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Journal articles on the topic 'Bacteriophage P22'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

AHN, JUHEE, SONGRAE KIM, LAE-SEUNG JUNG, and DEBABRATA BISWAS. "In Vitro Assessment of the Susceptibility of Planktonic and Attached Cells of Foodborne Pathogens to Bacteriophage P22-Mediated Salmonella Lysates." Journal of Food Protection 76, no. 12 (December 1, 2013): 2057–62. http://dx.doi.org/10.4315/0362-028x.jfp-13-183.

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This study was designed to evaluate the lytic activity of bacteriophage P22 against Salmonella Typhimurium ATCC 19585 (Salmonella Typhimurium P22−) at various multiplicities of infections (MOIs), the susceptibility of preattached Salmonella cells against bacteriophage P22, and the effect of P22-mediated bacterial lysates (extracellular DNA) on the attachment ability of Listeria monocytogenes ATCC 7644 and enterohemorrhagic Escherichia coli ATCC 700927 to surfaces. The numbers of attached Salmonella Typhimurium P22− cells were effectively reduced to below the detection limit (1 log CFU/ml) at the fixed inoculum levels of 3 × 102 CFU/ml (MOI = 3.12) and 3 × 103 CFU/ml (MOI = 4.12) by bacteriophage P22. The attached Salmonella Typhimurium P22− cells remained more than 2 log CFU/ml, with increasing inoculum levels from 3 × 104 to 3 × 107 CFU/ml infected with 4 × 108 PFU/ml of P22. The number of preattached Salmonella Typhimurium P22− cells was noticeably reduced by 2.72 log in the presence of P22. The highest specific attachment ability values for Salmonella Typhimurium P22−, Salmonella Typhimurium ATCC 23555 carrying P22 prophage (Salmonella Typhimurium P22+), L. monocytogenes, and enterohemorrhagic E. coli were 2.09, 1.06, 1.86, and 1.08, respectively, in the bacteriophage-mediated cell-free supernatants (CFS) containing high amounts of extracellular DNA. These results suggest that bacteriophages could potentially be used to effectively eliminate planktonic and preattached Salmonella Typhimurium P22− cells with increasing MOI. However, further research is needed to understand the role of bacteriophage-induced lysates in bacterial attachment, which can provide useful information for the therapeutic use of bacteriophage in the food system.

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2

Mattis, Aras N., Richard I. Gumport, and Jeffrey F. Gardner. "Purification and Characterization of Bacteriophage P22 Xis Protein." Journal of Bacteriology 190, no. 17 (May 23, 2008): 5781–96. http://dx.doi.org/10.1128/jb.00170-08.

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ABSTRACT The temperate bacteriophages λ and P22 share similarities in their site-specific recombination reactions. Both require phage-encoded integrase (Int) proteins for integrative recombination and excisionase (Xis) proteins for excision. These proteins bind to core-type, arm-type, and Xis binding sites to facilitate the reaction. λ and P22 Xis proteins are both small proteins (λ Xis, 72 amino acids; P22 Xis, 116 amino acids) and have basic isoelectric points (for P22 Xis, 9.42; for λ Xis, 11.16). However, the P22 Xis and λ Xis primary sequences lack significant similarity at the amino acid level, and the linear organizations of the P22 phage attachment site DNA-binding sites have differences that could be important in quaternary intasome structure. We purified P22 Xis and studied the protein in vitro by means of electrophoretic mobility shift assays and footprinting, cross-linking, gel filtration stoichiometry, and DNA bending assays. We identified one protected site that is bent approximately 137 degrees when bound by P22 Xis. The protein binds cooperatively and at high protein concentrations protects secondary sites that may be important for function. Finally, we aligned the attP arms containing the major Xis binding sites from bacteriophages λ, P22, L5, HP1, and P2 and the conjugative transposon Tn916. The similarity in alignments among the sites suggests that Xis-containing bacteriophage arms may form similar structures.

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3

Vershon, Andrew K., Sha-Mei Liao, William R. McClure, and Robert T. Sauer. "Bacteriophage P22 Mnt repressor." Journal of Molecular Biology 195, no. 2 (May 1987): 311–22. http://dx.doi.org/10.1016/0022-2836(87)90652-8.

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4

Tang, L., G. Lander, S. Casjens, W. Marion, G. Cingolani, P. Prevelige, and J. Johnson. "The Injectosome of Bacteriophage P22." Microscopy and Microanalysis 12, S02 (July 31, 2006): 394–95. http://dx.doi.org/10.1017/s1431927606064221.

