JCVI: Activation of a Prophage-encoded Tyrosine Kinase by a Heterologous Infecting Phage Results In a Self-inflicted Abortive Infection.
 
 
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Friedman, D. I., Mozola, C. C., Beeri, K., Ko, C. C., Reynolds, J. L., Friedman DI, Mozola CC, Beeri K, Ko CC, Reynolds JL

Activation of a Prophage-encoded Tyrosine Kinase by a Heterologous Infecting Phage Results In a Self-inflicted Abortive Infection.

Molecular microbiology. 2011 Nov 01; 82(3). : 567-77.

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Abstract

Bacteria in their struggle for survival have evolved or acquired defences against attacking phage. However, phage often contribute to this defence through mechanisms in which a prophage protects the bacterial population from attack by another, often unrelated, phage. The 933W prophage, which carries Shiga toxin genes that enhance pathogenicity of enterohaemorrhagic Escherichia coli strain O157:H7, also carries the stk gene encoding a eukaryotic-like tyrosine kinase that excludes (aborts) infection by phage HK97. This exclusion requires the kinase activity of Stk. Little, if any, protein tyrosine phosphorylation can be detected in a 933W lysogen prior to infection with HK97, while extensive Stk-mediated tyrosine phosphorylation is evident following infection. This includes autophosphorylation that stabilizes Stk protein from degradation. Although increased levels of Stk are found following HK97 infection, these higher levels are not necessary or sufficient for exclusion or protein phosphorylation. An HK97 open reading frame, orf41, is necessary for exclusion and Stk kinase activity. We hypothesize that interaction with gp41 stimulates Stk kinase activity. Exclusion of HK97 appears to be specific since other phages tested, λ, φ80, H-19B, λ-P22dis and T4rII, were not excluded. Infection of the 933W lysogen with a non-excluded phage fails to induce Stk-determined phosphorylation.

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