This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Martín, A. C. Articles by García, P. Search for Related Content PubMed PubMed Citation Articles by Martín, A. C. Articles by García, P.

 Previous Article  |  Next Article 

J. Bacteriol., Jan 1998, 210-217, Vol 180, No. 2
Copyright © 1998, American Society for Microbiology

Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells [In Process Citation]

AC Martin, R Lopez and P Garcia
Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, CSIC, Madrid, Spain.

The two lysis genes cph1 and cpl1 of the Streptococcus pneumoniae bacteriophage Cp-1 coding for holin and lysozyme, respectively, have been cloned and expressed in Escherichia coli. Synthesis of the Cph1 holin resulted in bacterial cell death but not lysis. The cph1 gene was able to complement a lambda Sam mutation in the nonsuppressing E. coli HB101 strain to produce phage progeny, suggesting that the holins encoded by both phage genes have analogous functions and that the pneumococcal holin induces a nonspecific lesion in the cytoplasmic membrane. Concomitant expression of both holin and lysin of Cp-1 in E. coli resulted in cell lysis, apparently due to the ability of the Cpl1 lysozyme to hydrolyze the peptidoglycan layer of this bacterium. The functional analysis of the cph1 and cpl1 genes cloned in a pneumococcal mutant with a complete deletion of the lytA gene, which codes for the S. pneumoniae main autolysin, provided the first direct evidence that, in this gram-positive-bacterium system, the Cpl1 endolysin is released to its murein substrate through the activity of the Cph1 holin. Demonstration of holin function was achieved by proving the release of pneumolysin to the periplasmic fraction, which strongly suggested that the holin produces a lesion in the pneumococcal membrane.

This article has been cited by other articles:

• Frias, M. J., Melo-Cristino, J., Ramirez, M. (2009). The Autolysin LytA Contributes to Efficient Bacteriophage Progeny Release in Streptococcus pneumoniae. J. Bacteriol. 191: 5428-5440 [Abstract] [Full Text]  
• Monterroso, B., Saiz, J. L., Garcia, P., Garcia, J. L., Menendez, M. (2008). Insights into the Structure-Function Relationships of Pneumococcal Cell Wall Lysozymes, LytC and Cpl-1. J. Biol. Chem. 283: 28618-28628 [Abstract] [Full Text]  
• Loessner, M. J., Gaeng, S., Scherer, S. (1999). Evidence for a Holin-Like Protein Gene Fully Embedded Out of Frame in the Endolysin Gene of Staphylococcus aureus Bacteriophage 187. J. Bacteriol. 181: 4452-4460 [Abstract] [Full Text]  
• Sheehan, M. M., Stanley, E., Fitzgerald, G. F., van Sinderen, D. (1999). Identification and Characterization of a Lysis Module Present in a Large Proportion of Bacteriophages Infecting Streptococcus thermophilus. Appl. Environ. Microbiol. 65: 569-577 [Abstract] [Full Text]