The attachment of the male-specific bacteriophage F1 to sensitive strains of Escherichia coli.

Lucien, G.; Schnös, Maria

doi:10.1073/pnas.56.1.126

Cited by 141 publications

(99 citation statements)

References 13 publications

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“…Thus, it seems probable that the A protein is the adsorption protein and is located at only one end of the virion (81,144,146,157). This is consistent with studies on polarity of the virus, which suggest that only one end of the virion acts as an adsorption site (41,66).…”

Section: Suppression Of Amber Mutationssupporting

confidence: 91%

“…This line has been interpreted in terms of a central DNA core in the virion (22), a hole down the center of the virion (23,24,41), or a groove between two parallel strands that might make up the virion (23,24). However, the diameter of these rings is more than 5.5 nm, so that they may not be single virions.…”

Section: Suppression Of Amber Mutationsmentioning

confidence: 99%

“…8). There are only a few of these pili per bacterium (32,41,128), corresponding to the two to three adsorption sites found for Ff (95,191). The adsorption sites apparently can be used only once, since infected cells cannot be superinfected, although they can be co-infected (85,91,95,190).…”

Section: Physiology Of Virus Infection Adsorptionmentioning

confidence: 99%

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Filamentous bacterial viruses

Höhn¹,

Schütz²,

Marvin³

1971

Journal of Molecular Biology

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Section: Suppression Of Amber Mutationssupporting

confidence: 91%

Section: Suppression Of Amber Mutationsmentioning

confidence: 99%

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Filamentous bacterial viruses

Höhn¹,

Schütz²,

Marvin³

1971

Journal of Molecular Biology

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“…One implication may be that tips of pili to which the phages adsorb possess more than one kind of adsorption site. This may be possible, as tips of F pili have at least three similar sites for adsorption of fl phage (Caro & Schnos, 1966).…”

Section: Discussionmentioning

confidence: 99%

Properties of R Plasmid R772 and the Corresponding Pilus-specific Phage PR772

Coetzee

Lecatsas

Coetzee

et al. 1979

Journal of General Microbiology

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R plasmid R772 was isolated from a strain of Proteus mirabilis and is a self-transmissible P-1 incompatibility group plasmid having a molecular weight of about 27 x lo6. It renders bacterial hosts resistant to kanamycin. Phage PR772 was isolated as a phage dependent on the presence of R772 in bacterial hosts. It is hexagonal-shaped with a diameter of 53 nm, has a thick inner membrane and no tail. Vaguely defined appendages are sometimes apparent at some vertices and the phage possesses double-stranded DNA. The DNA has a guanine plus cytosine molar content of 48':d. The phage is sensitive to chloroform and has a buoyant density of 1.26 g ~m -~. These observations suggested that the inner membrane of the phage could contain lipid. Phage PR772 differs in morphology from the doublestranded DNA plasmid-specific phages PR4 and PRRl which adsorb to tips and sides, respectively, of sex pili coded for by P-1 incompatibility group plasmids. Phage PR772 formed clear plaques which varied in diameter. Serologically, phages PR772 and PR4 are possibly related though very distantly, but the two phages have identical host ranges. Phage PR772 adsorbed by one of its apices to tips of sex pili coded for by plasmid R772 in Escherichia coli. It also formed plaques on Salmonella typhimurium, Proteus morganii and Providence strains harbouring this plasmid as well as strains of E. coli carrying plasmids of incompatibility groups N or W. The phage produced areas of partial clearing on lawns of P. mirabilis PM5006 harbouring plasmid R772, the P-1 incompatibility group plasmid RP4, the W group plasmid RSa or the N group plasmid N3, and on lawns of Providence strain P29 carrying plasmid RP4.

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“…F pili are filamentous appendages which help to establish the physical contact between the donor and recipient cells required for the conjugation process. In addition, F pili serve as receptors for F-specific filamentous DNA bacteriophage and icosahedral RNA bacteriophage (2,4,20,22). Pili are up to 2 ,um in length and have diameters of 8 nm and axial holes of 2 nm.…”

mentioning

confidence: 99%

Localization of TraC, a protein involved in assembly of the F conjugative pilus

1992

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TraC is one of the proteins encoded by the F transfer region of the F conjugative plasmid which is required for the assembly of F pilin into the mature F pilus structure. Overproduction of this protein from the plasmid pKAS2, which carries only traC, resulted in the formation of inclusion bodies from which soluble TraC was purified. When small amounts of TraC were produced from pKAS2, the protein was localized to the cytoplasm by using anti-TraC antibodies. Similar analysis of a set of TraC-alkaline phosphatase fusion proteins localized all of these fusion proteins to the cytoplasm. However, when TraC was expressed from the F plasmid, much of it appeared associated with the bacterial membrane fraction. Under these conditions, TraC does not appear to be part of the tip of the F pilus, as neither anti-TraC antibodies nor purified TraC had any effect on the infection of F-containing bacteria by the filamentous bacteriophage f1. These data suggest that TraC is normally associated with the membrane through interactions with other proteins specified by the tra region. This interaction may be via the carboxyl-terminal region of the TraC protein, as a mutant TraC protein containing an Arg-Cys substitution at amino acid 811 exhibits an interaction with the membrane weaker than that of the wild-type protein in the presence of the other Tra proteins.

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The attachment of the male-specific bacteriophage F1 to sensitive strains of Escherichia coli.

Cited by 141 publications

References 13 publications

Filamentous bacterial viruses

Filamentous bacterial viruses

Properties of R Plasmid R772 and the Corresponding Pilus-specific Phage PR772

Localization of TraC, a protein involved in assembly of the F conjugative pilus

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