Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors

被引：34

作者：

Aparicio, David ^{[1
,2
]}

Torres-Puig, Sergi ^{[3
,4
]}

Ratera, Merce ^{[1
,2
]}

Querol, Enrique ^{[3
,4
]}

Pinol, Jaume ^{[3
,4
]}

Pich, Oscar Q. ^{[3
,4
]}

Fita, Ignacio ^{[1
,2
]}

机构：

[1] CSIC, IBMB, Baldiri Reixac 10, E-08028 Barcelona, Spain

[2] Parc Cient Barcelona, Maria Maeztu Unit Excellence, Baldiri Reixac 10, Barcelona 08028, Spain

[3] Univ Autonoma Barcelona, Inst Biotecnol & Biomed, E-08193 Barcelona, Spain

[4] Univ Autonoma Barcelona, Dept Bioquim & Biol Mol, E-08193 Barcelona, Spain

来源：

NATURE COMMUNICATIONS | 2018年 / 9卷

关键词：

BETA-PROPELLER; ANTIGENIC VARIATION; GENETIC-VARIATION; HOST-CELLS; PNEUMONIAE; PROTEIN; INFECTION; RESISTANCE; FAILURE; CRYSTALLOGRAPHY;

D O I：

10.1038/s41467-018-06963-y

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. Herein, we present the crystal structures of the extracellular region of the virulence factor P110 (916 residues) unliganded and in complex with sialic acid oligosaccharides. P110 interacts only with the neuraminic acid moiety of the oligosaccharides and experiments with human cells demonstrate that these interactions are essential for mycoplasma cytadherence. Additionally, structural information provides a deep insight of the P110 antigenic regions undergoing programmed variation to evade the host immune response. These results enlighten the interplay of M. genitalium with human target cells, offering new strategies to control mycoplasma infections.

引用

页数：11

共 68 条

[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].