Article Abstract:
The morphology and protein profiles of 22 listeriaphages were determined. The morphological characteristics which include the head and tail diameter, tail length, contractility and flexibility were determined by electron microscopy. The phages were found to have icosohedral heads andexhibited either flexible or stiff and contractile or noncontractiletails. Two of the 22 phages belong to the Myoviridae family, while the other twnety were classified into the Siphoviridae family. In addition, electrophoretic analysis showed that all the phages possessed specific protein profiles. The major proteins were found to be the structural proteins of the capsid and tail.
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Article Abstract:
A study conducted on monocins produced by the bacteria Listeria shows that these monocins are flexible non-contractile bacteriophage-tail-like particles which are probably formed by a defect in the morphogenesis of phages. These monocins produce a lytic enzyme which causes lysis of Escherichia coli cells. The lytic enzyme is an endolysin and is encoded by the cpl2438 gene. The structure of cpl2438 is similar to that of other holin genes.
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Article Abstract:
A new technique uses a recombinant Listeria bacteriophage A118 lytic enzyme for the fast lysis of Listeria cells and the technique is compatible for all listerial species. DNA, RNA and proteins from Listeria cells are recovered by this technique. This method helps identify and differentiate Listeria strains at ambient temperatures.
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