Malaria circumsporozoite protein

Usynin, I., Klotz, C., and Frevert, U. (2007). Malaria circumsporozoite protein inhibits the respiratory burst in Kupffer cells. Cell Microbiol. 9, 2610-2628. 

Frevert U, Sinnis P, Cerami C, Shreffler W, Takacs B, Nussenzweig V. Malaria circumsporozoite protein binds to heparan sulfate proteoglycans associated with the surface membrane of hepatocytes. J Exp Med 1993 177 1287-1298. 

Rathore D, McCutchan TF, Garboczi DN, Toida T, Hernaiz MJ, LeBrun LA, Lang SC, Linhardt RJ. Direct measurement of the interactions of glycosami-noglycans and a heparin decasaccharide with the malaria circumsporozoite protein. Biochemistry 2001 40 11518-11524. 

Sinnis, P, Clavijo, P, Fenyo, D, Chait, BT, Cerami, C, and Nussenzweig, V (1994) Structural and functional properties of region II-plus of the malaria circumsporozoite protein. J Exp Med 180 297-306. 

Gantt SM, Clavijo P, Bai X, Esko JD, Sinnis P (1997) Cell adhesion to a motif shared by the malaria circumsporozoite protein and thrombospondin is mediated by its glycosaminoglycan-binding region and not by CSVTCG. J Biol Chem 272 19205-13. 

Shakibaei M, Frevert U 1996. Dual interaction of the malaria circumsporozoite protein with the low density lipoprotein receptor-related protein (LRP) and heparan sulfate proteoglycans. J Exp Med 184 1699-1711. 

The immunodominant portion of the malaria circumsporozoite surface protein contains a tetrapeptide motif (-Asn-Pro-Asn-Ala-), tandemly repeated almost 40 times. Bisang et aft165 incorporated the (I-turn mimetic 131 into the cyclic template 132 (Scheme 48). BALB/c mice... 

Malarial infection does not produce immunity in patients, and active research has been initiated to develop a malaria vaccine. " A vaccine that blocks the entry of sporozoites into the liver cells will prevent malaria at this stage. However, immunity to sporozoites does not protect the host against parasites in the erythrocytic cycle. Infective sporozoites of P. falciparum are covered by a polypeptide, circumsporozoite protein. Isolatiou aud ideutification of the gene encoding for this circumsporozoite protein have led to the development of a monoclonal antibody by recombinant DNA technology P. falciparum sporozoite vaccine is now under investigation. ... 

Plasmodium falciparum circumsporozoite protein (CSP) is an important potential component of a vaccine against malaria. It is obvious that P. falciparum should be expressed in D. discoideum, as the two organisms have quite similar A-i-T contents of their genomes (total genome 78% in D. discoideum and 81% in P. falciparum, re-... 

Stoute JA, Slaoui M, Heppner DG, Momin P, Kester KE, Desmons P, Wellde BT, Gargon N, Kazych U, Marchand M et al (1997) A preliminary evaluation of a recombinant circumsporozoite protein vaccine against Plasmodium falciparum malaria. N Engl J Med 336 86-91... 

Pancake SJ, Holt GD, Mellouk S, Hoffman SL (1992) Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates. J Cell Biol 117 1351 7. 

Malaria is a serious, sometimes fatal disease caused by a parasite, Plasmodium sporozoite, and is transmitted by the bite of an infected mosquito. More than 40% of the people in the world live in areas at risk for malaria. Plasmodium sporozoites traverse the cytosol of several cells before invading a hepatocyte (38). The invasion of liver cells by these sporozoites has been ascribed to the interaction of circumsporozoite (CS) protein, a 40-45 kDa antigen (39) that covers the plasma membrane of sporozoites, with GAG side chains of PGs located on the surface of the hepatocytes... 

Lowik et demonstrated that the secondary structure of certain peptide sequences conjugated to single Ci8 alkyl chains at both the N- and C-termini could be induced upon incorporation into a liposome membrane. A sequence derived from the circumsporozoite (CS) protein of the malaria parasite Plasmodium falciparum was chosen, as within the natural protein the Asn-Pro-Asn-Ala repeat is known to adopt a j6-tum. Both the unmodified peptide in solution and the analogous peptide with only one alkyl chain showed random coil folding characteristics. However, when the double alkylated peptide was inserted into l,2-dimyristoyl-OT-glycero-3-phosphoethanol-amine (DSPC) liposomes the peptide folded into a P-hairpin. This simple approach is a convenient way for stabilizing a variety of peptides into their preferred secondary structure and might be employed in the presentation of multiple (hairpin) epitopes. 

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