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5

Poteete, Anthony R., Anita C. Fenton, and Arlene V. Semerjian. "Bacteriophage P22 accessory recombination function." Virology 182, no. 1 (May 1991): 316–23. http://dx.doi.org/10.1016/0042-6822(91)90675-2.

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6

Heffron, Joe, Matthew Bork, Brooke K. Mayer, and Troy Skwor. "A Comparison of Porphyrin Photosensitizers in Photodynamic Inactivation of RNA and DNA Bacteriophages." Viruses 13, no. 3 (March 23, 2021): 530. http://dx.doi.org/10.3390/v13030530.

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Effective broad-spectrum antiviral treatments are in dire need as disinfectants and therapeutic alternatives. One such method of disinfection is photodynamic inactivation, which involves the production of reactive oxygen species from dissolved oxygen in response to light-stimulated photosensitizers. This study evaluated the efficacy of functionalized porphyrin compounds for photodynamic inactivation of bacteriophages as human virus surrogates. A blue-light light emitting diode (LED) lamp was used to activate porphyrin compounds in aqueous solution (phosphate buffer). The DNA bacteriophages ΦX174 and P22 were more resistant to porphyrin TMPyP photodynamic inactivation than RNA bacteriophage fr, with increasing rates of inactivation in the order: ΦX174 << P22 << fr. Bacteriophage ΦX174 was therefore considered a resistant virus suitable for the evaluation of three additional porphyrins. These porphyrins were synthesized from TMPyP by inclusion of a central palladium ion (PdT4) and/or the addition of a hydrophobic C14 chain (PdC14 or C14). While the inactivation rate of bacteriophage ΦX174 via TMPyP was similar to previous reports of resistant viruses, ΦX174 inactivation increased by a factor of approximately 2.5 using the metalloporphyrins PdT4 and PdC14. The order of porphyrin effectiveness was TMPyP < C14 < PdT4 < PdC14, indicating that both Pd2+ ligation and C14 functionalization aided virus inactivation.

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7

Adams, M. B., H. R. Brown, and S. Casjens. "Bacteriophage P22 tail protein gene expression." Journal of Virology 53, no. 1 (1985): 180–84. http://dx.doi.org/10.1128/jvi.53.1.180-184.1985.

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8

Walter, Monika, Christian Fiedler, Renate Grassl, Manfred Biebl, Reinhard Rachel, X. Lois Hermo-Parrado, Antonio L. Llamas-Saiz, Robert Seckler, Stefan Miller, and Mark J. van Raaij. "Structure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a Myovirus." Journal of Virology 82, no. 5 (December 12, 2007): 2265–73. http://dx.doi.org/10.1128/jvi.01641-07.

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ABSTRACT A new Salmonella enterica phage, Det7, was isolated from sewage and shown by electron microscopy to belong to the Myoviridae morphogroup of bacteriophages. Det7 contains a 75-kDa protein with 50% overall sequence identity to the tail spike endorhamnosidase of podovirus P22. Adsorption of myoviruses to their bacterial hosts is normally mediated by long and short tail fibers attached to a contractile tail, whereas podoviruses do not contain fibers but attach to host cells through stubby tail spikes attached to a very short, noncontractile tail. The amino-terminal 150 residues of the Det7 protein lack homology to the P22 tail spike and are probably responsible for binding to the base plate of the myoviral tail. Det7 tail spike lacking this putative particle-binding domain was purified from Escherichia coli, and well-diffracting crystals of the protein were obtained. The structure, determined by molecular replacement and refined at a 1.6-Å resolution, is very similar to that of bacteriophage P22 tail spike. Fluorescence titrations with an octasaccharide suggest Det7 tail spike to bind its receptor lipopolysaccharide somewhat less tightly than the P22 tail spike. The Det7 tail spike is even more resistant to thermal unfolding than the already exceptionally stable homologue from P22. Folding and assembly of both trimeric proteins are equally temperature sensitive and equally slow. Despite the close structural, biochemical, and sequence similarities between both proteins, the Det7 tail spike lacks both carboxy-terminal cysteines previously proposed to form a transient disulfide during P22 tail spike assembly. Our data suggest receptor-binding module exchange between podoviruses and myoviruses in the course of bacteriophage evolution.

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9

Pedulla, Marisa L., Michael E. Ford, Tharun Karthikeyan, Jennifer M. Houtz, Roger W. Hendrix, Graham F. Hatfull, Anthony R. Poteete, Eddie B. Gilcrease, Danella A. Winn-Stapley, and Sherwood R. Casjens. "Corrected Sequence of the Bacteriophage P22 Genome." Journal of Bacteriology 185, no. 4 (February 15, 2003): 1475–77. http://dx.doi.org/10.1128/jb.185.4.1475-1477.2003.

