An iron-binding Trypanosoma cruzi urinary antigen.
An 80-kDa Trypanosoma cruzi urinary antigen (UAg) was affinity-purified from the urine of infected dogs. We demonstrated that UAg is structurally and functionally related to proteins belonging to the transferrin family, as shown by amino acid sequence and iron binding experiments. Nevertheless, monoclonal antibodies raised against UAg specifically and selectively recognized this parasite's circulating antigen. The existence of an 80-kDa T. cruzi antigen co-migrating with UAg could be confirmed when epimastigotes were metabolically labelled with [35S] methionine and then immunoprecipitated with the above mentioned antibodies. We conclude that UAg is an iron-binding T. cruzi component eliminated in the urine of the infected host.
Corral
R S
RS
Laboratorio de Virología, Hospital de Niños, Buenos Aires, Argentina.
Bertot
G M
GM
Petray
P B
PB
Altcheh
J M
JM
Singh
M
M
Orn
A
A
Rapoport
M F
MF
Grinstein
S
S
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000953:Antigens, Protozoan / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D014355:Chagas Disease / Q000276:immunology* / Q000652:urine; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D007501:Iron / Q000378:metabolism*; D008969:Molecular Sequence Data; D014349:Trypanosoma cruzi / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000953:Antigens, Protozoan; D000939:Epitopes; D007501:Iron