Structure of the trypanosome transferrin receptor reveals mechanisms of ligand recognition and immune evasion.

ABSTRACT: To maintain prolonged infection of mammals, African trypanosomes have evolved remarkable surface coats and a system of antigenic variation¹. Within these coats are receptors for macromolecular nutrients such as transferrin^2,3. These must be accessible to their ligands but must not confer susceptibility to immunoglobulin-mediated attack. Trypanosomes have a wide host range and their receptors must also bind ligands from diverse species. To understand how these requirements are achieved, in the context of transferrin uptake, we determined the structure of a Trypanosoma brucei transferrin receptor in complex with human transferrin, showing how this heterodimeric receptor presents a large asymmetric ligand-binding platform. The trypanosome genome contains a family of arou

SUBMITTER: Trevor CE 

PROVIDER: S-EPMC6881179 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature