PhiEF24C is a virulent Myoviridae phage isolated for its therapeutic potential against E. faecalis infections . Its linear double-stranded DNA genome (142,072 bp) encodes 221 open reading frames (ORFs), including structural proteins essential for virion assembly and host recognition . Virion Protein 3 corresponds to a key structural component implicated in host adsorption, as identified through genomic and proteomic analyses .
A spontaneous mutant phage, phiEF24C-P2, harboring a point mutation in orf31 (encoding Virion Protein 3), demonstrated enhanced adsorption rates compared to the wild-type phage :
| Phage Variant | Adsorption Rate (% adsorbed in 10 min) | Host Strain |
|---|---|---|
| Wild-type phiEF24C | 58% | E. faecalis EF14 |
| Mutant phiEF24C-P2 | 92% | E. faecalis EF14 |
| Wild-type phiEF24C | 12% | E. faecalis VRE2 |
| Mutant phiEF24C-P2 | 67% | E. faecalis VRE2 |
This mutation (Glu798Lys in ORF31) improved binding to bacterial surfaces, particularly in low-sensitivity strains like VRE2 .
In Vivo Efficacy: PhiEF24C reduced mortality in sepsis mouse models infected with E. faecalis, even at low multiplicities of infection (MOI = 0.01) .
Safety Profile: Genomic analysis confirmed the absence of virulence factors, antibiotic resistance genes, or lysogeny-associated integrases .
Diagnostic Tools: The C-terminal domain of phiEF24C endolysin has been engineered into magnetic bead complexes for specific detection of E. faecalis in mixed cultures .
Phage Engineering: Recombinant Virion Protein 3 serves as a target for optimizing phage adsorption kinetics, as demonstrated in phiEF24C-P2 .
KEGG: vg:5666497