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ABSTRACT We report the first accurate genome sequence for bacteriophage P22, correcting a 0.14% error rate in previously determined sequences. DNA sequencing technology is now good enough that genomes of important model systems like P22 can be sequenced with essentially 100% accuracy with minimal investment of time and resources.

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10

Moore, Sean D., and Peter E. Prevelige. "Bacteriophage P22 portal vertex formation in vivo." Journal of Molecular Biology 315, no. 5 (February 2002): 975–94. http://dx.doi.org/10.1006/jmbi.2001.5275.

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11

Parker, Matthew H., Sherwood Casjens, and Peter E. Prevelige. "Functional domains of bacteriophage P22 scaffolding protein." Journal of Molecular Biology 281, no. 1 (August 1998): 69–79. http://dx.doi.org/10.1006/jmbi.1998.1917.

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12

Casjens, Sherwood, Wai Mun Huang, Melody Hayden, and Ryan Parr. "Initiation of bacteriophage P22 DNA packaging series." Journal of Molecular Biology 194, no. 3 (April 1987): 411–22. http://dx.doi.org/10.1016/0022-2836(87)90671-1.

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13

Zinno, Paola, Chiara Devirgiliis, Danilo Ercolini, Duncan Ongeng, and Gianluigi Mauriello. "Bacteriophage P22 to challenge Salmonella in foods." International Journal of Food Microbiology 191 (November 2014): 69–74. http://dx.doi.org/10.1016/j.ijfoodmicro.2014.08.037.

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14

Rennell, D., and A. R. Poteete. "Genetic analysis of bacteriophage P22 lysozyme structure." Genetics 123, no. 3 (November 1, 1989): 431–40. http://dx.doi.org/10.1093/genetics/123.3.431.

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Abstract The suppression patterns of 11 phage P22 mutants bearing different amber mutations in the gene encoding lysozyme (19) were determined on six different amber suppressor strains. Of the 60 resulting single amino acid substitutions, 18 resulted in defects in lysozyme activity at 30 degrees; an additional seven were defective at 40 degrees. Revertants were isolated on the "missuppressing" hosts following UV mutagenesis; they were screened to distinguish primary- from second-site revertants. It was found that second-site revertants were recovered with greater efficiency if the UV-irradiated phage stocks were passaged through an intermediate host in liquid culture rather than plated directly on the nonpermissive host. Eleven second-site revertants (isolated as suppressors of five deleterious substitutions) were sequenced: four were intragenic, five extragenic; three of the extragenic revertants were found to have alterations near and upstream from gene 19, in gene 13. Lysozyme genes from the intragenic revertant phages were introduced into unmutagenized P22, and found to confer the revertant plating phenotype.

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15

Poteete, Anthony R., Kathleen Hehir, and Robert T. Sauer. "Bacteriophage P22 Cro protein: sequence, purification, and properties." Biochemistry 25, no. 1 (January 14, 1986): 251–56. http://dx.doi.org/10.1021/bi00349a035.

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16

Prevelige, Peter E., Dennis Thomas, Kelly L. Aubrey, Stacy A. Towse, and George J. Thomas. "Subunit conformational changes accompanying bacteriophage P22 capsid maturation." Biochemistry 32, no. 2 (January 19, 1993): 537–43. http://dx.doi.org/10.1021/bi00053a019.

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17

Wyckoff, E., and S. Casjens. "Autoregulation of the bacteriophage P22 scaffolding protein gene." Journal of Virology 53, no. 1 (1985): 192–97. http://dx.doi.org/10.1128/jvi.53.1.192-197.1985.

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18

Parker, Matthew H., Walter F. Stafford, and Peter E. Prevelige. "Bacteriophage P22 scaffolding protein forms oligomers in solution." Journal of Molecular Biology 268, no. 3 (May 1997): 655–65. http://dx.doi.org/10.1006/jmbi.1997.0995.

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19

Semerjian, Arlene V., Diane C. Malloy, and Anthony R. Poteete. "Genetic structure of the bacteriophage P22 PL operon." Journal of Molecular Biology 207, no. 1 (May 1989): 1–13. http://dx.doi.org/10.1016/0022-2836(89)90437-3.

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20

Gilcrease, Eddie B., Danella A. Winn-Stapley, F. Curtis Hewitt, Lisa Joss, and Sherwood R. Casjens. "Nucleotide Sequence of the Head Assembly Gene Cluster of Bacteriophage L and Decoration Protein Characterization." Journal of Bacteriology 187, no. 6 (March 15, 2005): 2050–57. http://dx.doi.org/10.1128/jb.187.6.2050-2057.2005.

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ABSTRACT The temperate Salmonella enterica bacteriophage L is a close relative of the very well studied bacteriophage P22. In this study we show that the L procapsid assembly and DNA packaging genes, which encode terminase, portal, scaffold, and coat proteins, are extremely close relatives of the homologous P22 genes (96.3 to 99.1% identity in encoded amino acid sequence). However, we also identify an L gene, dec, which is not present in the P22 genome and which encodes a protein (Dec) that is present on the surface of L virions in about 150 to 180 molecules/virion. We also show that the Dec protein is a trimer in solution and that it binds to P22 virions in numbers similar to those for L virions. Its binding dramatically stabilizes P22 virions against disruption by a magnesium ion chelating agent. Dec protein binds to P22 coat protein shells that have expanded naturally in vivo or by sodium dodecyl sulfate treatment in vitro but does not bind to unexpanded procapsid shells. Finally, analysis of phage L restriction site locations and a number of patches of nucleotide sequence suggest that phages ST64T and L are extremely close relatives, perhaps the two closest relatives that have been independently isolated to date among the lambdoid phages.

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21

Wang, Jigang, Ti Fang, Ming Li, Wenjing Zhang, Zhi-Ping Zhang, Xian-En Zhang, and Feng Li. "Intracellular delivery of peptide drugs using viral nanoparticles of bacteriophage P22: covalent loading and cleavable release." Journal of Materials Chemistry B 6, no. 22 (2018): 3716–26. http://dx.doi.org/10.1039/c8tb00186c.

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22

Cocozaki, Alexis I., Ingrid R. Ghattas, and Colin A. Smith. "Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of λ." Journal of Bacteriology 190, no. 12 (April 18, 2008): 4263–71. http://dx.doi.org/10.1128/jb.00059-08.

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ABSTRACT Transcription antitermination in phages λ and P22 uses N proteins that bind to similar boxB RNA hairpins in regulated transcripts. In contrast to the λ N-boxB interaction, the P22 N-boxB interaction has not been extensively studied. A nuclear magnetic resonance structure of the P22 N peptide boxBleft complex and limited mutagenesis have been reported but do not reveal a consensus sequence for boxB. We have used a plasmid-based antitermination system to screen boxBs with random loops and to test boxB mutants. We find that P22 N requires boxB to have a GNRA-like loop with no simple requirements on the remaining sequences in the loop or stem. U:A or A:U base pairs are strongly preferred adjacent to the loop and appear to modulate N binding in cooperation with the loop and distal stem. A few GNRA-like hexaloops have moderate activity. Some boxB mutants bind P22 and λ N, indicating that the requirements imposed on boxB by P22 N overlap those imposed by λ N. Point mutations can dramatically alter boxB specificity between P22 and λ N. A boxB specific for P22 N can be mutated to λ N specificity by a series of single mutations via a bifunctional intermediate, as predicted by neutral theories of evolution.

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23

Sharma, Jhanvi, Masaki Uchida, Heini M. Miettinen, and Trevor Douglas. "Modular interior loading and exterior decoration of a virus-like particle." Nanoscale 9, no. 29 (2017): 10420–30. http://dx.doi.org/10.1039/c7nr03018e.

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24

Cho, Eun Hee, Chan-Eun Nam, Renato Alcaraz, and Jeffrey F. Gardner. "Site-Specific Recombination of Bacteriophage P22 Does Not Require Integration Host Factor." Journal of Bacteriology 181, no. 14 (July 15, 1999): 4245–49. http://dx.doi.org/10.1128/jb.181.14.4245-4249.1999.

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ABSTRACT Site-specific recombination by phages λ and P22 is carried out by multiprotein-DNA complexes. Integration host factor (IHF) facilitates λ site-specific recombination by inducing DNA bends necessary to form an active recombinogenic complex. Mutants lacking IHF are over 1,000-fold less proficient in supporting λ site-specific recombination than wild-type cells. Although the attPregion of P22 contains strong IHF binding sites, in vivo measurements of integration and excision frequencies showed that infecting P22 phages can perform site-specific recombination to its maximum efficiency in the absence of IHF. In addition, a plasmid integration assay showed that integrative recombination occurs equally well in wild-type and ihfA mutant cells. P22 integrative recombination is also efficient in Escherichia coli in the absence of functional IHF. These results suggest that nucleoprotein structures proficient for recombination can form in the absence of IHF or that another factor(s) can substitute for IHF in the formation of complexes.

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25

Mann, Brandon A., and James M. Slauch. "Transduction of Low-Copy Number Plasmids by Bacteriophage P22." Genetics 146, no. 2 (June 1, 1997): 447–56. http://dx.doi.org/10.1093/genetics/146.2.447.

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The generalized transducing bacteriophage of Salmonella typhimurium, P22, can transduce plasmids in addition to chromosomal markers. Previous studies have concentrated on transduction of pBR322 by P22 and P22HT, the high transducing mutant of P22. This study investigates the mechanism of P22HT transduction of low-copy number plasmids, namely pSC101 derivatives. We show that P22HT transduces pSC101 derivatives that share homology with the chromosome by two distinct mechanisms. In the first mechanism, the plasmid integrates into the chromosome of the donor by homologous recombination. This chromosomal fragment is then packaged in the transducing particle. The second mechanism is a size-dependent mechanism involving a putative plasmid multimer. We propose that this multimer is formed by interplasmidic recombination. In contrast, P22HT can efficiently transduce pBR322 by a third mechanism, which is independent of plasmid homology with the chromosome. It has been proposed that the phage packages a linear concatemer created during rolling circle replication of pBR322, similar in fashion to phage genome packaging. This study investigates the role of RecA, RecD, and RecF recombination proteins in plasmid/plasmid and plasmid/chromosome interactions that form packageable substrates in the donor. We also examine the resolution of various transduced plasmid species in the recipient and the roles of RecA and RecD in these processes.

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26

Cingolani, Gino, Sean D. Moore, Peter E. Prevelige, and John E. Johnson. "Preliminary crystallographic analysis of the bacteriophage P22 portal protein." Journal of Structural Biology 139, no. 1 (July 2002): 46–54. http://dx.doi.org/10.1016/s1047-8477(02)00512-9.

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27

Casjens, S., and M. B. Adams. "Posttranscriptional modulation of bacteriophage P22 scaffolding protein gene expression." Journal of Virology 53, no. 1 (1985): 185–91. http://dx.doi.org/10.1128/jvi.53.1.185-191.1985.

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28

Riggs, P. D., and D. Botstein. "Bacteriophage P22 gene 23 product acts preferentially in cis." Journal of Virology 61, no. 7 (1987): 2316–18. http://dx.doi.org/10.1128/jvi.61.7.2316-2318.1987.

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29

Carbonell, X., and A. Villaverde. "Insertional Mutagenesis in the Tailspike Protein of Bacteriophage P22." Biochemical and Biophysical Research Communications 244, no. 2 (March 1998): 428–33. http://dx.doi.org/10.1006/bbrc.1998.8285.

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30

Tang, Liang, William R. Marion, Gino Cingolani, Peter E. Prevelige, and John E. Johnson. "Three-dimensional structure of the bacteriophage P22 tail machine." EMBO Journal 24, no. 12 (June 2, 2005): 2087–95. http://dx.doi.org/10.1038/sj.emboj.7600695.

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31

Weigele, Peter R., Laura Sampson, Danella Winn-Stapley, and Sherwood R. Casjens. "Molecular Genetics of Bacteriophage P22 Scaffolding Protein's Functional Domains." Journal of Molecular Biology 348, no. 4 (May 2005): 831–44. http://dx.doi.org/10.1016/j.jmb.2005.03.004.

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32

Carbonell, X., and A. Villaverde. "Peptide display on functional tailspike protein of bacteriophage P22." Gene 176, no. 1-2 (October 1996): 225–29. http://dx.doi.org/10.1016/0378-1119(96)00255-7.

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33

Casjens, Sherwood, and Melody Hayden. "Analysis in vivo of the bacteriophage P22 headful nuclease." Journal of Molecular Biology 199, no. 3 (February 1988): 467–74. http://dx.doi.org/10.1016/0022-2836(88)90618-3.

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34

Thuman-Commike, Pamela A., Barrie Greene, Joanita Jakana, Amy McGough, Peter E. Prevelige, and Wah Chiu. "Identification of Additional Coat-Scaffolding Interactions in a Bacteriophage P22 Mutant Defective in Maturation." Journal of Virology 74, no. 8 (April 15, 2000): 3871–73. http://dx.doi.org/10.1128/jvi.74.8.3871-3873.2000.

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ABSTRACT Scaffolding proteins play a critical role in the assembly of certain viruses by directing the formation and maturation of a precursor capsid. Using electron cryomicroscopy difference mapping, we have identified an altered arrangement of a mutant scaffolding within the bacteriophage P22 procapsid. This mutant scaffolding allows us to directly visualize scaffolding density within the P22 procapsid. Based on these observations we propose a model for why the mutant prevents scaffolding release and capsid maturation.

