A Maurer’s cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane

• Published in: Biochemical and biophysical research communications 2009-02, Vol.380 (1), p.122-126
• Main Authors: García, Jeison, Curtidor, Hernando, Gil, Olga L., Vanegas, Magnolia, Patarroyo, Manuel E.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antimalarial candidate; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Erythrocyte Membrane - metabolism; Erythrocyte Membrane - parasitology; High-activity binding peptide; MAHRP-1; Malaria; Maurer’s clefts; Molecular Sequence Data; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Plasmodium falciparum; Plasmodium falciparum - metabolism; Plasmodium falciparum - physiology; Protozoan Proteins - chemistry; Protozoan Proteins - genetics; Protozoan Proteins - metabolism
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2009.01.050

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 α-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.