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A fragment of the PfHRP-II gene of Plasmodium falciparum was cloned using recombinant DNA techniques. This clone is capable of encoding PfHRP-II protein, a water-soluble, histidine-rich molecule that may be effective in the detection, diagnosis, and treatment of human malaria, which is caused by the parasite, P. falciparum. This protein may be particularly useful in the development of an anti-malaria vaccine. To date, no malaria vaccine has been successful in human trials and most exhibit only limited effectiveness in primates. Recombinant DNA clone containing a genomic fragment of PfHRP-II gene from plasmodium falciparum The invention relates to isolated clones of DNA from Plasmodium falciparum that encode a histidine-rich protein from that organism. The PfHRPII protein is expressed in P. falciparum-infected erythrocytes. The cloned gene segment includes an intron-exon boundary near the amino-terminus of the coding sequence. The PfHRPII protein has a Mr of 60-80 kDa as determined by SDS-PAGE. This is substantially higher than the molecular weight of about 35 kDa as estimated from the predicted amino acid sequence of PfHRPII. The PfHRPII amino acid sequence includes a hydrophobic leader sequence, consistent with secretion of PfHRPII observed in vivo and in vivo. The amino acid sequence of PfHRPII is also characterized by a number of tandem repeats having a high content of histidine, alanine and aspartic acid.
Monoclonal antibodies (MABs) that block the transmission of malaria (Plasmodium falciparum or Plasmodium gallinaceum) to mosquitoes offer an improved method for controlling the spread of this disease. There has previously been no effective method of preventing mosquitoes for acquiring malarial parasites. These MABs, which block fertilization of the gametes preventing formation of the zygote and development of the zygote in the mosquito midgut, exhibit affinity and specificity for proteins located on the surface of the gametes or ookinetes of the malaria parasite.
This invention relates to novel methods and compositions for blocking transmission of Plasmodium vivax which cause malaria. In particular, Pvs25 and Pvs28 polypeptides, variants and fusion proteins thereof, are disclosed which, when administered to a susceptible organism, induce an immune response against a 25 kD and 28 kD protein, respectively, on the surface of Plasmodium vivax zygotes and ookinetes. This immune response in the susceptible organism can block transmission of malaria. {RefNo is 1182 }
Invention provides a malaria antigen-carrier conjugate, which comprises a carrier protein and a plurality of Plasmodium antigen polypeptides. Each of the antigen polypeptides is a wild type antigen protein expressed in athe maosquito stage of Plasmodium or a derivative of the wild-type antigen protein, and each of the antigen polypeptides may be the same or different. The plurality of the Plasmodium antigen polypeptides are covalently linked to the carrier protein. The present invention further provides a vaccine against malaria, which comprises the conjugate absorbed on an aluminum adjuvant.
Mycobacterium tuberculosis is a bacteria that causes one of the most deadly and debilitating diseases of humans today. The CBER investigators developed Hybridoma 7C4.1F7 which produces a IgG2 a monoclonal antibody that recognizes the polyglycine repeat sequence, PGRS, a domain of PE_PGRS proteins from Mycobacterium. The monoclonal antibody elicited by the 7C4.1F7 hybridoma specifically identifies the PE_PGRS proteins from this bacteria that are markers for infection with TB and related pathogneic mycobacteria. Furthermore, this MAb has potential as a powerful research tool in investigating the role of PE_PGRS proteins in the immunopathogenesis of M. tuberculosis. PE_PGRS proteins belong to the PE and PE_PGRS multigene family of Mycobacterium which contains over 65 open reading frames (ORF's) with an N-terminal Proline-Glutamine amino acid motif (PE) and a C-terminal Glycine-Alanine Rich domain. PE_PGRS proteins are found on the surface of Mycobacteria, are expressed during infection, are involved as virulence factors, and are also involved in antigen diversity.
An immunologically active substantially pure peptide capable of inducing in human an immune response which is cross reactive with and protective against infection by a malaria parasite, wherein the peptide contains at least 2 consecutive repeats of a sequence Asn-X-Y-Pro wherein X is Ala or Val and Y is Asn or Asp or a sequence of the formula Thr-Glu-Trp-Z-Pro-Cys-Ser-Val-Thr-Cys-Gly-Asn-Gly wherein Z is Ser or Thr or the formula Lys-Pro-S-T-S-Lys-Leu-Lys-Gln-Pro-U-V-Gly-W-Pro wherein S is Lys or Asn, T is His or Glu, U is Gly or Asn, V is As or Glu, and W is Asn or Gln is disclosed along with DNA sequences and various other genetic materials useful in producing these peptides through biological methods.