Bacteriophage-tail-like Particles Associated with Intra-species Killing of Proteus vulgaris

Abstract

SUMMARYOne hundred and eighteen different strains of Proteus vulgaris were investigated for bacteriocinogeny. These and an additional 44 strains of P.vulgaris were used as indicators. Sixty-seven of the strains had a nontransmissible killing effect on one or more of the indicator organisms and 3o of these 67 bacteriocins with different spectra of activity were further investigated. Individual bacteriocins killed from 5 to 87 of the P. vulgaris indicators and a number of 44 different P. mirabilis strains but had no action on strains of other species of the family Enterobacteriaeeae. Broth cultures of bacteriocinogenic strains are inducible by ultraviolet fight and yield bacteriocin titres of about I/IOO. Activity is sedimentable by high-speed centrifugation. Electron microscopy of all 3o preparations revealed similar phage-tail-like structures with a contractile sheath round a hollow core. The structures consisted of protein and did not contain DNA. The particles resembled some pyocins and also the tail of a P. vulgaris transducing phage. In z preparations a few phage-like particles resembling other Proteus phages were also seen. Bacteriocin activity was always associated with uncontracted sheaths, and triggered tails did not adsorb to susceptible organisms. We conclude that the tail-like structures are the products of defective lysogeny. The high incidence of the latter state may be accounted for by the selection of genes favourable to the host which were originally acquired through transduction by lysogenization or lysogenic conversion.

Characterization of Enterocoliticin, a Phage Tail-Like Bacteriocin, and Its Effect on Pathogenic Yersinia enterocolitica Strains

“…The longitudinal length of enterocoliticin particles (ca. 80 nm) was clearly smaller than described for other particles of Enterobacteriacea, i.e., the length of carotovericin of Erwinia carotovora Er was 184 nm (27), the length of xenorhabdicin of Xenorhabdus nematophilus was 170 nm (31), and the proteocins of Proteus vulgaris had a length of 128 nm (11). The ultrastructural details of the enterocoliticin particles, including the measurements of tail length and diameter, resembled those of bacteriophages of the T-even phages (1) or coliphage Mu (32).…”

The purification, structure and synthesis of proticine 3

“…Other workers (Taubeneck, 1963;Coetzee, de Klerk and Coetzee, 1968;Al-Jumaili, 1976) have found bacteriocin activity from Proteus strains to be associated with phage tail-like structures similar in morphology and dimensions to those of proticine 3. Although tail-like fibres, base plates and pins were not found with P. vulgaris bacteriocins (Coetzee et al, 1968) they appear to be present in proticine 3 and have been found in other bacteriocins from P. mirabilis (Al-Jumaili, 1976). These structures are important for attachment to specific receptor sites on the cell surface before contraction of the "nail" form to the "rocket" form.…”

“…These structures are important for attachment to specific receptor sites on the cell surface before contraction of the "nail" form to the "rocket" form. Biological activity is thought to be associated only with the "nail" form of the particulate bacteriocins (Coetzee et al, 1968;Higerd, Baechler and Berk, 1969). Higerd et al (1969) reported that the conversion reaction of "nails" to "rockets" is reversible for pyocines although the conversion of a "rocket" back to a "nail" did not restore biological activity; it appeared that the lethal activity was lost in the initial change of a "nail" into a "rocket" form.…”

Rod-shaped Pyocin 28

“…Recently, electron microscopic studies have revealed that the structure of some bacteriocins resembles a phage-like object or phage component such as the tail assembly. (Endo et al 1965;Meningmann, 1965;Sandoval, Reilly & Tandler, 1965; Ishii, Nishi & Egami, 1965; Bradley & Dewar, 1966; Higerd, Baechler & Berk, 1967;Bradley, 1967;Lang, McDonald & Gardner, 1968;Coetzee et al 1968).…”

“…Recently, electron microscopic studies have revealed that the structure of some bacteriocins resembles a phage-like object or phage component such as the tail assembly. (Endo et al 1965;Meningmann, 1965;Sandoval, Reilly & Tandler, 1965; Ishii, Nishi & Egami, 1965; Bradley & Dewar, 1966; Higerd, Baechler & Berk, 1967;Bradley, 1967;Lang, McDonald & Gardner, 1968;Coetzee et al 1968).Ishii et aL (1965) showed that a trypsin-resistant pyocin, a bacteriocin of Pseudomonas aeruginosa closely resembles T-even phage tails with a contracti/e sheath. Takeya et al (1966) isolated a small pyocin with a different morphology and designated it pyocin 28.…”