2MUF

Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins

2MUF の概要

• エントリーDOI: 10.2210/pdb2muf/pdb
• NMR情報: BMRB: 25209
• 分子名称: TRSP (1 entity in total)
• 機能のキーワード: trsp, vaccine, immune system
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2432.67

構造登録者

Curtidor, H.,Arevalo-Pinzon, G.,Bermudez, A.,Calderon, D.,Vanegas, M.,Patino, L.,Patarroyo, M. (登録日: 2014-09-09, 公開日: 2015-09-23, 最終更新日: 2024-05-15)

主引用文献

Curtidor, H.,Arevalo-Pinzon, G.,Bermudez, A.,Calderon, D.,Vanegas, M.,Patino, L.C.,Patarroyo, M.A.,Patarroyo, M.E.
Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins.
Amino Acids, 43:365-378, 2012

PubMed Abstract: Several sporozoite proteins have been associated with Plasmodium falciparum cell traversal and hepatocyte invasion, including the cell-traversal protein for ookinetes and sporozoites (CelTOS), and thrombospondin-related sporozoite protein (TRSP). CelTOS and TRSP amino acid sequences have been finely mapped to identify regions specifically binding to HeLa and HepG2 cells, respectively. Three high-activity binding peptides (HABPs) were found in CelTOS and one HABP was found in TRSP, all of them having high α-helical structure content. These HABPs' specific binding was sensitive to HeLa and HepG2 cells' pre-treatment with heparinase I and chondroitinase ABC. Despite their similarity at three-dimensional (3D) structural level, TRSP and TRAP HABPs located in the TSR domain did not compete for the same binding sites. CelTOS and TRSP HABPs were used as a template for designing modified sequences to then be assessed in the Aotus monkey experimental model. Antibodies directed against these modified HABPs were able to recognize both the native parasite protein by immunofluorescence assay and the recombinant protein (expressed in Escherichia coli) by Western blot and ELISA assays. The results suggested that these modified HABPs could be promising targets in designing a fully effective, antimalarial vaccine.

PubMed: 21952731
DOI: 10.1007/s00726-011-1087-8

実験手法

SOLUTION NMR