Abstract:
:MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein's repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33kDa protein on red blood cell membrane. HABPs' possible function in merozoite invasion of erythrocytes is also discussed.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ocampo M,Curtidor H,Vera R,Valbuena JJ,Rodríguez LE,Puentes A,López R,García JE,Tovar D,Pacheco P,Navarro MA,Patarroyo MEdoi
10.1016/j.bbrc.2004.01.050subject
Has Abstractpub_date
2004-03-05 00:00:00pages
319-29issue
2eissn
0006-291Xissn
1090-2104pii
S0006291X04000920journal_volume
315pub_type
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journal_title:Biochemical and biophysical research communications
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