Bacteriophage P1

Yarmolinsky, Michael B.; Sternberg, Nat

doi:10.1007/978-1-4684-5424-6_9

Cited by 132 publications

(152 citation statements)

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“…Notwithstanding the well-known broad-host-range phages such as Mu and P1 (Harshey, 1988;Yarmolinsky & Sternberg, 1988), phage host range is popularly thought to be narrow; this view is enshrined in, and strengthened by, the phage-typing system for classifying bacteria (reviewed by Pitt & Gaston, 1995). Despite a 1998 study specifically assessing the prevalence of broad-host-range phages (Jensen et al, 1998), and recent examples of such phages in Gram-positive genera (Ammann et al, 2008;Chen & Novick, 2009), the consensus remains that phage infection tends to be species and strain specific.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a broad-host-range flagellum-dependent phage that mediates high-efficiency generalized transduction in, and between, Serratia and Pantoea

et al. 2010

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A phage (WOT8) isolated on Serratia sp. ATCC 39006 was shown to be flagellum-dependent, and to mediate generalized transduction with high efficiency (up to 10 "4 transductants per p.f.u.). WOT8 was shown to have a broad host range because it also infected a strain of Pantoea agglomerans isolated from the rhizosphere. Transduction of plasmid-borne antibiotic resistance between the two bacterial genera was demonstrated, consistent with purported ecological roles of phages in dissemination of genes between bacterial genera. Serratia sp. ATCC 39006 and P. agglomerans produce a number of interesting secondary metabolites that have potential applications in cancer therapy and biocontrol of fungal infections. WOT8 has utility as a powerful functional genomics tool in these bacteria.

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Section: Discussionmentioning

confidence: 99%

Characterization of a broad-host-range flagellum-dependent phage that mediates high-efficiency generalized transduction in, and between, Serratia and Pantoea

et al. 2010

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“…One possible explanation as to why we were unable to demonstrate transduction is superinfection immunity. This phenomenon occurs when a lysogen is exposed to a mature bacteriophage that is similar to the integrated prophage (Voyles, 1993), and has been thoroughly studied and documented for both λ and T4 phage infection of E. coli (Yarmolinsky & Sternberg, 1988 ;Voyles, 1993 (Battisti et al, 1998 ;Battisti & Minnick, 1999). Finally, the odds of a doublestranded crossover event would be low, especially considering the heterogeneity of the BLP DNA, i.e.…”

Section: Discussionmentioning

confidence: 99%

“…The heterogeneous mixture of double-stranded host DNA contained in the B. henselae BLPs is protected from chloroform\DNase I treatments by capsid proteins (Anderson et al, 1994 ;Bowers et al, 1998). Furthermore, BLPs are non-lytic even when the host cell is subjected to UV irradiation and\or the addition of mitomycin C. Little more is known about Bartonella BLPs or the mechanisms by which the DNA is packaged, although similarities with generalized defective phages suggest that headful packaging into a pre-formed capsid head may be taking place (Yarmolinsky & Sternberg, 1988 ;Birge, 1994).…”

Section: Introductionmentioning

confidence: 99%

“…Although they share some properties that are similar to true phages, most defective phages package host DNA into pre-formed capsid heads and do not contain any apparent genomic material from the phage (Garro & Marmur, 1970). Defective phages have been found in a variety of unrelated bacteria including the Bacillus subtilis PBSX phage (Yarmolinsky & Sternberg, 1988 ;Birge, 1994) and the Serpulina hyodysenteriae VSH-1 phage (Humphrey et al, 1997), the latter of which has been shown to undergo generalized transduction. The purpose of this study was to characterize the molecular biology of the B. bacilliformis BLPs and begin to address our hypothesis that Bartonella BLPs participate in intraspecies (and possibly interspecies) horizontal gene transfer via transduction.…”

Section: Introductionmentioning

confidence: 99%

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A bacteriophage-like particle from Bartonella bacilliformis

