A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane.
The membrane-associated histidine-rich protein-1 (MAHRP-1) is a Maurer's cleft-resident molecule that has been recently described as an important protein for the trafficking of PfEMP-1 to infected erythrocyte membrane, a major virulence factor. We have studied the specific interactions between 20-mer-long synthetic peptides spanning the complete MAHRP-1 sequence and erythrocytes. A high-activity binding peptide (HABP) with saturable binding to a 46-kDa erythrocyte membrane protein was identified and its binding was affected by chymotrypsin treatment. Random coil and alpha-helical features were found in the HABP's structure. Our results suggest that MAHRP-1 specifically interacts with erythrocyte membrane through a 20-mer-long amino acid region, raising questions about this region's potential as a therapeutic target against malaria.
García
Jeison
J
Fundación Instituto de Inmunología de Colombia, Carrera 50, No. 26-00, Bogotá, Colombia.
Curtidor
Hernando
H
Gil
Olga L
OL
Vanegas
Magnolia
M
Patarroyo
Manuel E
ME
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000469:parasitology*; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010963:Plasmodium falciparum / Q000378:metabolism / Q000502:physiology*; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D002352:Carrier Proteins; C478484:MAHRP-1 protein, Plasmodium falciparum; D008565:Membrane Proteins; D010455:Peptides; D015800:Protozoan Proteins