3N26

Cpn0482 : the arginine binding protein from the periplasm of chlamydia Pneumoniae

「3G41」から置き換えられました

3N26 の概要

• エントリーDOI: 10.2210/pdb3n26/pdb
• 関連するPDBエントリー: 1HSL 3DEL
• 分子名称: Amino acid ABC transporter, periplasmic amino acid-binding protein, ARGININE (3 entities in total)
• 機能のキーワード: vaccine development, alpha and beta protein (a/b), structural genomics, bacabs - eu fp6 programme, marseilles structural genomics program @ afmb, msgp, transport protein
• 由来する生物種: Chlamydophila pneumoniae (Chlamydophila pneumoniae)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27850.00

構造登録者

Petit, P.,Garcia, C.,Vuillard, L.,Soriani, M.,Grandi, G.,Marseilles Structural Genomics Program AFMB (MSGP),Marseilles Structural Genomics Program @ AFMB (MSGP) (登録日: 2010-05-17, 公開日: 2010-06-16, 最終更新日: 2023-11-01)

主引用文献

Soriani, M.,Petit, P.,Grifantini, R.,Petracca, R.,Gancitano, G.,Frigimelica, E.,Nardelli, F.,Garcia, C.,Spinelli, S.,Scarabelli, G.,Fiorucci, S.,Affentranger, R.,Ferrer-Navarro, M.,Zacharias, M.,Colombo, G.,Vuillard, L.,Daura, X.,Grandi, G.
Exploiting antigenic diversity for vaccine design: the Chlamydia ArtJ paradigm.
J.Biol.Chem., 2010

PubMed Abstract: We present an interdisciplinary approach that, by incorporating a range of experimental and computational techniques, allows the identification and characterization of functional/immunogenic domains. This approach has been applied to ArtJ, an arginine-binding protein whose orthologs in Chlamydiae trachomatis (CT ArtJ) and pneumoniae (CPn ArtJ) are shown to have different immunogenic properties despite a high sequence similarity (60% identity). We have solved the crystallographic structures of CT ArtJ and CPn ArtJ, which are found to display a type II transporter fold organized in two α-β domains with the arginine-binding region at their interface. Although ArtJ is considered to belong to the periplasm, we found that both domains contain regions exposed on the bacterial surface. Moreover, we show that recombinant ArtJ binds to epithelial cells in vitro, suggesting a role for ArtJ in host-cell adhesion during Chlamydia infection. Experimental epitope mapping and computational analysis of physicochemical determinants of antibody recognition revealed that immunogenic epitopes reside mainly in the terminal (D1) domain of both CPn and CT ArtJ, whereas the surface properties of the respective binding-prone regions appear sufficiently different to assume divergent immunogenic behavior. Neutralization assays revealed that sera raised against CPn ArtJ D1 partially reduce both CPn and CT infectivity in vitro, suggesting that functional antibodies directed against this domain may potentially impair chlamydial infectivity. These findings suggest that the approach presented here, combining functional and structure-based analyses of evolutionary-related antigens can be a valuable tool for the identification of cross-species immunogenic epitopes for vaccine development.

PubMed: 20592031
DOI: 10.1074/jbc.M110.118513

実験手法

X-RAY DIFFRACTION (2.1 Å)