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PgtE Enzyme of Salmonella enterica Shares the Similar Biological Roles to Plasminogen Activator (Pla) in Interacting With DEC-205 (CD205), and Enhancing Host Dissemination and Infectivity by Yersinia pestis

Authors :
Qiao Li
Chenglin Ye
Fei Zhao
Wenjin Li
Sizhe Zhu
Yin Lv
Chae Gyu Park
Yingmiao Zhang
Ling-Yu Jiang
Kun Yang
Yingxia He
Huahua Cai
Song Zhang
Hong-Hui Ding
Olivia Adhiambo Njiri
John Mambwe Tembo
Ayman Ahmad Alkraiem
An-Yi Li
Zi-Yong Sun
Wei Li
Mei-Ying Yan
Biao Kan
Xixiang Huo
John D. Klena
Mikael Skurnik
Andrey P. Anisimov
Xiaofang Gao
Yanping Han
Rui-Fu Yang
Xiding Xiamu
Yuanzhi Wang
Hongxiang Chen
Bao Chai
Yicheng Sun
Jingping Yuan
Tie Chen
Source :
Frontiers in Immunology, Vol 13 (2022)
Publication Year :
2022
Publisher :
Frontiers Media S.A., 2022.

Abstract

Yersinia pestis, the cause of plague, is a newly evolved Gram-negative bacterium. Through the acquisition of the plasminogen activator (Pla), Y. pestis gained the means to rapidly disseminate throughout its mammalian hosts. It was suggested that Y. pestis utilizes Pla to interact with the DEC-205 (CD205) receptor on antigen-presenting cells (APCs) to initiate host dissemination and infection. However, the evolutionary origin of Pla has not been fully elucidated. The PgtE enzyme of Salmonella enterica, involved in host dissemination, shows sequence similarity with the Y. pestis Pla. In this study, we demonstrated that both Escherichia coli K-12 and Y. pestis bacteria expressing the PgtE-protein were able to interact with primary alveolar macrophages and DEC-205-transfected CHO cells. The interaction between PgtE-expressing bacteria and DEC-205-expressing transfectants could be inhibited by the application of an anti-DEC-205 antibody. Moreover, PgtE-expressing Y. pestis partially re-gained the ability to promote host dissemination and infection. In conclusion, the DEC-205-PgtE interaction plays a role in promoting the dissemination and infection of Y. pestis, suggesting that Pla and the PgtE of S. enterica might share a common evolutionary origin.

Details

Language :
English
ISSN :
16643224
Volume :
13
Database :
Directory of Open Access Journals
Journal :
Frontiers in Immunology
Publication Type :
Academic Journal
Accession number :
edsdoj.93caedba81d54c49ae926aca25323044
Document Type :
article
Full Text :
https://doi.org/10.3389/fimmu.2022.791799