Next Article in Journal
Phospho-Specific Flow Cytometry Reveals Signaling Heterogeneity in T-Cell Acute Lymphoblastic Leukemia Cell Lines
Previous Article in Journal
The Synergistic Effect of Cyclic Tensile Force and Periodontal Ligament Cell-Laden Calcium Silicate/Gelatin Methacrylate Auxetic Hydrogel Scaffolds for Bone Regeneration
 
 
Article

Host HSPD1 Translocation from Mitochondria to the Cytoplasm Induced by Streptococcus suis Serovar 2 Enolase Mediates Apoptosis and Loss of Blood–Brain Barrier Integrity

1
State Key Laboratory for Zoonotic Diseases/Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Changchun 130062, China
2
School of Basic Medicine, Jilin University, Changchun 130021, China
3
Section of Paediatric Infectious Disease, Imperial College London, London W2 1NY, UK
4
Department of Veterinary Medicine, College of Animal Science, Yangtze University, Jingzhou 434023, China
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Bingmei Fu
Cells 2022, 11(13), 2071; https://doi.org/10.3390/cells11132071
Received: 26 May 2022 / Revised: 25 June 2022 / Accepted: 27 June 2022 / Published: 29 June 2022
Streptococcus suis serovar 2 (S. suis serovar 2) is a zoonotic pathogen that causes meningitis in pigs and humans, and is a serious threat to the swine industry and public health. Understanding the mechanism(s) by which S. suis serovar 2 penetrates the blood–brain barrier (BBB) is crucial to elucidating the pathogenesis of meningitis. In a previous study, we found that expression of the virulence factor enolase (Eno) by S. suis serovar 2 promotes the expression of host heat shock protein family D member 1 (HSPD1) in brain tissue, which leads to the apoptosis of porcine brain microvascular endothelial cells (PBMECs) and increased BBB permeability, which in turn promotes bacterial translocation across the BBB. However, the mechanism by which HSPD1 mediates Eno-induced apoptosis remains unclear. In this study, we demonstrate that Eno promotes the translocation of HSPD1 from mitochondria to the cytoplasm, where HSPD1 binds to β-actin (ACTB), the translocated HSPD1, and its interaction with ACTB led to adverse changes in cell morphology and promoted the expression of apoptosis-related proteins, second mitochondria-derived activator of caspases (Smac), and cleaved caspase-3; inhibited the expression of X-linked inhibitor of apoptosis protein (XIAP); and finally promoted cell apoptosis. These results further elucidate the role of HSPD1 in the process of Eno-induced apoptosis and increased BBB permeability, increasing our understanding of the pathogenic mechanisms of meningitis, and providing a framework for novel therapeutic strategies. View Full-Text
Keywords: Streptococcus suis serovar 2; heat shock protein family D member 1; enolase; blood–brain barrier; meningitis Streptococcus suis serovar 2; heat shock protein family D member 1; enolase; blood–brain barrier; meningitis
Show Figures

Figure 1

MDPI and ACS Style

Wu, T.; Jia, L.; Lei, S.; Jiang, H.; Liu, J.; Li, N.; Langford, P.R.; Liu, H.; Lei, L. Host HSPD1 Translocation from Mitochondria to the Cytoplasm Induced by Streptococcus suis Serovar 2 Enolase Mediates Apoptosis and Loss of Blood–Brain Barrier Integrity. Cells 2022, 11, 2071. https://doi.org/10.3390/cells11132071

AMA Style

Wu T, Jia L, Lei S, Jiang H, Liu J, Li N, Langford PR, Liu H, Lei L. Host HSPD1 Translocation from Mitochondria to the Cytoplasm Induced by Streptococcus suis Serovar 2 Enolase Mediates Apoptosis and Loss of Blood–Brain Barrier Integrity. Cells. 2022; 11(13):2071. https://doi.org/10.3390/cells11132071

Chicago/Turabian Style

Wu, Tong, Li Jia, Siyu Lei, Hexiang Jiang, Jianan Liu, Na Li, Paul R. Langford, Hongtao Liu, and Liancheng Lei. 2022. "Host HSPD1 Translocation from Mitochondria to the Cytoplasm Induced by Streptococcus suis Serovar 2 Enolase Mediates Apoptosis and Loss of Blood–Brain Barrier Integrity" Cells 11, no. 13: 2071. https://doi.org/10.3390/cells11132071

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop