Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1997-2-3
|
pubmed:abstractText |
Among the synthetic peptides derived from the 28-kDa Schistosoma mansoni gluthatione-S-transferase (Sm28GST), the C-terminal peptide, comprising amino acid residues 190 to 211, represents a major T-cell epitope in both infected humans and Sm28GST-immunized mice. The aim of this study was to determine the nature of the immune response induced by the 190-211 peptide coupled to a fatty acid (lipopeptide construction) in comparison to the free form. We explored B- and T-cell responses elicited by these two peptidic constructions in three different mouse strains (BALB/c, CBA/N and C57B1/6). For all strains, the addition of a lipid chain to the 190-211 peptide greatly modified its immunogenicity. The lipopeptide, compared to the free form, induced a greatly reduced antibody response against the peptide, whereas the production of messenger for cytokines was greatly increased after immunization with the lipopeptide. Immunization with peptide led mainly to a Th1-type cytokine profile following antigenic restimulation in vitro, while lipopeptide, in general, induced a mixed profile, and that occurred most significantly with the production of messengers for the protective cytokines IFN-gamma and IL-2, even without antigenic restimulations. This modification of immunogenicity of a peptide by the addition of a lipid chain could be of value in the development of efficient peptide vaccines.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoconjugates,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/P28 antigen, Schistosoma,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
|
pubmed:status |
MEDLINE
|
pubmed:issn |
1040-5704
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
136-43
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8875593-Animals,
pubmed-meshheading:8875593-Antigens, Helminth,
pubmed-meshheading:8875593-B-Lymphocytes,
pubmed-meshheading:8875593-Drug Administration Routes,
pubmed-meshheading:8875593-Helminth Proteins,
pubmed-meshheading:8875593-Immunization,
pubmed-meshheading:8875593-Immunoconjugates,
pubmed-meshheading:8875593-Lipoproteins,
pubmed-meshheading:8875593-Lymphocyte Activation,
pubmed-meshheading:8875593-Mice,
pubmed-meshheading:8875593-Mice, Inbred BALB C,
pubmed-meshheading:8875593-Mice, Inbred C57BL,
pubmed-meshheading:8875593-Mice, Inbred CBA,
pubmed-meshheading:8875593-Peptide Fragments,
pubmed-meshheading:8875593-Species Specificity,
pubmed-meshheading:8875593-T-Lymphocytes
|
pubmed:articleTitle |
Comparison of the immune response elicited by a free peptide and a lipopeptide construct.
|
pubmed:affiliation |
CNRS URA 1854, Institut Pasteur, Lille, France.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|