Recombinant Streptococcus phage Cp-1 Holin (CPH1) is a protein encoded by the cph1 gene of the bacteriophage Cp-1, which infects Streptococcus pneumoniae. This protein belongs to the family of holins, which are essential components in the lysis process of bacterial cells infected by bacteriophages. Holins create lesions in the bacterial cell membrane, allowing endolysins to access and degrade the peptidoglycan layer, leading to cell lysis and the release of phage progeny .
CPH1 is a small protein consisting of 134 amino acids with a molecular weight of approximately 15.4 kDa . It exhibits characteristics typical of holin proteins, such as the ability to form pores in bacterial membranes. The cph1 gene is located upstream of the cpl1 gene, which encodes for a lysozyme (endolysin) in the Cp-1 phage genome. The stop codon of cph1 overlaps with the start codon of cpl1, a common feature in two-component phage lytic systems .
CPH1 can complement a lambda Sam mutation in E. coli, which is a lysis-defective mutant. This suggests that CPH1 has functional similarities with the holin encoded by the lambda phage, further supporting its role in membrane disruption .
The study of CPH1 provides insights into the mechanisms of phage-mediated lysis and has potential applications in the development of novel antimicrobial strategies. By understanding how holins and endolysins work together, researchers can explore new ways to combat bacterial infections, particularly those caused by antibiotic-resistant strains.
| Feature | Description |
|---|---|
| Gene | cph1 |
| Protein Size | 134 amino acids |
| Molecular Weight | Approximately 15.4 kDa |
| Function | Creates lesions in bacterial membranes |
| Expression | Causes cell death but not lysis when expressed alone in E. coli |
| Co-expression with Cpl1 | Leads to efficient lysis of E. coli cells |
| Holin | Source | Function |
|---|---|---|
| CPH1 | Cp-1 phage | Creates lesions in bacterial membranes, facilitating endolysin access |
| Lambda S | Lambda phage | Essential for lysis by creating pores in the membrane |
KEGG: vg:1261217