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35

Bloch, Sylwia, Bożena Nejman-Faleńczyk, Gracja Topka, Aleksandra Dydecka, Katarzyna Licznerska, Magdalena Narajczyk, Agnieszka Necel, Alicja Węgrzyn, and Grzegorz Węgrzyn. "UV-Sensitivity of Shiga Toxin-Converting Bacteriophage Virions Φ24B, 933W, P22, P27 and P32." Toxins 7, no. 9 (September 21, 2015): 3727–39. http://dx.doi.org/10.3390/toxins7093727.

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36

Rydman, Pia S., and Dennis H. Bamford. "The Lytic Enzyme of Bacteriophage PRD1 Is Associated with the Viral Membrane." Journal of Bacteriology 184, no. 1 (January 1, 2002): 104–10. http://dx.doi.org/10.1128/jb.184.1.104-110.2002.

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ABSTRACT Bacteriophage PRD1 encodes two proteins (P7 and P15) that are associated with a muralytic activity. Protein P15 is a soluble β-1,4-N-acetylmuramidase that causes phage-induced host cell lysis. We demonstrate here that P15 is also a structural component of the PRD1 virion and that it is connected to the phage membrane. Small viral membrane proteins P20 and P22 modulate incorporation of P15 into the virion and may connect it to the phage membrane. The principal muralytic protein involved in PRD1 DNA entry seems to be the putative lytic transglycosylase protein P7, as the absence of protein P15 did not delay initiation of phage DNA replication in the virus-host system used. The incorporation of two different lytic enzymes into virions may reflect the broad host range of bacteriophage PRD1.

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37

Cocozaki, Alexis I., Ingrid R. Ghattas, and Colin A. Smith. "The RNA-Binding Domain of Bacteriophage P22 N Protein Is Highly Mutable, and a Single Mutation Relaxes Specificity toward λ." Journal of Bacteriology 190, no. 23 (September 26, 2008): 7699–708. http://dx.doi.org/10.1128/jb.00997-08.

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ABSTRACT Antitermination in bacteriophage P22, a lambdoid phage, uses the arginine-rich domain of the N protein to recognize boxB RNAs in the nut site of two regulated transcripts. Using an antitermination reporter system, we screened libraries in which each nonconserved residue in the RNA-binding domain of P22 N was randomized. Mutants were assayed for the ability to complement N-deficient virus and for antitermination with P22 boxBleft and boxBright reporters. Single amino acid substitutions complementing P22 N− virus were found at 12 of the 13 positions examined. We found evidence for defined structural roles for seven nonconserved residues, which was generally compatible with the nuclear magnetic resonance model. Interestingly, a histidine can be replaced by any other aromatic residue, although no planar partner is obvious. Few single substitutions showed bias between boxBleft and boxBright, suggesting that the two RNAs impose similar constraints on genetic drift. A separate library comprising only hybrids of the RNA-binding domains of P22, λ, and φ21 N proteins produced mutants that displayed bias. P22 N− plaque size plotted against boxBleft and boxBright reporter activities suggests that lytic viral fitness depends on balanced antitermination. A few N proteins were able to complement both λ N- and P22 N-deficient viruses, but no proteins were found to complement both P22 N- and φ21 N-deficient viruses. A single tryptophan substitution allowed P22 N to complement both P22 and λ N−. The existence of relaxed-specificity mutants suggests that conformational plasticity provides evolutionary transitions between distinct modes of RNA-protein recognition.

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38

Zaworski, Julie, Colleen McClung, Cristian Ruse, Peter R. Weigele, Roger W. Hendrix, Ching-Chung Ko, Robert Edgar, Graham F. Hatfull, Sherwood R. Casjens, and Elisabeth A. Raleigh. "Genome analysis of Salmonella enterica serovar Typhimurium bacteriophage L, indicator for StySA (StyLT2III) restriction-modification system action." G3 Genes|Genomes|Genetics 11, no. 1 (December 22, 2020): 1–10. http://dx.doi.org/10.1093/g3journal/jkaa037.

