An 80-kDa Trypanosoma cruzi urinary antigen (UAg) was affinity purifie
d from the urine of infected dogs. We demonstrated that UAg is structu
rally and functionally related to proteins belonging to the transferri
n 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 ex
istence of an 80-kDa T. cruzi antigen co-migrating with UAS could be c
onfirmed when epimastigotes were metabolically labelled with [S-35] me
thionine and then immunoprecipitated with the above mentioned antibodi
es. We conclude that UAg is an iron-binding T. cruzi component elimina
ted in the urine of the infected host.