| Literature DB >> 18451305 |
Benoit Vanhollebeke1, Géraldine De Muylder, Marianne J Nielsen, Annette Pays, Patricia Tebabi, Marc Dieu, Martine Raes, Soren K Moestrup, Etienne Pays.
Abstract
The protozoan parasite Trypanosoma brucei is lysed by apolipoprotein L-I, a component of human high-density lipoprotein (HDL) particles that are also characterized by the presence of haptoglobin-related protein. We report that this process is mediated by a parasite glycoprotein receptor, which binds the haptoglobin-hemoglobin complex with high affinity for the uptake and incorporation of heme into intracellular hemoproteins. In mice, this receptor was required for optimal parasite growth and the resistance of parasites to the oxidative burst by host macrophages. In humans, the trypanosome receptor also recognized the complex between hemoglobin and haptoglobin-related protein, which explains its ability to capture trypanolytic HDLs. Thus, in humans the presence of haptoglobin-related protein has diverted the function of the trypanosome haptoglobin-hemoglobin receptor to elicit innate host immunity against the parasite.Entities:
Mesh：
Substances：
Year: 2008 PMID： 18451305 DOI： 10.1126/science.1156296
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728