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Immunological properties of recombinant proteins of the transmission blocking vaccine candidate, Pfs48/45, of the human malaria parasite Plasmodium falciparum produced in Escherichia coli
Author(s) -
MILEK RICHARD L.B.,
ROEFFEN WILL F.G.,
KOCKEN CLEMENS H.M.,
JANSEN JOSEPHINE,
KAAN ANITA M.,
ELING WIJNAND M.C.,
SAUERWEIN ROBERT W.,
KONINGS RUUD N.H.
Publication year - 1998
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1046/j.1365-3024.1998.00171.x
Subject(s) - biology , plasmodium falciparum , gametocyte , recombinant dna , virology , heterologous , escherichia coli , antigen , malaria vaccine , immunogenicity , monoclonal antibody , antibody , microbiology and biotechnology , immunology , malaria , gene , genetics
A precondition for the development of a transmission blocking vaccine based on the sexual stage‐specific surface antigen Pfs48/45 of Plasmodium falciparum is its heterologous synthesis in a native state. Here we describe the production of recombinant Pfs48/45 in Escherichia coli . Two recombinant proteins, of which one is a glutathione‐S‐transferase fusion protein, were produced. Enzyme‐linked immunosorbent assays showed that at least a subfraction of the recombinant proteins had a conformation capable of binding transmission blocking monoclonal antibodies. However, despite the fact that both proteins were very immunogenic, they did not induce transmission blocking immunity in mice or rabbits. Immunological studies with congenic mouse strains demonstrated that immune responses could be boosted with gametocyte extracts and were not restricted to a particular class II major histocompatibility complex haplotype .