Chemical characterization of the parasitophorous vacuole membrane antigen QF 116 from Plasmodium falciparum.
On the basis of amino acid sequencing and immunological cross-reactivity, the Plasmodium falciparum parasitophorous vacuole antigens QF116 and exp-1/CRA are apparently identical. The epitope recognized by an inhibitory monoclonal antibody directed against QF116 is located proximal to the C-terminus of the protein. The QF116 protein is processed during maturation by the cleavage of a 22-amino-acid signal peptide and acylated as measured by labeling with myristic acid.
Kara
U
U
Queensland Institute of Medical Research, Herston, Brisbane, Australia.
Murray
B
B
Pam
C
C
Lahnstein
J
J
Gould
H
H
Kidson
C
C
Saul
A
A
D000215:Acylation; D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan / Q000302:isolation & purification; D000954:Antigens, Surface / Q000302:isolation & purification; D002846:Chromatography, Affinity; D000939:Epitopes / Q000235:genetics; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000276:immunology*; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000378:metabolism; D015800:Protozoan Proteins / Q000276:immunology* / Q000302:isolation & purification
D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan; D000954:Antigens, Surface; D000939:Epitopes; D021382:Protein Sorting Signals; D015800:Protozoan Proteins; C063362:QF116 antigen, Plasmodium falciparum