Source:http://linkedlifedata.com/resource/pubmed/id/15752762
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2005-3-8
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| pubmed:abstractText |
The C-terminal portion of the Plasmodium falciparum blood stage MSP-1 antigen plays a key role in invasion of human erythrocytes. The MSP-1(1282-1301) non-polymorphic 1585 peptide, from the processed MSP-1(42) fragment, is poorly immunogenic and highly alpha-helical [Angew. Chem. Int. Ed. 40 (2001) 4654]. Assessing the alpha-carbon asymmetry and its implication in the host immune response is proposed in this work to overcome the 1585 peptide's immunological properties. Accordingly, the effect of incorporating single D-amino acids and psi-[CH(2)-NH] isoster bonds into the 1585 peptide was examined both at the immunogenic and 3D-structure levels. Therefore, specific binding to RBCs is promoted by site-directed chiral modifications on the native peptide as well as by simultaneously combining specific D-substitutions with psi-[CH(2)-NH] isoster bonds transforming this molecule into a high specific HLAbeta1*1101 allele binder. D-analog pseudopeptide immunized animals induced antibodies selectively recognizing a recombinant as well as native MSP-1(42) and MSP-1(33) fragments. Protection and low parasitemia levels were induced in Aotus monkeys immunized with the EVLYL(dK)PLAGVYRSLKKQLE analog. Peptide alpha-carbon chiral transformation is therefore an important target for structural modulation and, consequently, represents a novel approach towards designing multi-component subunit-based malarial vaccines.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0006-291X
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| pubmed:author |
pubmed-author:CortésJimenaJ,
pubmed-author:EspejoFabiolaF,
pubmed-author:LesmesLilianaL,
pubmed-author:LozanoJosé ManuelJM,
pubmed-author:PatarroyoManuel ElkinME,
pubmed-author:RosasJaiverJ,
pubmed-author:SilvaYolandaY,
pubmed-author:TorresElizabethE,
pubmed-author:VargasLuis EduardoLE,
pubmed-author:VeraRicardoR
|
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
329
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1053-66
|
| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15752762-Amino Acid Substitution,
pubmed-meshheading:15752762-Animals,
pubmed-meshheading:15752762-Antimalarials,
pubmed-meshheading:15752762-Aotidae,
pubmed-meshheading:15752762-Binding Sites,
pubmed-meshheading:15752762-Cells, Cultured,
pubmed-meshheading:15752762-Computer Simulation,
pubmed-meshheading:15752762-Humans,
pubmed-meshheading:15752762-Isomerism,
pubmed-meshheading:15752762-Malaria, Falciparum,
pubmed-meshheading:15752762-Malaria Vaccines,
pubmed-meshheading:15752762-Mice,
pubmed-meshheading:15752762-Mice, Inbred BALB C,
pubmed-meshheading:15752762-Models, Molecular,
pubmed-meshheading:15752762-Plasmodium falciparum,
pubmed-meshheading:15752762-Protein Binding,
pubmed-meshheading:15752762-Protein Conformation,
pubmed-meshheading:15752762-Structure-Activity Relationship,
pubmed-meshheading:15752762-Subtilisins,
pubmed-meshheading:15752762-Women
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| pubmed:year |
2005
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| pubmed:articleTitle |
Protection against malaria induced by chirally modified Plasmodium falciparum's MSP-1 42 pseudopeptides.
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| pubmed:affiliation |
Fundación Instituto de Inmunología de Colombia (FIDIC), Bogotá D.C., Colombia. jm_lozano@fidic.org.co
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|