Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue

2017 ◽  
Vol 51 (1) ◽  
pp. 112-121 ◽  
Author(s):  
A. R. Kayumov ◽  
M. I. Bogachev ◽  
V. A. Manuvera ◽  
V. N. Lazarev ◽  
A. V. Sabantsev ◽  
...  
2013 ◽  
Vol 62 (7) ◽  
pp. 959-967 ◽  
Author(s):  
Jayapal Jeya Maheshwari ◽  
Kuppamuthu Dharmalingam

The aim of this study is to examine the in vivo role of a small heat-shock protein (sHsp18) from Mycobacterium leprae in the survival of heterologous recombinant hosts carrying the gene encoding this protein under different environmental conditions that are normally encountered by M. leprae during its infection of the human host. Using an Escherichia coli system where shsp18 expression is controlled by its native promoter, we show that expression of shsp18 is induced under low oxygen tension, nutrient depletion and oxidative stress, all of which reflect the natural internal environment of the granulomas where the pathogen resides for long periods. We demonstrate the in vivo chaperone activity of sHsp18 through its ability to confer survival advantage to recombinant E. coli at heat-shock temperatures. Additional evidence for the protective role of sHsp18 was obtained when Mycobacterium smegmatis harbouring a copy of shsp18 was found to multiply better in human macrophages. Furthermore, the autokinase activity of sHsp18 protein demonstrated for what is believed to be the first time in this study implies that some of the functions of sHsp18 might be controlled by the phosphorylation state of this protein. Results from this study suggest that shsp18 might be one of the factors that facilitate the survival and persistence of M. leprae under stress and autophosphorylation of sHsp18 protein could be a mechanism used by this protein to sense changes in the external environment.


2001 ◽  
Vol 183 (17) ◽  
pp. 5198-5202 ◽  
Author(s):  
Pongpan Laksanalamai ◽  
Dennis L. Maeder ◽  
Frank T. Robb

ABSTRACT The small heat shock protein (sHSP) from the hyperthermophilePyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105°C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105°C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56°C. Survivability of E. colioverexpressing the sHSP was enhanced approximately sixfold during exposure to 50°C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.


2016 ◽  
Vol 6 (4) ◽  
pp. 437-442 ◽  
Author(s):  
Innokentii E. Vishnyakov ◽  
Mikhail I. Bogachev ◽  
Ilnur Salafutdinov ◽  
Sergei N. Borchsenius ◽  
Airat R. Kayumov

2013 ◽  
Vol 59 (8) ◽  
pp. 848-854 ◽  
Author(s):  
Qiu-Ning Liu ◽  
Bao-Jian Zhu ◽  
Li-Shang Dai ◽  
Wei-Wei Fu ◽  
Kun-Zhang Lin ◽  
...  

1999 ◽  
Vol 120 (2) ◽  
pp. 521-528 ◽  
Author(s):  
Alvaro Soto ◽  
Isabel Allona ◽  
Carmen Collada ◽  
Maria-Angeles Guevara ◽  
Rosa Casado ◽  
...  

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