Chemical characterization of the parasitophorous vacuole membrane antigen QF 116 from Plasmodium falciparum

U Kara; B Murray; C Pam; J Lahnstein; H Gould; C Kidson; A Saul

doi:10.1016/0166-6851(90)90200-6

Chemical characterization of the parasitophorous vacuole membrane antigen QF 116 from Plasmodium falciparum

Mol Biochem Parasitol. 1990 Jan 1;38(1):19-23. doi: 10.1016/0166-6851(90)90200-6.

Authors

U Kara¹, B Murray, C Pam, J Lahnstein, H Gould, C Kidson, A Saul

Affiliation

¹ Queensland Institute of Medical Research, Herston, Brisbane, Australia.

PMID: 1690855
DOI: 10.1016/0166-6851(90)90200-6

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acylation
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antigens, Protozoan* / isolation & purification
Antigens, Surface* / isolation & purification
Chromatography, Affinity
Epitopes / genetics
Molecular Sequence Data
Plasmodium falciparum / immunology*
Protein Processing, Post-Translational
Protein Sorting Signals / metabolism
Protozoan Proteins / immunology*
Protozoan Proteins / isolation & purification

Substances

Antibodies, Monoclonal
Antigens, Protozoan
Antigens, Surface
Epitopes
Protein Sorting Signals
Protozoan Proteins
QF116 antigen, Plasmodium falciparum