Tumour necrosis factor and interleukin-6 production induced by components associated with merozoite proteins of Plasmodium falciparum

TY - JOUR

T1 - Tumour necrosis factor and interleukin-6 production induced by components associated with merozoite proteins of Plasmodium falciparum

AU - Jakobsen, P H

AU - Moon, R

AU - Ridley, R G

AU - Bate, C A

AU - Taverne, J

AU - Hansen, M B

AU - Takacs, B

AU - Playfair, J H

AU - McBride, J S

N1 - Keywords: Animals; Antibodies, Monoclonal; Antibodies, Protozoan; Antigens, Protozoan; Antigens, Surface; Blotting, Western; Cross Reactions; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique; Humans; Immune Sera; Immunoelectrophoresis, Two-Dimensional; Interleukin-6; Malaria, Falciparum; Merozoite Surface Protein 1; Plasmodium falciparum; Plasmodium yoelii; Protein Precursors; Protozoan Proteins; Tumor Necrosis Factor-alpha

PY - 1993

Y1 - 1993

N2 - P. falciparum merozoite antigens, merozoite surface protein-1 (MSP-1) and rhoptry associated protein-1 (RAP-1), were shown to be liberated into the supernatant of in vitro parasite cultures and to be included in the endotoxin-like exoantigen complex, previously designated Ag7. Material affinity purified from culture supernatants, using immobilized monoclonal antibodies specific for RAP-1 or MSP-1, stimulated normal human mononuclear cells to produce TNF and IL-6 in vitro. However, stimulation of TNF was absent, and that of IL-6 was reduced, when the antigens were purified from detergent extracts of infected erythrocytes. These results indicate that the RAP-1 and MSP-1 proteins themselves do not stimulate the production of TNF. Instead, other components associating with these exoantigens may be responsible for the TNF production. Mouse antisera blocking TNF production stimulated by P. yoelii exoantigens also blocked TNF production stimulated by material affinity purified from P. falciparum culture supernatants using RAP-1 specific monoclonal antibody, indicating the conserved structure of the TNF inducing component.

AB - P. falciparum merozoite antigens, merozoite surface protein-1 (MSP-1) and rhoptry associated protein-1 (RAP-1), were shown to be liberated into the supernatant of in vitro parasite cultures and to be included in the endotoxin-like exoantigen complex, previously designated Ag7. Material affinity purified from culture supernatants, using immobilized monoclonal antibodies specific for RAP-1 or MSP-1, stimulated normal human mononuclear cells to produce TNF and IL-6 in vitro. However, stimulation of TNF was absent, and that of IL-6 was reduced, when the antigens were purified from detergent extracts of infected erythrocytes. These results indicate that the RAP-1 and MSP-1 proteins themselves do not stimulate the production of TNF. Instead, other components associating with these exoantigens may be responsible for the TNF production. Mouse antisera blocking TNF production stimulated by P. yoelii exoantigens also blocked TNF production stimulated by material affinity purified from P. falciparum culture supernatants using RAP-1 specific monoclonal antibody, indicating the conserved structure of the TNF inducing component.

M3 - Journal article

C2 - 8506119

SN - 0141-9838

VL - 15

SP - 229

EP - 237

JO - Parasite Immunology

JF - Parasite Immunology

IS - 4

ER -