Relevant bibliographies by topics / Bacteriophage P22

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Bacteriophage P22'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Bacteriophage P22"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Bacteriophage P22"

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Marion, William R. "Bacteriophage P22 scaffolding protein functions and mechanisms in procapsid assembly /." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2009r/marion.pdf.

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Keifer, David Z. "Charge detection mass spectrometry| Improved charge precision and applications to bacteriophage P22." Thesis, Indiana University, 2016. http://pqdtopen.proquest.com/#viewpdf?dispub=10129671.

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Electrospray ionization (ESI) is a premier method for volatilizing and ionizing biological analytes for mass spectrometry. In conventional mass spectrometry (MS), the spectrum of mass-to-charge ratio (m/z) for an ensemble of ions is measured. ESI produces a distribution of charges for each ionized species, and the mass of each species is determined by assigning a charge state to each peak in the m/z spectrum. These peaks are difficult to resolve for species above the 100-kDa range because of peak broadening and shifting due to salt adducts, incomplete desolvation, and intrinsic heterogeneity. Without resolved charge states, the mass cannot be determined. Charge detection mass spectrometry (CDMS) offers a solution to this problem.

In CDMS, both the m/z and the charge are measured simultaneously for individual ions. Multiplying those measurements for each ion yields the mass. Thus, there is no need for charge state resolution in an m/z spectrum. CDMS can therefore be used to measure the masses of extremely heavy and heterogeneous analytes far beyond the capabilities of conventional MS. This comes at the cost of efficiency, since single ions are measured serially, and resolution, since the charge measurement historically has been imprecise in CDMS.

Here we report a nearly perfect charge measurement in CDMS by analyzing each ion for 3 s in an electrostatic ion trap and implementing a novel analysis method. Then we discuss spontaneous mass and charge losses of trapped ions. Finally, we discuss multiple applications of CDMS to bacteriophage P22. P22 capsids assemble into T = 7 ‘procapsids’ with the assistance of a distribution of scaffolding proteins; we report the typical width of that distribution. Next we report our observation of mass loss in P22 procapsids over the course of weeks due to precipitation of scaffolding proteins. Then we discuss how the charge on electrosprayed P22 capsids allows us to distinguish morphologies of P22 capsids. Finally, we report an accurate mass measurement of the infectious P22 phage, a >50 MDa particle containing nucleic acid and nine kinds of protein.

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Ranade, Koustubh. "sieB and esc genes of Bacteriophage P22: A Dissertation." eScholarship@UMMS, 1993. https://escholarship.umassmed.edu/gsbs_diss/59.

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The superinfection exclusion gene (sieB) of Salmonella phage P22 was mapped using phage deletion mutants. The DNA sequence in the region was re-examined in order to find an open reading frame consistent with the deletion mapping. Several discrepancies from the previously published sequence were discovered. The revised sequence revealed a single open reading frame of 242 codons with six likely translation initiation codons. On the basis of deletion and amber mutant phenotypes the second of these six sites was inferred to be the translation initiation site of the sieB gene. The sieB gene encodes a polypeptide with 192 amino acid residues with a calculated molecular weight of 22,442, which is in reasonable agreement with that estimated from polyacrylamide gels. The transcription start-site of sieB was identified by the use of an RNAase protection assay. The sieB promoter thus identified was inactivated by a two-base substitution in its -10 hexamer. The sieB gene of coliphage λ was also identified. The promoter for λ sieB was identified by homology to that of P22 sieB. sieB aborts the lytic development of some phages. P22 itself is insensitive to the lethal effect of SieB because it harbours a determinant called esc. It was found that the sieB gene encodes two polypeptides-SieB, which is the exclusion protein, and Esc, which is a truncated version of SieB that inhibits its action. Superinfecting P22 synthesizes an antisense RNA, sas, that inhibits synthesis of SieB but allows continued synthesis of Esc, thus allowing P22 to by-pass SieB-mediated exclusion. This translational switch induced by sas RNA is essential to vegetatively developing P22; a mutation that prevents this switch causes P22 to commit SieB-mediated suicide. It was also found that P22's Esc allows it to circumvent the SieB-mediated exclusion system of bacteriophage λ.
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Semerjian, Arlene. "Genetic Structure of the Bacteriophage P22 PL Operon: A Thesis." eScholarship@UMMS, 1989. http://escholarship.umassmed.edu/gsbs_diss/316.

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The sequence of 1360 base pairs of the P22 PL operon was determined, linking a continuous sequence from PL through abc2. P22 mutants bearing deletions in the sequenced region were constructed and tested for their phenotypes. Plasmids were constructed to express PL operon genes singly and in combinations from PlacUV5. Two previously known genes, 17 and c3, are located within this sequence. In addition, three new genes have been identified: ral, kil and arf. Genes ral and c3 are homologous, as well as functionally analogous, to λ ral and cIII, respectively. P22 kil, like λ kil, kills the host cell when it is expressed. The two kil genes, although analogous in cell killing and map location, have no apparent sequence homology. The functions of the P22 and λ kil genes are unknown; however, P22 kil is essential for lytic growth in the absence of abc. Gene arf (accessory recombination function) is located just upstream of erf; it is essential for P22 growth in the absence of kil or other genes upstream in PL. The growth defect of P22 bearing a deletion that removes arf is complemented by expression of either arf or the λ red genes from plasmids. P22 sequences that include the stop codon for 17 potentially form a small stem-loop structure; these sequences are nearly identical to λ sequences that contain the stop codon for ssb. In λ this potential stem-loop structure occupies a map position near the terminator tL2b. Plasmids that include the potential P22 structure negatively regulate kil gene expression in cis.
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Ramírez, Vázquez Maria Ester. "Analysis of the bacteriophage P22 viral spread within bacterial populations and its characterization as immunobiosensor." Doctoral thesis, Universitat Autònoma de Barcelona, 2015. http://hdl.handle.net/10803/382638.

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Aquest treball estudia la dinàmica poblacional de fags P22 en poblacions d'hostes que envelleixen, com a model de la resposta vírica a situacions d'estrès de l'hoste. Per tal d'analitzar les respostes adaptatives del virus a l'envelliment i conseqüent pèrdua d'eficiència replicativa de les cèl·lules hoste, hem estudiat la propagació vírica en poblacions hoste aïllades, utilitzant com a model un bacteriòfag mutant que no integra el seu DNA al cromosoma del bacteri. Els resultats mostren una asimetria a l'aparició de la transmissió horitzontal i vertical. Durant el creixement exponencial, els cicles lítics son fortament reprimits i quan la taxa de creixement de la població hoste disminueix, les funcions lítiques són expressades en colònies independents. La asimetria observada a l'aparició de les estratègies de transmissió sembla mantenir la viabilitat de les cèl·lules infectades quan creixen exponencialment, però promou la producció vírica i eficient propagació horitzontal quan entren en fase estacionaria. L'anàlisi de la dinàmica d'inducció del profag en hostes RecA- van mostrar una amplificació de P22 no sincrònica en colònies independents, indicant que la sobtada amplificació vírica durant l'entrada en fase estacionaria en colònies separades és depenent de la proteïna funcional RecA. Els resultats també van mostrar que el temps anterior a l'amplificació vírica i tota la dinàmica de propagació vírica està influenciada per la història de la colònia infectada de la que deriva la cèl·lula fundadora. D'una altra banda, amb l'objectiu de desenvolupar nous components de vacunes, una de les línies de recerca del Laboratori de Nanobiotecnologia del Prof. Villaverde era el disseny i producció de proteïnes recombinants multifuncionals, en especial de β-galactosidasa i TSP, per trobar llocs permissius a on inserir pèptids amb activitat biològica, tal com el lloc A del FMDV. Villaverde, A. i col·laboradors van mostrar que la β-galactosidasa recombinant M278VP1 és sensible a la modulació enzimàtica per unió a anticòs, lo qual podria representar una nova aplicació potencial de β-galactosidases quimèriques com a sensors moleculars per la detecció d'anticossos. En aquest treball hem analitzat el mecanisme de reactivació de la β-galactosidasa recombinant M278VP1. També Carbonell, X. i Villaverde, A. van mostrar que l'extrem carboxi terminal de TSP és permissiu a llargues insercions peptídiques, resultant en proteïnes quimèriques biològicament actives (TSPA), no tòxiques, capaces d'acoblar-se amb càpsids de P22 sense cua i promoure la infecció de cèl·lules hoste de Salmonella. En aquest treball hem explorat l'efecte de diferents anticossos i els seus respectius fragments Fab anti-lloc A en la infectivitat de partícules de P22 quimèriques acoblades in vitro a partir de càpsids de P22 sense cua amb TSPA recombinant. L'increment observat de la infectivitat vírica indica que els bacteriòfags presentadors de pèptids poden actuar com a biosensors moleculars que responen a interaccions moleculars específiques.
This work studies the phage P22 spread dynamics in ageing bacterial populations, as a model of the viral response to host stress situations. In order to analyze the adaptative responses of the virus to the ageing, and consequent loss of replicative fitness of the host cells, we have explored the viral spread within isolated host populations, by using as a model a mutant bacteriophage unable to integrate its prophage DNA into the bacterial chromosome. The results show an asymmetry in the occurrence of horizontal and vertical transmission. During the exponential cell growth, lytic cycles are tightly repressed and when the growth rate of the host population decreases, lytic functions are expressed in independent colonies. The observed asymmetry in the occurrence of these transmission strategies seems to tend to maintain the viability of infected cells when exponentially growing, but promotes viral production and efficient horizontal spread when entering into the stationary phase. The analysis of prophage induction dynamics in a RecA- host showed a non-synchronous P22 amplification in independent colonies, indicating that the sudden viral burst observed during the entry into stationary phase in separated colonies is dependent on a functional RecA protein. Additionally the results showed that pre-burst time and the whole dynamics of phage spread is influenced by the history of the infected colony from which the founder cell derives. On the other hand, with the aim to develop new vaccine components, one of the research areas of the Nanobiotechnology Laboratory of Prof. Villaverde was to design and produce multifunctional recombinant proteins, specifically focusing into the β-galactosidase and TSP, to find permissive regions where to insert peptides with biological activity, such as the Site A of FMDV. Villaverde, A. et al. showed that the recombinant β-galactosidase M278VP1 is sensitive enough to enzymatic modulation mediated by antibody binding, which could represent a new potential application of chimeric β-galactosidases as molecular sensors to detect antibodies. In this work we have analyzed the reactivation mechanism of the recombinant β-galactosidase M278VP1. Additionally, Carbonell, X. and Villaverde, A. showed that the carboxy terminal end of TSP is permissive to long peptide insertions, resulting in biologically active (TSPA), non-toxic chimeric proteins able to assemble with P22 heads and to promote infection of Salmonella host cells. In this work, we have explored the effect of different antibodies and their respective Fab fragments anti-Site A on the infectivity of chimeric P22 particles assembled in vitro of tailless P22 heads with recombinant TSPA. The observed increase of the infective titre indicates that peptide-displaying bacteriophages can act as molecular biosensors that are responsive to specific molecular interactions.
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Conlin, Christopher Arthur. "Characterization of the Salmonella typhimuriumopdA gene, encoding oligopeptidase A: Nucleotide sequence; identity with the Escherichia coliprlC gene; and its role in bacteriophage P22 development." Case Western Reserve University School of Graduate Studies / OhioLINK, 1992. http://rave.ohiolink.edu/etdc/view?acc_num=case1055962404.

