The transferrin (Tf) receptor of Trypanosoma brucei (TbTfR) is encoded by two expression-site-associated genes, ESAG6 and ESAG7. There are around 20 different expression sites containing different copies of these genes that encode TbTfRs with quite distinct affinities for Tf of various hosts. It was proposed that T. brucei has developed multiple expression sites encoding different TbTfRs to ensure sufficient iron uptake in the presence of antibodies competing for binding to Tf. Here it is shown that anti-TbTfR antibody titres produced during chronic murine trypanosomiasis are only one-tenth of those achieved by immunisation of mice using recombinant TbTfR. Calculations indicate that the concentrations of competing anti-TbTfR antibodies present during chronic T. brucei infection are too low to deprive the parasite of iron. In addition, during human African trypanosomiasis the antibody response to the TbTfR seems to be poor and transient. Altogether, the results suggest that the host antibody response to the TbTfR during chronic infection with T. brucei is too low, if present at all, to prevent sufficient iron uptake by bloodstream forms to promote their growth.