Characterization and determination of holin protein of Streptococcus suis bacteriophage SMP in heterologous host

Virology Journal

Jianhe Sun¹  Hengan Wang¹  Xiangpeng Meng¹  Bin Du¹  Wenhui Ji¹  Yaxian Yan¹  Yibo Shi¹ 

[1] Department of Animal Science, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai Key Laboratory of Veterinary Biotechnology, 800 Dongchuan Road, Shanghai, People's Republic of China

关键词: Lysin;    Holin;    Bacteriophage;    Streptococcus suis;   

Others  :  1154846
DOI  :  10.1186/1743-422X-9-70

 received in 2011-10-16, accepted in 2012-03-22,  发布年份 2012

【 摘 要 】

Background

Holins are a group of phage-encoded membrane proteins that control access of phage-encoded endolysins to the peptidoglycan, and thereby trigger the lysis process at a precise time point as the 'lysis clock'. SMP is an isolated and characterized Streptococcus suis lytic phage. The aims of this study were to determine the holin gene, HolSMP, in the genome of SMP, and characterized the function of holin, HolSMP, in phage infection.

Results

HolSMP was predicted to encode a small membrane protein with three hydrophobic transmembrane helices. During SMP infections, HolSMP was transcribed as a late gene and HolSMP accumulated harmlessly in the cell membrane before host cell lysis. Expression of HolSMP in Escherichia coli induced an increase in cytoplasmic membrane permeability, an inhibition of host cell growth and significant cell lysis in the presence of LySMP, the endolysin of phage SMP. HolSMP was prematurely triggered by the addition of energy poison to the medium. HolSMP complemented the defective λ S allele in a non-suppressing Escherichia coli strain to produce phage plaques.

Conclusions

Our results suggest that HolSMP is the holin protein of phage SMP and a two-step lysis system exists in SMP.

【 授权许可】

   
2012 Shi et al; licensee BioMed Central Ltd.

【 图 表 】

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