期刊
VIRUSES-BASEL
卷 13, 期 2, 页码 -出版社
MDPI
DOI: 10.3390/v13020296
关键词
Y; pseudotuberculosis; bacteriophage; receptor; Myoviridae; lipopolysaccharide; tail fiber; Gp38
类别
资金
- Ministry of Higher Education and Scientific Research, Tripoli, Libya
- Doctoral Programme in Microbiology and Biotechnology (MBDP) of University of Helsinki
- Academy of Finland [1288701]
The Yersinia bacteriophages fPS-2, fPS-65, and fPS-90 isolated from pig stools exhibit relatively wide host ranges and genetic diversity in terms of genome structure and receptor recognition. The study also revealed the genetic mutations in phage-resistant mutants and the successful complementation of these mutations by introducing wild-type genes. The host recognition was assigned to a specific protein, Gp38, which plays a key role in binding to the host cells.
The Yersinia bacteriophages fPS-2, fPS-65, and fPS-90, isolated from pig stools, have long contractile tails and elongated heads, and they belong to genus Tequatroviruses in the order Caudovirales. The phages exhibited relatively wide host ranges among Yersinia pseudotuberculosis and related species. One-step growth curve experiments revealed that the phages have latent periods of 50-80 min with burst sizes of 44-65 virions per infected cell. The phage genomes consist of circularly permuted dsDNA of 169,060, 167,058, and 167,132 bp in size, respectively, with a G + C content 35.3%. The number of predicted genes range from 267 to 271. The phage genomes are 84-92% identical to each other and ca 85% identical to phage T4. The phage receptors were identified by whole genome sequencing of spontaneous phage-resistant mutants. The phage-resistant strains had mutations in the ompF, galU, hldD, or hldE genes. OmpF is a porin, and the other genes encode lipopolysaccharide (LPS) biosynthetic enzymes. The ompF, galU, and hldE mutants were successfully complemented in trans with respective wild-type genes. The host recognition was assigned to long tail fiber tip protein Gp38, analogous to that of T-even phages such as Salmonella phage S16, specifically to the distal beta-helices connecting loops.
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