The adhesion ofPlasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated byP. falciparumerythrocyte membrane protein 1
Author(s) -
John C. Reeder,
Alan F. Cowman,
Kathleen Davern,
James G. Beeson,
Jennifer K. Thompson,
Stephen J. Rogerson,
Graham V. Brown
Publication year - 1999
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.96.9.5198
Subject(s) - plasmodium falciparum , biology , chondroitin sulfate , ligand (biochemistry) , cd36 , parasite hosting , adhesion , membrane protein , heparan sulfate , receptor , microbiology and biotechnology , biochemistry , chemistry , immunology , malaria , membrane , glycosaminoglycan , world wide web , computer science , organic chemistry
Chondroitin sulfate A (CSA) is an important receptor for the sequestration of Plasmodium falciparum in the placenta, but the parasite ligand involved in adhesion has not previously been identified. Here we report the identification of a var gene transcribed in association with binding to CSA and present evidence that the P. falciparum erythrocyte membrane protein 1 product of the gene is the parasite ligand mediating CSA binding. Description of this gene and the implication of P. falciparum erythrocyte membrane protein 1 as the parasite ligand paves the way to a more detailed understanding of the pathogenesis of placental infection and potential therapeutic strategies targeting the interaction.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom