Characterization of a Plasmodium falciparum epitope recognized by a monoclonal antibody with broad isolate and species specificity.
Southeast Asian J Trop Med Public Health
;
1990 Sep; 21(3): 388-96
Article
Dans Anglais
| IMSEAR
| ID: sea-32324
ABSTRACT
Monoclonal antibody (MAb) 7H8 raised against Plasmodium yoelii reacted with a series of proteins from P. falciparum that range in molecular weight from 46 to 194 kDa. By immunofluorescence assay, this MAb reacted with all isolates of P. falciparum tested. MAb 7H8 was used to screen a genomic expression library of asexual blood stage antigens of P. falciparum, Malayan Camp K+ and 7 independent clones were identified. These 7 clones were sequenced and the epitope recognized by MAb 7H8 in the recombinant protein of one of these clones was mapped. This epitope contained Lys Tyr Pro as core amino acids. However, similar sequences were not found in the other clones, indicating that this MAb binds to a structural epitope formed by different amino acids. The variable composition of the epitope may account for the number of P. falciparum malarial proteins recognized by MAb 7H8.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Plasmodium falciparum
/
Protéines recombinantes
/
Données de séquences moléculaires
/
Séquence nucléotidique
/
Séquence d'acides aminés
/
Clones cellulaires
/
Animaux
/
Paludisme
/
Anticorps monoclonaux
/
Épitopes
Type d'étude:
Étude pronostique
langue:
Anglais
Texte intégral:
Southeast Asian J Trop Med Public Health
Année:
1990
Type:
Article
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