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Abstract Bacteriophage L, a P22-like phage of Salmonella enterica sv Typhimurium LT2, was important for definition of mosaic organization of the lambdoid phage family and for characterization of restriction-modification systems of Salmonella. We report the complete genome sequences of bacteriophage L cI–40 13–am43 and L cII–101; the deduced sequence of wildtype L is 40,633 bp long with a 47.5% GC content. We compare this sequence with those of P22 and ST64T, and predict 72 Coding Sequences, 2 tRNA genes and 14 intergenic rho-independent transcription terminators. The overall genome organization of L agrees with earlier genetic and physical evidence; for example, no secondary immunity region (immI: ant, arc) or known genes for superinfection exclusion (sieA and sieB) are present. Proteomic analysis confirmed identification of virion proteins, along with low levels of assembly intermediates and host cell envelope proteins. The genome of L is 99.9% identical at the nucleotide level to that reported for phage ST64T, despite isolation on different continents ∼35 years apart. DNA modification by the epigenetic regulator Dam is generally incomplete. Dam modification is also selectively missing in one location, corresponding to the P22 phase-variation-sensitive promoter region of the serotype-converting gtrABC operon. The number of sites for SenLTIII (StySA) action may account for stronger restriction of L (13 sites) than of P22 (3 sites).

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Karaca, Basar, Nefise Akcelik, and Mustafa Akcelik. "Effects of P22 bacteriophage on salmonella Enterica subsp. enterica serovar Typhimurium DMC4 strain biofilm formation and eradication." Archives of Biological Sciences 67, no. 4 (2015): 1361–67. http://dx.doi.org/10.2298/abs141120114k.

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Over the last decades, several antimicrobial agents have been made available. Due to increasing antimicrobial resistance, bacteriophages were rediscovered for their potential applications against bacterial infections. In the present study, biofilm inhibition and eradication of Salmonella enterica subsp. enterica serovar Typhimurium DMC4 strain (S. Typhimurium) was evaluated with respect to different incubation periods at different P22 phage titrations. The efficacy of P22 phage on biofilm formation and eradication of S. Typhimurium DMC4 strain was screened in vitro on polystyrene and stainless steel surfaces. The biofilm forming capacity of S. Typhimurium was significantly reduced at higher phage titrations (106 pfu/mL ?). All phage titers (104-108 pfu/mL) were found to be effective at the end of the 24 h-incubation period whereas higher phage titrations were found to be effective at the end of the 48 h and 72 h of incubation. P22 phage has less efficacy on already formed, especially mature biofilms (72 h-old biofilm). Notable results of P22 phage treatment on S. Typhimurium biofilm suggest that P22 phage has potential uses in food systems.

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Tang, J., G. Lander, A. Olia, R. Li, S. Casjens, P. Prevelige, G. Cingolani, J. Johnson, and T. Baker. "P22 Bacteriophage Portal: The Conduit for DNA Packaging and Release." Microscopy and Microanalysis 17, S2 (July 2011): 100–101. http://dx.doi.org/10.1017/s1431927611001371.

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Herzog, Amanda B., Alok K. Pandey, David Reyes-Gastelum, Charles P. Gerba, Joan B. Rose, and Syed A. Hashsham. "Evaluation of Sample Recovery Efficiency for Bacteriophage P22 on Fomites." Applied and Environmental Microbiology 78, no. 22 (August 31, 2012): 7915–22. http://dx.doi.org/10.1128/aem.01370-12.

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ABSTRACTFomites are known to play a role in the transmission of pathogens. Quantitative analysis of the parameters that affect sample recovery efficiency (SRE) at the limit of detection of viruses on fomites will aid in improving quantitative microbial risk assessment (QMRA) and infection control. The variability in SRE as a function of fomite type, fomite surface area, sampling time, application media, relative humidity (rH), and wetting agent was evaluated. To quantify the SRE, bacteriophage P22 was applied onto fomites at average surface densities of 0.4 ± 0.2 and 4 ± 2 PFU/cm2. Surface areas of 100 and 1,000 cm2of nonporous fomites found in indoor environments (acrylic, galvanized steel, and laminate) were evaluated with premoistened antistatic wipes. The parameters with the most effects on the SRE were sampling time, fomite surface area, wetting agent, and rH. At time zero (the initial application of bacteriophage P22), the SRE for the 1,000-cm2fomite surface area was, on average, 40% lower than that for the 100-cm2fomite surface area. For both fomite surface areas, the application medium Trypticase soy broth (TSB) and/or the laminate fomite predominantly resulted in a higher SRE. After the applied samples dried on the fomites (20 min), the average SRE was less than 3%. A TSB wetting agent applied on the fomite improved the SRE for all samples at 20 min. In addition, an rH greater than 28% generally resulted in a higher SRE than an rH less than 28%. The parameters impacting SRE at the limit of detection have the potential to enhance sampling strategies and data collection for QMRA models.

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Mahan, M. J., A. Garzón, and J. Casadesús. "Host RecJ is required for growth of P22 erf bacteriophage." Journal of Bacteriology 175, no. 1 (1993): 288–90. http://dx.doi.org/10.1128/jb.175.1.288-290.1993.

