Pyruvate: ferredoxin oxidoreductase from Entamoeba histolytica recognized by a monoclonal antibody.
Southeast Asian J Trop Med Public Health
;
1996 Mar; 27(1): 63-70
Artigo
em Inglês
| IMSEAR
| ID: sea-33239
ABSTRACT
A mouse monoclonal antibody, Eh208C2-2 MAb, raised against whole cell antigens of Entamoeba histolytica trophozoites of the pathogenic strain HM-1 IMSS and polyclonal antisera (PAb) against membrane antigens of E. histolytica trophozoites of strain HTH-56 MUTM were screened against a cDNA library of the pathogenic strain, SFL3. The monoconal antibody detected many phage plaques expressing an E. histolytica protein. The DNA sequence encoding the protein was approximately 55% identical, over 1,100bp, to Trichomonas vaginalis pyruvate ferredoxin oxidoreductase (PFOR) and pyruvate flavodoxin oxidoreductase from Klebsiella pneumoniae, Anabaena variabilis and Enterobacter agglomerans. Two of seven clones detected by mouse polyclonal antisera also encoded this protein. Two others encoded Entamoeba Hsp70, another encoded Entamoeba alkyl-hydroperoxide reductase and the remaining two were unidentified sequences. Entamoeba PFOR is an abundant, antigenic protein which may be a useful target for the development of protective host immune responses against invasive amebiasis.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Dados de Sequência Molecular
/
Sequência de Bases
/
Biblioteca Gênica
/
Sequência de Aminoácidos
/
DNA Complementar
/
Entamoeba histolytica
/
Entamebíase
/
Piruvato Sintase
/
Cetona Oxirredutases
/
Animais
Idioma:
Inglês
Revista:
Southeast Asian J Trop Med Public Health
Ano de publicação:
1996
Tipo de documento:
Artigo
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