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
in English
| 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Plasmodium falciparum
/
Recombinant Proteins
/
Molecular Sequence Data
/
Base Sequence
/
Amino Acid Sequence
/
Clone Cells
/
Animals
/
Malaria
/
Antibodies, Monoclonal
/
Epitopes
Type of study:
Prognostic study
Language:
English
Journal:
Southeast Asian J Trop Med Public Health
Year:
1990
Type:
Article
Similar
MEDLINE
...
LILACS
LIS