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McMahan, Linda. "Tn1 Insertions in the 3' Untranslated Region of the ant Operon of Bacteriophage P22 Affect ant Gene Expression and Alter ant mRNA Stability: a Thesis." eScholarship@UMMS, 1985. http://escholarship.umassmed.edu/gsbs_diss/249.

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Insertion of transposable elements within an operon has been known not only to abolish expression of the gene interrupted by the insertion, but also to exert a strong polar effect on the expression of downstream genes in the same operon. In this dissertation, I have shown that insertions of the transposable ampicillin-resistance element Tn1, either in the polar or nonpolar orientation, in the 3' untranslated region of the bacteriophage P22 antirepressor (ant) operon reduce the rate of upstream ant gene expression; insertions of Tn1 in the nonpolar orientation reduce the rate of ant gene expression more significantly than those in the polar orientation. This effect appears to be due to reduced stability of ant mRNA. Tn1 deletion mutants of one of the nonpolar Tn1 insertion mutations have been isolated. Two classes of Tn1 deletions are obtained. Class I retains a 68 bp Tn1 sequence that shows a potential 14 bp stem and 37 bp loop conformation, while class II retains 147 bp Tn1 sequence that shows a potential 69 bp stem and 6 bp loop conformation. These two classes of Tn1 deletions do not delete any P22 sequences. Class I but not class II Tn1 deletion mutants restore the rate of ant gene expression and ant mRNA stability. Six different Ant+ revertants of the class II Tn1 deletion mutant simultaneously restore the rate of ant gene expression and ant mRNA stability. They all have deletions that remove all or part of the class II Tn1 sequence. In one case, the Tn1 sequence retained shows a potential 15 bp stem and 8 bp loop conformation, in the other cases, no secondary structure is predicted to form. The results of the Tn1 deletion mutants suggest that the stem-and-loop structures and the length of stems potentially formed by the Tn1 sequences in mRNA may affect its stability.
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Mattis, Aras Nikodemas. "The P22 Xis protein : regulation of bacteriophage P22 site-specific recombination /." 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3290313.

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Thesis (Ph. D.)--University of Illinois at Urbana-Champaign, 2007.
Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7321. Adviser: Richard I. Gumport. Includes bibliographical references. Available on microfilm from Pro Quest Information and Learning.
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Dutt, Sarang. "Use of surfaces functionalized with phage tailspike proteins to capture and detect bacteria in biosensors and bioassays." Master's thesis, 2010. http://hdl.handle.net/10048/1186.

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The food safety and human diagnostics markets are in need of faster working, reliable, sensitive, specific, low cost bioassays and biosensors for bacterial detection. This thesis reports the use of P22 bacteriophage tailspike proteins (TSP) immobilized on silanized silicon surfaces, roughened at a nano-scale, for specific capture and detection of Salmonella. Towards developing TSP biosensors, TSP immobilization characteristics were studied, and methods to improve bacterial capture were explored. Atomic force microscopy was used to count TSP immobilized on gold thin-films. Surface density counts are dependent on the immobilization scheme used. TSP immobilized on flat silicon (Si), silanized with 3-aminopropyltriethoxysilane and activated with glutaraldehyde, showed half the bacterial capture of gold thin-films. To improve bacterial capture, roughened mountain-shaped ridge-covered silicon (MSRCS) surfaces were coated with TSP and tested. Measurements of their bacterial surface density show that such MSRCS surfaces can produce bacterial capture close to or better than TSP-coated gold thin-films.
Biomedical Engineering
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Book chapters on the topic "Bacteriophage P22"

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Poteete, Anthony R. "Bacteriophage P22." In The Bacteriophages, 647–82. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5490-1_11.

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Lawes, Matthew, and Stanley R. Maloy. "Use of Bacteriophage Mu-P22 Hybrids for Genome Mapping." In Bacterial Genomes, 337–47. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-6369-3_27.

