Erythrocyte G protein-coupled receptor signaling in malarial infection.

Harrison T, Samuel BU, Akompong T, Hamm H, Mohandas N, Lomasney JW, Haldar K
Science. 2003 301 (5640): 1734-6

PMID: 14500986 · DOI:10.1126/science.1089324

Erythrocytic mechanisms involved in malarial infection are poorly understood. We have found that signaling via the erythrocyte beta2-adrenergic receptor and heterotrimeric guanine nucleotide-binding protein (Galphas) regulated the entry of the human malaria parasite Plasmodium falciparum. Agonists that stimulate cyclic adenosine 3',5'-monophosphate production led to an increase in malarial infection that could be blocked by specific receptor antagonists. Moreover, peptides designed to inhibit Galphas protein function reduced parasitemia in P. falciparum cultures in vitro, and beta-antagonists reduced parasitemia of P. berghei infections in an in vivo mouse model. Thus, signaling via the erythrocyte beta2-adrenergic receptor and Galphas may regulate malarial infection across parasite species.

MeSH Terms (27)

Adrenergic beta-2 Receptor Agonists Adrenergic beta-2 Receptor Antagonists Adrenergic beta-Agonists Adrenergic beta-Antagonists Alprenolol Animals Catecholamines Cyclic AMP Erythrocyte Membrane Erythrocytes GTP-Binding Protein alpha Subunits, Gs Humans Malaria Membrane Microdomains Mice Parasitemia Peptide Fragments Plasmodium berghei Plasmodium falciparum Propranolol Purinergic P1 Receptor Agonists Purinergic P1 Receptor Antagonists Receptors, Adrenergic, beta-2 Receptors, Purinergic P1 Signal Transduction Stereoisomerism Vacuoles

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