Barbian

Minnick

2000

Microbiology

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Bartonella bacilliformis and Bartonella henselae, the respective agents of Oroya fever and cat-scratch disease in humans, are known to produce bacteriophage-like particles (BLPs) that package 14 kbp segments of the host chromosome. Data from this study suggest that other Bartonella species including Bartonella quintana, Bartonella doshiae and Bartonella grahamii also contain similar BLPs, as evidenced by the presence of a 14 kbp extrachromosomal DNA element in their genomes, whereas Bartonella elizabethae and Bartonella clarridgeiae do not. A purification scheme utilizing chloroform, DNase I and centrifugation was devised to isolate BLPs from B. bacilliformis. Intact BLPs were observed by transmission electron microscopy and were round to icosahedral in shape and approximately 80 nm in diameter. RFLP and Southern blot analysis of BLP DNA from B. bacilliformis suggest that packaging, while non-selective, is less than the near-random packaging previously reported for the B. henselae phage. Data also suggest that the linear, double-stranded BLP DNA molecules have blunt ends with noncovalently closed termini. Packaging of the BLP DNA molecules into a protein coat appears to be closely related to nucleic acid synthesis, as unpackaged phage DNA is not detectable within the host cell. SDS-PAGE analysis of purified BLPs from B. bacilliformis showed three major proteins with apparent molecular masses of 32, 34 and 36 kDa ; values that closely correspond to proteins found in B. henselae BLPs. Western blot analysis performed with patient convalescent serum showed that BLP proteins are slightly immunogenic in humans. To determine if BLPs contribute to horizontal gene transfer, mutants of B. bacilliformis were generated by allelic exchange with an internal fragment of the 16S-23S rDNA intergenic spacer region and a suicide vector construct, termed pKB1. BLPs from one of the resultant strains were able to package the mutagenized region containing the kanamycinresistance cassette ; however, numerous approaches and attempts at intraspecies transduction using these BLPs were unsuccessful.

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“…P1 is unusual in that its endolysin gene, lyz, is not clustered with the holin and antiholin, as is found in all lambdoid and many other phage genomes (6). Moreover, unlike phage , which requires both its holin and endolysin to effect host lysis, P1 mutants deleted for the putative holin gene lydA are plaque formers, although lysis is somewhat delayed when compared with the wild-type phage (7,8). Here, we report the results of experiments to determine the mechanism of the apparent holin independence of P1 Lyz-mediated host lysis.…”

mentioning

confidence: 99%

A signal-arrest-release sequence mediates export and control of the phage P1 endolysin

Struck

Deaton

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

149

207

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The Lyz endolysin of bacteriophage P1 was found to cause lysis of the host without a holin. Induction of a plasmid-cloned lyz resulted in lysis, and the lytic event could be triggered prematurely by treatments that dissipate the proton-motive force. Instead of requiring a holin, export was mediated by an N-terminal transmembrane domain (TMD) and required host sec function. Exported Lyz of identical SDS͞PAGE mobility was found in both the membrane and periplasmic compartments, indicating that periplasmic Lyz was not generated by the proteolytic cleavage of the membrane-associated form. In gene fusion experiments, the Lyz TMD directed PhoA to both the membrane and periplasmic compartments, whereas the TMD of the integral membrane protein FtsI restricts Lyz to the membrane. Thus, the N-terminal domain of Lyz is both necessary and sufficient not only for export of this endolysin to the membrane but also for its release into the periplasm. The unusual N-terminal domain, rich in residues that are weakly hydrophobic, thus functions as a signal-arrest-release sequence, which first acts as a normal signal-arrest domain to direct the endolysin to the periplasm in membrane-tethered form and then allows it to be released as a soluble active enzyme in the periplasm. Examination of the protein sequences of related bacteriophage endolysins suggests that the presence of an N-terminal signalarrest-release sequence is not unique to Lyz. These observations are discussed in relation to the role of holins in the control of host lysis by bacteriophage encoding a secretory endolysin.

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Bacteriophage P1

Cited by 132 publications

References 405 publications

Characterization of a broad-host-range flagellum-dependent phage that mediates high-efficiency generalized transduction in, and between, Serratia and Pantoea

Characterization of a broad-host-range flagellum-dependent phage that mediates high-efficiency generalized transduction in, and between, Serratia and Pantoea

A bacteriophage-like particle from Bartonella bacilliformis

A signal-arrest-release sequence mediates export and control of the phage P1 endolysin

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