scholarly journals Bacteriophage P2

Bacteriophage ◽  
2016 ◽  
Vol 6 (1) ◽  
pp. e1145782 ◽  
Author(s):  
Gail E. Christie ◽  
Richard Calendar
Keyword(s):  
1984 ◽  
Vol 178 (3) ◽  
pp. 629-651 ◽  
Author(s):  
Berit Lundqvist ◽  
G. Bertani
Keyword(s):  

2011 ◽  
Vol 79 (8) ◽  
pp. 3262-3272 ◽  
Author(s):  
Anna Allué-Guardia ◽  
Cristina García-Aljaro ◽  
Maite Muniesa

ABSTRACTCytolethal distending toxin (Cdt) is produced by a variety of pathogenic bacteria, including pathogenic serotypes of Shiga toxin-producingEscherichia coli(STEC). The Cdt family comprises five variants (Cdt-I to Cdt-V) encoded by three genes located within the chromosome or plasmids or, in the case of Cdt-I, within bacteriophages. In this study, we evaluated the occurrence of thecdtgene in a collection of 140 environmental STEC isolates.cdtwas detected in 12.1% of strains, of which five strains carried inducible bacteriophages containing the Cdt-V variant. Two Cdt-V phages of theSiphoviridaemorphology lysogenizedShigella sonnei, generating two lysogens: a single Cdt phage lysogen and a double lysogen, containing a Cdt phage and an Stx phage, both from the wild-type strain. The rates of induction of Cdt phages were evaluated by quantitative PCR, and spontaneous induction of Cdt-V phage was observed, whereas induction of Stx phage in the double lysogen was mitomycin C dependent. The Cdt distending effect was observed in HeLa cells inoculated with the supernatant of the Cdt-V phage lysogen. A ClaI fragment containing thecdt-Vgene of one phage was cloned, and sequencing confirmed the presence of Cdt-V, as well as a fragment downstream from thecdthomolog togpA, encoding a replication protein of bacteriophage P2. Evaluation of Cdt-V phages in nonclinical water samples showed densities of 102to 109gene copies in 100 ml, suggesting the high prevalence of Cdt phages in nonclinical environments.


2013 ◽  
Vol 42 (4) ◽  
pp. 2725-2735 ◽  
Author(s):  
Ronnie P.-A. Berntsson ◽  
Richard Odegrip ◽  
Wilhelmina Sehlén ◽  
Karin Skaar ◽  
Linda M. Svensson ◽  
...  

Abstract The Cox protein from bacteriophage P2 is a small multifunctional DNA-binding protein. It is involved in site-specific recombination leading to P2 prophage excision and functions as a transcriptional repressor of the P2 Pc promoter. Furthermore, it transcriptionally activates the unrelated, defective prophage P4 that depends on phage P2 late gene products for lytic growth. In this article, we have investigated the structural determinants to understand how P2 Cox performs these different functions. We have solved the structure of P2 Cox to 2.4 Å resolution. Interestingly, P2 Cox crystallized in a continuous oligomeric spiral with its DNA-binding helix and wing positioned outwards. The extended C-terminal part of P2 Cox is largely responsible for the oligomerization in the structure. The spacing between the repeating DNA-binding elements along the helical P2 Cox filament is consistent with DNA binding along the filament. Functional analyses of alanine mutants in P2 Cox argue for the importance of key residues for protein function. We here present the first structure from the Cox protein family and, together with previous biochemical observations, propose that P2 Cox achieves its various functions by specific binding of DNA while wrapping the DNA around its helical oligomer.


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