We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2msa

From Proteopedia

Jump to: navigation, search

Structural and immunological analysis of circumsporozoite protein peptides: a further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine.

Structural highlights

2msa is a 1 chain structure with sequence from Plasmodium falciparum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 1 model
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CSP_PLAFA The circumsporozoite protein is the immunodominant surface antigen on the sporozoite (the infective stage of the malaria parasite that is transmitted from the mosquito to the vertebrate host).

Publication Abstract from PubMed

The Plasmodium falciparum circumsporozoite protein is considered a major antimalarial-vaccine target due to its involvement in sporozoite invasion of mosquito's salivary glands and human hepatocytes. The 4383, 4388 and 4389 CSP-conserved high activity hepatocyte binding peptides and their modified analogues were synthesised and their immunogenicity was tested in Aotus monkeys. Peptide 4388 modified analogues induced higher and more permanent antibody titers against sporozoites in approximately 40% of immunised monkeys; whilst peptides 4383 and 4389 modified analogues elicited high, long-lasting antibody titers as well as short-lived antibodies. (1)H NMR studies showed that native peptides displayed random conformations, whereas most modified immunogenic HABPs contained type I, II and IV beta-turn structures. HLA-DRbeta1* molecule binding assays revealed that 4383 modified HABPs bound to HLA-DRbeta1*0701/HLA-DRbeta1*0401 molecules, whilst 4388 and 4389 modified HABPs bound to HLA-DRbeta1*0401/HLA-DRbeta1*0101, respectively. The results support these high-immunogenic CSP-derived modified peptides' inclusion in a multi-antigenic, multistage, minimal subunit-based synthetic antimalarial vaccine.

Structural and immunological analysis of circumsporozoite protein peptides: a further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine.,Bermudez A, Vanegas M, Patarroyo ME Vaccine. 2008 Dec 9;26(52):6908-18. doi: 10.1016/j.vaccine.2008.09.071. Epub 2008, Oct 16. PMID:18930095^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bermudez A, Vanegas M, Patarroyo ME. Structural and immunological analysis of circumsporozoite protein peptides: a further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine. Vaccine. 2008 Dec 9;26(52):6908-18. doi: 10.1016/j.vaccine.2008.09.071. Epub 2008, Oct 16. PMID:18930095 doi:http://dx.doi.org/10.1016/j.vaccine.2008.09.071