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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.
Protective Synthetic Peptide Against Malaria And Encoding Gene; NIH reference E-519-1985 A synthetic peptide that is capable of inducing antibodies protective against malarial infection caused by Plasmodium vivax offers an important new tool for the delopment of a malarial vaccine. In order to provide this peptide in a vaccine composition, the nature of the immunodominant epitope of the surface protein of P. vivax sporozoite was identified and the gene encoding the epitope was cloned. The peptide can be administered with an adjuvant in an acceptable carrier such as a nontoxic bacterial cell or liposome.
Aegyptin and uses thereof Exposed collagen in injured blood vessels provides a substrate for platelets to adhere and aggregate initiating the first step in thrombosis, the formation of blood clots inside a blood vessel. Despite the essential role of platelets in vascular injury, excessive platelet aggregation may also result in thrombotic diseases such as stroke and heart attack. Available for licensing is a collagen binding protein, named aegyptin, which selectively inhibits collagen-platelet aggregation, but not platelet aggregation induced by other agonists. Collagen initiates recruitment of circulating platelets and triggers platelet activation. Collagen also plays a critical role in angiogenesis. Aegyptin blocks the interaction of collagen with its major ligands, von Willebrand factor, glycoprotein VI GPVI , and integrin alpha2beta1. These three ligands are of particular importance because von Willebrand factor plays a critical role in tethering platelets to collagen, GPVI is the major signaling platelet receptor, and integrin alpha2beta1 mediates platelet adhesion and contributes to activation. Since these ligands play a critical role in the early stages of thrombus formation, aegyptin represents a potentially highly effective therapeutic that can prevent and treat patients with thrombotic disease. Alternatively, aegyptin is potentially useful in conditions where collagen plays a critical role in angiogenesis or in conditions where excessive deposition of collagen plays a pathological role e.g., pancreatic carcinoma .