Journal of Microbiology

Jinghua Cui

2 Articles

Molecular Cloning and Characterization of clyA Genes in Various Serotypes of Salmonella enterica: Lan Ji Huang , Jinghua Cui , Hong Hua Piao , Yeongjin Hong , Hyon E. Choy , Phil Youl Ryu; J. Microbiol. 2010;48(5):663-667. Published online November 3, 2010; DOI: https://doi.org/10.1007/s12275-010-9268-9

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Cytolysin A (ClyA) is a pore-forming hemolytic protein encoded by the clyA gene. It has been identified in Salmonella enterica serovars Typhi and Paratyphi A. To identify and characterize the clyA genes in various Salmonella enterica strains, 21 different serotypes of strains isolated from clinical specimens were presently examined. Full-length clyA genes were found in S. enterica serovar Brandenburg, Indiana, Panama, and Schwarzengrund strains by polymerase chain reaction amplification. The ClyA proteins from these four strains showed >97% amino acid identity to that of S. enterica serovar Typhi. Although all four serovars expressed detectable levels of ClyA as determined by Western blot analysis, they did not show a strong hemolytic effect on blood agar, indicating that ClyA may not be efficiently expressed or secreted. Escherichia coli transformed with clyA genes from the four serovars enhanced production of ClyA proteins and hemolytic activities to a level similar to S. enterica serovar Typhi ClyA. The present results suggest that ClyA may play a role in the pathogenesis of S. enterica serovar Brandenburg, Indiana, Panama and Schwarzengrund.

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Effect of Iron on Cytolysin A Expression in Salmonella enterica serovar Typhi: Jinghua Cui , Honghua Piao , Shen Jin , Hee Sam Na , Yeongjin Hong , Hyon E Choy , Phil Youl Ryu; J. Microbiol. 2009;47(4):479-485. Published online September 9, 2009; DOI: https://doi.org/10.1007/s12275-009-0039-4

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Abstract PDF

Previously, a novel protein ClyA (Cytolysin A) has been identified in Escherichia coli K-12, Salmonella enterica serovars Typhi and Paratyphi A and Shigella. Salmonella spp. synthesize substantial amounts of ClyA upon infection of the human host, although the mechanism by which ClyA is induced in vivo is unclear. Since environmental signals could control the expression of virulence determinants, ClyA expression in S. Typhi Ty2 was tested by Western blotting in the presence of normal pooled human serum (NPS). The level of ClyA expression increased in the presence of NPS in a concentration-dependent manner. RPMI 1640 medium similarly induced ClyA expression. ClyA expression was inversely proportional to the concentration of iron in RPMI medium. Therefore, we speculated that iron inhibited the expression of ClyA in S. Typhi Ty2, and free iron depletion may be one of the causes of S. Typhi-mediated induction of ClyA in vivo. Transcription from a clyA-lacZ fusion gene decreased as iron concentration increased, but not as significantly as the ClyA protein expression. It is concluded that the regulatory effect of iron on clyA expression is mainly at translational level.

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MicrobiologyOpen.2013; 2(2): 326. CrossRef
Molecular cloning and characterization of clyA genes in various serotypes of Salmonella enterica
Lan Ji Huang, Jinghua Cui, Hong Hua Piao, Yeongjin Hong, Hyon E. Choy, Phil Youl Ryu
The Journal of Microbiology.2010; 48(5): 663. CrossRef

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