed-meshheading:11585454-Myelin Basic Proteins,
pubmed-meshheading:11585454-Palmitic Acid,
pubmed-meshheading:11585454-Peptide Fragments,
pubmed-meshheading:11585454-Peptide Hydrolases,
pubmed-meshheading:11585454-Rats,
pubmed-meshheading:11585454-Rats, Inbred Lew,
pubmed-meshheading:11585454-Structure-Activity Relationship
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pubmed:year |
2001
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pubmed:articleTitle |
Palmitoyl derivatives of GpMBP epitopes: T-cell response and peptidases susceptibility.
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pubmed:affiliation |
Dipartimento di Chimica Organica "Ugo Schiff" and Centro di Studio sulla Chimica e la Struttura dei Composti Eterociclici e loro Applicazioni del C.N.R., Polo Scientifico Universitario, Sesto Fiorentino, Italy. annamaria.papini@unifi.it
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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