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Zheng, H., G. Wisedchaisri, and T. Gonen. "Single Particle Electron Cryomicroscopy of Bacteriophage P22 Portal Protein Complexes." Microscopy and Microanalysis 14, S2 (August 2008): 1572–73. http://dx.doi.org/10.1017/s1431927608088661.

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Ho, Y. S., D. Pfarr, J. Strickler, and M. Rosenberg. "Characterization of the transcription activator protein C1 of bacteriophage P22." Journal of Biological Chemistry 267, no. 20 (July 1992): 14388–97. http://dx.doi.org/10.1016/s0021-9258(19)49724-x.

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Roy, Ankoor, Anshul Bhardwaj, and Gino Cingolani. "Crystallization of the nonameric small terminase subunit of bacteriophage P22." Acta Crystallographica Section F Structural Biology and Crystallization Communications 67, no. 1 (December 23, 2010): 104–10. http://dx.doi.org/10.1107/s174430911004697x.

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Wang, Chunyan, Jiagang Tu, Bo Hu, Ian Molineux, and Jun Liu. "Visualizing Infection Initiation of Bacteriophage P22 by Cryo-Electron Tomography." Biophysical Journal 112, no. 3 (February 2017): 314a. http://dx.doi.org/10.1016/j.bpj.2016.11.1704.

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Vershon, Andrew K., Sha-Mei Liao, William R. McClure, and Robert T. Sauer. "Interaction of the bacteriophage P22 arc repressor with operator DNA." Journal of Molecular Biology 195, no. 2 (May 1987): 323–31. http://dx.doi.org/10.1016/0022-2836(87)90653-x.

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Garzón, A., D. A. Cano, and J. Casadesús. "Role of Erf recombinase in P22-mediated plasmid transduction." Genetics 140, no. 2 (June 1, 1995): 427–34. http://dx.doi.org/10.1093/genetics/140.2.427.

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Abstract In the absence of host RecA function, plasmid transduction by bacteriophage P22 can be mediated by Erf recombinase. Erf is not carried on the infecting particle but synthesized upon infection. In the recipient cell, Erf can promote both generalized plasmid transduction (which requires the circularization of plasmids transduced as linear multimers) and specialized plasmid transduction (which requires the release of plasmid DNA from linear plasmid-phage cointegrates). Both processes of Erf-mediated plasmid transduction require host RecBCD function. In contrast, RecBCD is not required for Erf-mediated circularization of P22 DNA.

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Díaz-Barriga, Cristina, Francisca Villanueva-Flores, Katrin Quester, Andrés Zárate-Romero, Ruben Dario Cadena-Nava, and Alejandro Huerta-Saquero. "Asparaginase-Phage P22 Nanoreactors: Toward a Biobetter Development for Acute Lymphoblastic Leukemia Treatment." Pharmaceutics 13, no. 5 (April 22, 2021): 604. http://dx.doi.org/10.3390/pharmaceutics13050604.

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Asparaginase (ASNase) is a biopharmaceutical for Acute Lymphoblastic Leukemia (ALL) treatment. However, it shows undesirable side effects such as short lifetimes, susceptibility to proteases, and immunogenicity. Here, ASNase encapsidation was genetically directed in bacteriophage P22-based virus-like particles (VLPs) (ASNase-P22 nanoreactors) as a strategy to overcome these challenges. ASNase-P22 was composed of 58.4 ± 7.9% of coat protein and 41.6 ± 8.1% of tetrameric ASNase. Km and Kcat values of ASNase-P22 were 15- and 2-fold higher than those obtained for the free enzyme, respectively. Resulting Kcat/Km value was 2.19 × 105 M−1 s−1. ASNase-P22 showed an aggregation of 60% of the volume sample when incubated at 37 °C for 12 days. In comparison, commercial asparaginase was completely aggregated under the same conditions. ASNase-P22 was stable for up to 24 h at 37 °C, independent of the presence of human blood serum (HBS) or whether ASNase-P22 nanoreactors were uncoated or PEGylated. Finally, we found that ASNase-P22 caused cytotoxicity in the leukemic cell line MOLT-4 in a concentration dependent manner. To our knowledge, this is the first work where ASNase is encapsulated inside of VLPs, as a promising alternative to fight ALL.

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Murphy, Kenan C., Anita C. Fenton, and Anthony R. Poteete. "Sequence of the bacteriophage P22 Anti-RecBCD (abc) genes and properties of P22 abc region deletion mutants." Virology 160, no. 2 (October 1987): 456–64. http://dx.doi.org/10.1016/0042-6822(87)90017-1.

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