Imperial College London
Alternate

ProfessorPaulLangford

Faculty of Medicine, Department of Infectious Disease

Professor of Paediatric Infectious Diseases
 
 
 
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Contact

 

+44 (0)20 7594 3359p.langford Website

 
 
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Location

 

236Wright Fleming WingSt Mary's Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wu:2022:10.3390/cells11132071,
author = {Wu, T and Jia, L and Lei, S and Jiang, H and Liu, J and Li, N and Langford, PR and Liu, H and Lei, L},
doi = {10.3390/cells11132071},
journal = {Cells},
pages = {1--16},
title = {Host HSPD1 translocation from mitochondria to the cytoplasm induced by streptococcus suis Serovar 2 enolase mediates apoptosis and loss of blood–brain barrier integrity},
url = {http://dx.doi.org/10.3390/cells11132071},
volume = {11},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Wu,T
AU  - Jia,L
AU  - Lei,S
AU  - Jiang,H
AU  - Liu,J
AU  - Li,N
AU  - Langford,PR
AU  - Liu,H
AU  - Lei,L
DO  - 10.3390/cells11132071
EP  - 16
PY  - 2022///
SN  - 2073-4409
SP  - 1
TI  - Host HSPD1 translocation from mitochondria to the cytoplasm induced by streptococcus suis Serovar 2 enolase mediates apoptosis and loss of blood–brain barrier integrity
T2  - Cells
UR  - http://dx.doi.org/10.3390/cells11132071
UR  - https://www.mdpi.com/2073-4409/11/13/2071
UR  - http://hdl.handle.net/10044/1/98013
VL  - 11
ER  -
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