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Genome and proteome of Campylobacter jejuni bacteriophage NCTC 12673.
- Source :
-
Applied and environmental microbiology [Appl Environ Microbiol] 2011 Dec; Vol. 77 (23), pp. 8265-71. Date of Electronic Publication: 2011 Sep 30. - Publication Year :
- 2011
-
Abstract
- Campylobacter jejuni continues to be the leading cause of bacterial food-borne illness worldwide, so improvements to current methods used for bacterial detection and disease prevention are needed. We describe here the genome and proteome of C. jejuni bacteriophage NCTC 12673 and the exploitation of its receptor-binding protein for specific bacterial detection. Remarkably, the 135-kb Myoviridae genome of NCTC 12673 differs greatly from any other proteobacterial phage genome described (including C. jejuni phages CP220 and CPt10) and instead shows closest homology to the cyanobacterial T4-related myophages. The phage genome contains 172 putative open reading frames, including 12 homing endonucleases, no visible means of packaging, and a putative trans-splicing intein. The phage DNA appears to be strongly associated with a protein that interfered with PCR amplification and estimation of the phage genome mass by pulsed-field gel electrophoresis. Identification and analyses of the receptor-binding protein (Gp48) revealed features common to the Salmonella enterica P22 phage tailspike protein, including the ability to specifically recognize a host organism. Bacteriophage receptor-binding proteins may offer promising alternatives for use in pathogen detection platforms.
- Subjects :
- DNA, Viral chemistry
DNA, Viral genetics
Molecular Sequence Data
Myoviridae chemistry
Myoviridae genetics
Open Reading Frames
Sequence Analysis, DNA
Bacteriophages chemistry
Bacteriophages genetics
Campylobacter jejuni virology
Genes, Viral
Genome, Viral
Proteome analysis
Viral Proteins analysis
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5336
- Volume :
- 77
- Issue :
- 23
- Database :
- MEDLINE
- Journal :
- Applied and environmental microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 21965409
- Full Text :
- https://doi.org/10.1128/AEM.05562-11