Immunological properties of recombinant proteins of the transmission blocking vaccine candidate, Pfs48/45, of the human malaria parasite Plasmodium falciparum produced in Escherichia coli.

Autor: Milek RL; Department of Molecular Biology and Cell Biology, University of Nijmegen, Toernooiveld 2, 6525 ED Nijmegen, The Netherlands., Roeffen WF, Kocken CH, Jansen J, Kaan AM, Eling WM, Sauerwein RW, Konings RN
Jazyk: angličtina
Zdroj: Parasite immunology [Parasite Immunol] 1998 Aug; Vol. 20 (8), pp. 377-85.
DOI: 10.1046/j.1365-3024.1998.00171.x
Abstrakt: 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.
Databáze: MEDLINE