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Patterson, Dustin P. "Encapsulation of Active Enzymes within Bacteriophage P22 Virus-Like Particles." In Methods in Molecular Biology, 11–24. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7893-9_2.

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Becka, Renee, Stacy A. Towse, and George J. Thomas. "Protein conformation and stability in relation to virus assembly: Investigation of bacteriophage P22 structural proteins by Raman spectroscopy." In Proteins, 138–44. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_20.

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Stafford, Walter F., Sen Liu, and Peter E. Prevelige. "New high sensitivity sedimentation methods: Application to the analysis of the assembly of bacteriophage P22." In Techniques in Protein Chemistry, 427–32. Elsevier, 1995. http://dx.doi.org/10.1016/s1080-8914(06)80052-9.

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Silva, Jerson L., and Andrea T. Da Poian. "Pressure and Cold Denaturation of Proteins, Protein-DNA Complexes, and Viruses." In High Pressure Effects in Molecular Biophysics and Enzymology. Oxford University Press, 1996. http://dx.doi.org/10.1093/oso/9780195097221.003.0013.

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The application of hydrostatic pressure provides a means of appraising interprotein and intraprotein interactions isothermally and makes it possible to sample partially folded conformations. A number of proteins exhibit cold denaturation and cold dissociation. We have used the combined effects of pressure and low temperature to promote dissociation or denaturation of single-chain proteins, oligomers, protein-DNA complexes, and viruses. In this article, we summarize results that have biological relevance. The dissociation and denaturation of the hexameric protein, allophycocyanin, are accomplished only when the temperature is decreased to —10 °C, indicating the entropic character of the folding and association reaction. The folding and dimerization of Arc repressor in the temperature range of 0—20 °C is also favored by a large positive entropy that counteracts an unfavorable positive enthalpy. On binding operator DNA, Arc repressor becomes extremely stable against denaturation. However, the Arc repressor-operator DNA complex is cold denatured at subzero temperatures under pressure. The entropy increases greatly when Arc repressor binds tightly to its operator sequence but not to a nonspecific sequence. The dissociation and denaturation of icosahedral viruses by pressure and low temperature also have been studied. The procapsid shells of bacteriophage P22 only dissociate by pressure at temperatures below 0 °C. On the other hand, the monomeric coat protein is very unstable toward pressure. Cowpea mosaic virus (CPMV) dissociates only in the presence of 1.0 M urea, at 2.5 kbar when the temperature is decreased to — 15°C. At temperatures close to — 20 °C, partial denaturation is obtained even in the absence of urea. The assembly of CPMV is related to large and positive variations or enthalpy and entropy, making the assembly of ribonucleoprotein components an entropy-driven process. We conclude that protein folding, protein association, and protein-DNA recognition seem to need positive entropy to occur. We are facing a puzzle in which a final, apparently more ordered state is achieved, a state that paradoxically has more entropy. In the last 20 years, several studies have described the cold denaturation of proteins (Brandts, 1964; Sturtevant, 1977; Privalov et al., 1986; Griko et al., 1988; Chen & Schellman, 1989, and as reviewed in Privalov, 1990). However, unlike thermal denaturation, cold denaturation is not well understood.
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Conference papers on the topic "Bacteriophage P22"

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Lee, Junghoon, Yili Zheng, Zhye Yin, Peter C. Doerschuk, and John E. Johnson. "Classification of cryo electron microscopy images, noisy tomographic images recorded with unknown projection directions, by simultaneously estimating reconstructions and application to an assembly mutant of Cowpea Chlorotic Mottle Virus and portals of the bacteriophage P22." In SPIE Optical Engineering + Applications, edited by Philip J. Bones, Michael A. Fiddy, and Rick P. Millane. SPIE, 2010. http://dx.doi.org/10.1117/12.862066.

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