Two-component nature of bacteriophage T4 receptor activity in Escherichia coli K-12

Henning, Ulf; Jann, Klaus

doi:10.1128/jb.137.1.664-666.1979

Cited by 64 publications

(37 citation statements)

References 22 publications

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“…We reasoned that the expression of the phage receptor could be osmolarity regulated, since the infection of C600 by Stx2⌽-I and 933W was greatly affected by changing the osmolarity of the medium used to grow C600. Since the outer membrane porin proteins such as OmpF and OmpC are known to be the receptors of phage T2 and T4, respectively (13,16,30) and FadL is known to be the receptor of phage T2 (31), the effects of defined mutations of ompC, ompF, or fadL in E. coli on infection of the three converting phages were examined. Examination of the sensitivity of RAM191 ⌬ompC178 zei-198:: Tn10 (28) and RK4786 ompF::Tn5 (15) mutants to the three Stx2-converting phages showed no significant difference among the phages, suggesting that OmpC and OmpF were not involved in phage infection.…”

Section: Isolation Of Stx2-converting Phages From Stec Strainsmentioning

confidence: 99%

Identification and Characterization of a Newly Isolated Shiga Toxin 2-Converting Phage from Shiga Toxin-ProducingEscherichia coli

et al. 1998

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Science 226: [694][695][696] 1984). In this study, we isolated two Stx2-converting phages, designated Stx2⌽-I and Stx2⌽-II, from two clinical strains of STEC associated with the outbreaks in Japan in 1996 and found that Stx2⌽-I resembled 933W, the previously reported Stx2-converting phage, in its infective properties for E. coli K-12 strain C600 while Stx2⌽-II was distinct from them. The sizes of the plaques of Stx2⌽-I and Stx2⌽-II in C600 were different; the former was larger than the latter. The restriction maps of Stx2⌽-I and Stx2⌽-II were not identical; rather, Stx2⌽-II DNA was approximately 3 kb larger than Stx2⌽-I DNA. Furthermore, Stx2⌽-I and Stx2⌽-II showed different phage immunity, with Stx2⌽-I and 933W belonging to the same group. Infection of C600 by Stx2⌽-I or 933W was affected by environmental osmolarity differently from that by Stx2⌽-II. When C600 was grown under conditions of high osmolarity, the infectivity of Stx2⌽-I and 933W was greatly decreased compared with that of Stx2⌽-II. Examination of the plating efficiency of the three phages for the defined mutations in C600 revealed that the efficiency of Stx2⌽-I and 933W for the fadL mutant decreased to less than 10 ؊7 compared with that for C600 whereas the efficiency of Stx2⌽-II decreased to 0.1% of that for C600. In contrast, while the plating efficiency of Stx2⌽-II for the lamB mutant decreased to a low level (0.05% of that for C600), the efficiencies of Stx2⌽-I and 933W were not changed. This was confirmed by the phage neutralization experiments with isolated outer membrane fractions from C600, fadL mutant, or lamB mutant or the purified His 6 -tagged FadL and LamB proteins. Based on the data, we concluded that FadL acts as the receptor for Stx2⌽-I and Stx2⌽-II whereas LamB acts as the receptor only for Stx2⌽-II.

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Section: Isolation Of Stx2-converting Phages From Stec Strainsmentioning

confidence: 99%

Identification and Characterization of a Newly Isolated Shiga Toxin 2-Converting Phage from Shiga Toxin-ProducingEscherichia coli

et al. 1998

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“…Proteins 0-SjO-9 are identical with Ib/Ia, c/b and lb/la, respectively [2-51. The interaction between lipopolysaccharide and major outer membrane proteins has also been suggested from a functional point of view in E. coli. The receptor activity for bacteriophage T4 depends on both lipopolysaccharide and 0 -8 in the K12 strain [6,7], and that for phages T2 [8] and TuIa [9] requires both 0 -9 and lipopolysaccharide. Another major outer membrane protein, called 11* [lo] or d [3], requires lipopolysaccharide to exhibit the receptor activity for phages TuII* [9] and K3 [ l l ] and to inhibit the F-pilus-mediated conjugation [I 1,121.…”

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confidence: 99%

Interaction between Major Outer Membrane Protein (O‐8) and Lipopolysaccharide in Escherichia coli K12

Yamada

Mizushima

1980

European Journal of Biochemistry

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An ordered hexagonal lattice structure with a lattice constant of about 7 nm was reconstituted from outer membrane protein 0 -8 and/or 0 -9 and lipopolysaccharide [H. Yamada and S. Mizushima, J . Bacteriol. 135, 1024Bacteriol. 135, -1031Bacteriol. 135, (1978l. Using this reconstitution system, the interaction between 0 -8 and lipopolysaccharide was studied and the following results were obtained.At least one lipopolysaccharide molecule per one 0 -8 trimer was required for the hexagonal lattice formation. The lattice constant of the hexagonal lattice formed under the conditions was about 6.5 nm. In the presence of a larger amount of lipopolysaccharide, the lattice constant increased to 7.5 nm, being almost the same as that observed in the dodecylsulfate-treated cell envelope.The lattice constant observed with the heptoseless lipopolysaccharide was also 6.5 nm when the lipopolysaccharide/O-8 ratio was low. Although the increase of the lattice constant was observed upon further addition of the lipopolysaccharide, it was appreciably smaller than that with the wildtype lipopolysaccharide.A hexagonal lattice was also formed when lipopolysaccharide was replaced by an equivalent amount of lipid A or even fatty acids. The lattice constant was the same as that with the wild-type lipopolysaccharide when the lipid/protein ratio was low. However, contrary to the case of lipopolysaccharide, the lattice constant remained almost unchanged even when a larger amount of either lipid A or fatty acid was added to the reconstitution system. A slight increase in the lattice constant was observed only when an extremely large amount of lipid A was added to the reconstitution system.These results suggest that (1) both the lipid A moiety and the polysaccharide moiety of lipopolysaccharide participate in the interaction with the 0 -8 trimer, (2) in the lipid A moiety the fatty acid region primarily participates in the hexagonal arrangement of the 0 -8 trimer and the minimum requirement of lipopolysaccharide for the lattice formation is most probably one lipopolysaccharide molecule per 0 -8 trimer and (3) the polysaccharide moiety, probably both the 3-deoxy-~-mannooctulosonate region and the distal end region including heptose, are involved in an interaction of lipopolysaccharide with the 0 -8 trimer to give a proper lattice conformation.In a previous paper [l], we reported the following results for Escherichia coli K12: (a) an ordered hexagonal lattice structure with a lattice constant of about 7 nm was reconstituted on the entire surface of the lipoprotein-bearing peptidoglycan from outer membrane protein 0 -8 and lipopolysaccharide; (b) the lattice structure resembled that observed in the cell envelopes which had been treated with sodium dodecylsulfate; (c) in the absence of the lipoprotein-bearing peptidoglycan or in the presence of the peptidoglycan lacking the bound form of the lipoprotein, 0 -8 and/or 0 -9 and lipopolysaccharide assembled into vesicles with an ordered hexagonal lattice structure, the lattice constant of which was ...

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“…Since the LPS of the polylysogen and the nonlysogen were indistinguishable in both quantity ( Figure 6) and composition (Table 4), and since the plating efficiencies of T3 and T7 were also similar in the two bacteria (Table 3), the differential T4 plating efficiency seems to be very specific for the T4 phage and perhaps not directly related to LPS. In contrast to LPS from E. coli strain B/r, that from strain K12 was shown to require a major outer membrane protein, namely protein Ib (also known as O8), for T4 reception [44,45]. This protein is the same as our protein peak number 9 ( Figure 6), with a Mr of 39,000, which also corresponds to peak 4 of Inouye [23].…”

Section: Summary and Discussionmentioning

confidence: 71%

Altered Growth and Envelope Properties of Polylysogens Containing Bacteriophage Lambda N−cI− Prophages

Barik

Mandal

2020

IJMS

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The bacterial virus lambda (λ) is a temperate bacteriophage that can lysogenize host Escherichia coli (E. coli) cells. Lysogeny requires λ repressor, the cI gene product, which shuts off transcription of the phage genome. The λ N protein, in contrast, is a transcriptional antiterminator, required for expression of the terminator-distal genes, and thus, λ N mutants are growth-defective. When E. coli is infected with a λ double mutant that is defective in both N and cI (i.e., λN -cI -), at high multiplicities of 50 or more, it forms polylysogens that contain 20-30 copies of the λN -cIgenome integrated in the E. coli chromosome. Early studies revealed that the polylysogens underwent "conversion" to long filamentous cells that form tiny colonies on agar. Here, we report a large set of altered biochemical properties associated with this conversion, documenting an overall degeneration of the bacterial envelope. These properties reverted back to those of nonlysogenic E. coli as the metastable polylysogen spontaneously lost the λN -cIgenomes, suggesting that conversion is a direct result of the multiple copies of the prophage. Preliminary attempts to identify lambda genes that may be responsible for conversion ruled out several candidates, implicating a potentially novel lambda function that awaits further studies.

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Two-component nature of bacteriophage T4 receptor activity in Escherichia coli K-12

Abstract: Escherichia coli bacteriophage T4 uses the lipopolysaccharide of the outer cell envelope membrane as a receptor. Lipopolysaccharide from E. coli K-12 required a major outer membrane protein, polypeptide Ib, for phage inactivation.

Cited by 64 publications

References 22 publications

Identification and Characterization of a Newly Isolated Shiga Toxin 2-Converting Phage from Shiga Toxin-ProducingEscherichia coli

Identification and Characterization of a Newly Isolated Shiga Toxin 2-Converting Phage from Shiga Toxin-ProducingEscherichia coli

Interaction between Major Outer Membrane Protein (O‐8) and Lipopolysaccharide in Escherichia coli K12

Altered Growth and Envelope Properties of Polylysogens Containing Bacteriophage Lambda N−cI− Prophages

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