A novel lysis system in PM2, a lipid-containing marine double-stranded DNA bacteriophage
Author | Affiliation | |||
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Krupovič, Mart | ||||
Date |
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2007 |
In this study we investigated the lysis system of the lipid-containing double-stranded DNA bacteriophage PM2 infecting Gram-negative marine Pseudoalteromonas species. We analysed wt and lysis-deficient phage-induced changes in the host physiology and ascribed functions to two PM2 gene products (gp) involved in lysis. We show that bacteriophage PM2 uses a novel system to disrupt the infected cell. The novelty is based on the following findings: (i) gp k is needed for the permeabilization of the cytoplasmic membrane and appears to play the role of a typical holin. However, its unique primary structure [53 aa, 1 transmembrane domain (TMD)] places it into a new class of holins. (ii) We have proposed that, unlike other bacteriophages studied, PM2 relies on lytic factors of the cellular origin for digestion of the peptidoglycan. (iii) gp l (51 aa, no TMDs) is needed for disruption of the outer membrane, which is highly rigidified by the divalent cations abundant in the marine environment. The gp l has no precedent in other phage lytic systems studied so far. However, the presence of open reading frame l-like genes in genomes of other bacterial viruses suggests that the same system might be used by other phages and is not unique to PM2.
Journal | IF | AIF | AIF (min) | AIF (max) | Cat | AV | Year | Quartile |
---|---|---|---|---|---|---|---|---|
MOLECULAR MICROBIOLOGY | 5.462 | 3.772 | 3.319 | 4.225 | 2 | 1.386 | 2007 | Q1 |
Journal | IF | AIF | AIF (min) | AIF (max) | Cat | AV | Year | Quartile |
---|---|---|---|---|---|---|---|---|
MOLECULAR MICROBIOLOGY | 5.462 | 3.772 | 3.319 | 4.225 | 2 | 1.386 | 2007 | Q1 |