Jc. Doury et al., ANALYSIS OF THE HIGH-MOLECULAR-WEIGHT RHOPTRY COMPLEX OF PLASMODIUM-FALCIPARUM USING MONOCLONAL-ANTIBODIES, Parasitology, 108, 1994, pp. 269-280
Twenty-one monoclonal antibodies, obtained after immunization of mice
with erythrocytic stages of Plasmodium falciparum, produced a double d
ot image in IFA. Immunoelectronmicroscopy indicated that the mAbs reac
ted with the rhoptries. Rhoptries are pear-shaped apical organelles, b
elieved to be involved in invasion of the host cell by the parasite. T
he mAbs all immunoprecipitated the high molecular weight antigen compl
ex. Some mAbs recognized on immunoblots only 1 protein of this complex
, whereas others reacted with RhopH1 and RhopH3, or RhopH2 and RhopH3
or with the 3 proteins. An additional antigen of 52 kDa was also recog
nized by some of the mAbs. The epitopes defined by the mAbs were prese
nt in most of the 40 P. falciparum strains or isolates studied by IFA.
Interestingly, the mAbs also reacted with high titres on P. vivax and
P. ovale, but produced images that did not indicate an apical locatio
n. The mAbs failed to react on the non-human malaria parasites studied
, P. cynomolgi and P. inui. On P. berghei or P. chabaudi parasites, on
ly 5 mAbs gave a positive reaction, labelling a large network outside
the parasite. Finally, the mAbs did not react with P. falciparum sporo
zoites, indicating that the rhoptries of merozoites and sporozoites, t
he two invasive stages of the malaria life-cycle are equipped with dis
tinct sets of proteins.