STUDIESON BINDING DOMAINSOF MAJOR MEROZOITE SURFACE PROTEIN OF PLASMODIUM FALCIPARUM TO HUMAN ERYTHROCYTE / 中国寄生虫学与寄生虫病杂志

ABSTRACT

AIM:To understand the interaction between a195- kilodalton protein,P195, on the surface of Plasmodium falciparum merozoite and human erythrocyte.METHODS:P195 was expressed in eight fragments in E.coli.After being refolded,the expressed proteins were la- belled with12 5 I,and incubated with human erythrocytes.RESULTS:According to binding assay, three fragments of P195M3,M6,M9were found to have ability to bind to human erythrocyte. M6,which is equal to amino acid( AA) sequence from384 to595,could bind to human erythro- cytes but not to trypsin treated human erythrocytes,and the binding could be eluted by low p H buffer solution. M3( AA 12 3to 30 2 ) and M9( AA 10 78to 12 51) also have the ability to bind to human erythrocytes,but the binding was not affected by trypsin treatment and low p H buffer elu- tion. CONCL USIONThe binding site of M6might be a surface protein receptor of human ery- throcytes,while the binding site of M3and M9might be an intracellular componentof human ery- throcyte.