MersV1, Main, Exploration, bibRecord, 004160

Mapping of the linear antigenic determinants from the Leishmania infantum histone H2A recognized by sera from dogs with leishmaniasis

Identifieur interne : 004160 ( Main/Exploration ); précédent : 004159; suivant : 004161

Mapping of the linear antigenic determinants from the Leishmania infantum histone H2A recognized by sera from dogs with leishmaniasis

Auteurs : Manuel Soto [Espagne] ; Jose M. Requena [Espagne] ; Luis Quijada [Espagne] ; Mercedes García [Espagne] ; Fanny Guzman [Colombie] ; Manuel E. Patarroyo [Colombie] ; Carlos Alonso [Espagne]

Source :

Immunology Letters [ 0165-2478 ] ; 1995.

RBID : ISTEX:978DB23AE0C2B15BEE956E2476796FAB1857EC92

English descriptors

KwdEn :
- Anti-histone antibody, B-cell epitope, Canine leishmaniasis, Histone H2A, Synthetic peptide.
Teeft :
- Absorbance, Absorbance values, Amino, Amino acids, Antigenic, Antigenic determinants, Calf thymus histones, Canine, Canine leishmaniasis sera, Cruzi, Determinant, Histone, Histone protein, Humoral, Humoral response, Immunology, Immunology letters, Infantum, Infantum histone, Leishmania, Leishmania histone, Leishmania infection, Leishmaniasis, Leishmaniasis sera, Nucleic acids, Parasite, Peptide, Reactivity values, Rlih2a, Room temperature, Soto, Specific antibodies, Synthetic peptides.

Abstract

Abstract: Antibodies reacting against the H2A histone protein were frequently observed in the sera from dogs naturally infected with the protozoan parasite Leishmania infantum. Using synthetic peptides covering the complete sequence of the protein we have identified the amino terminal region, comprising from amino acids 1 to 20, and the carboxyl terminal region, comprising from amino acids 106 to 132, as conforming the antigenic determinants of the protein. Those regions, exposed in the nucleosome surface, are highly divergent in sequence relative to the mammalian H2A histones. The anti-H2A histone antibodies present in the sera of these dogs specifically recognize the L. infantum H2A histone and they do not react with mammalian histones. The present data indicate that, in spite of the evolutionary conservation of the H2A histone protein among eukaryotic organisms, the humoral response against this protein during natural infection is specifically triggered by the parasite protein antigenic determinants.

Url:

https://api.istex.fr/ark:/67375/6H6-FR1N5K3C-F/fulltext.pdf

DOI: 10.1016/0165-2478(95)02473-5

Affiliations:

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Le document en format XML

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<term>Antigenic determinants</term>
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<front><div type="abstract" xml:lang="en">Abstract: Antibodies reacting against the H2A histone protein were frequently observed in the sera from dogs naturally infected with the protozoan parasite Leishmania infantum. Using synthetic peptides covering the complete sequence of the protein we have identified the amino terminal region, comprising from amino acids 1 to 20, and the carboxyl terminal region, comprising from amino acids 106 to 132, as conforming the antigenic determinants of the protein. Those regions, exposed in the nucleosome surface, are highly divergent in sequence relative to the mammalian H2A histones. The anti-H2A histone antibodies present in the sera of these dogs specifically recognize the L. infantum H2A histone and they do not react with mammalian histones. The present data indicate that, in spite of the evolutionary conservation of the H2A histone protein among eukaryotic organisms, the humoral response against this protein during natural infection is specifically triggered by the parasite protein antigenic determinants.</div>
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Mapping of the linear antigenic determinants from the Leishmania infantum histone H2A recognized by sera from dogs with leishmaniasis

Mapping of the linear antigenic determinants from the Leishmania infantum histone H2A recognized by sera from dogs with leishmaniasis

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri