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Volumn 3, Issue 2, 2014, Pages 257-270

In silico analysis of AHJD-like viruses, Staphylococcus aureus phages S24-1 and S13', and study of phage S24-1 adsorption

Author keywords

Bacteriophage; Phage adsorption; Staphylococcus aureus; Wall teichoic acid

Indexed keywords

BINDING PROTEIN; OPEN READING FRAME 16 PROTEIN; TEICHOIC ACID; UNCLASSIFIED DRUG; SEWAGE; VIRUS DNA; VIRUS RECEPTOR;

EID: 84897990946     PISSN: None     EISSN: 20458827     Source Type: Journal    
DOI: 10.1002/mbo3.166     Document Type: Article
Times cited : (15)

References (47)
  • 1
    • 80055121440 scopus 로고    scopus 로고
    • Lysis from without
    • Abedon, S. T. 2011. Lysis from without. Bacteriophage 1:46-49.
    • (2011) Bacteriophage , vol.1 , pp. 46-49
    • Abedon, S.T.1
  • 2
    • 0038392706 scopus 로고    scopus 로고
    • Bacteriophage observations and evolution
    • Ackermann, H. W. 2003. Bacteriophage observations and evolution. Res. Microbiol. 154:245-251.
    • (2003) Res. Microbiol. , vol.154 , pp. 245-251
    • Ackermann, H.W.1
  • 3
    • 43349101058 scopus 로고    scopus 로고
    • Prokaryotic gene prediction using GeneMark and GeneMark.hmm. In Current Protocols in
    • Borodovsky, M., R. Mills, J. Besemer, and A. Lomsadze. 2003. Prokaryotic gene prediction using GeneMark and GeneMark.hmm. In Current Protocols in. Bioinformatics 4:5.
    • (2003) Bioinformatics , vol.4 , pp. 5
    • Borodovsky, M.1    Mills, R.2    Besemer, J.3    Lomsadze, A.4
  • 4
    • 84858166155 scopus 로고    scopus 로고
    • Short noncontractile tail machines: adsorption and DNA delivery by podoviruses
    • Casjens, S. R., and I. J. Molineux. 2012. Short noncontractile tail machines: adsorption and DNA delivery by podoviruses. Adv. Exp. Med. Biol. 726:143-179.
    • (2012) Adv. Exp. Med. Biol. , vol.726 , pp. 143-179
    • Casjens, S.R.1    Molineux, I.J.2
  • 5
    • 69249083586 scopus 로고    scopus 로고
    • Waves of resistance: Staphylococcus aureus in the antibiotic era
    • Chambers, H. F., and F. R. Deleo. 2009. Waves of resistance: Staphylococcus aureus in the antibiotic era. Nat. Rev. Microbiol. 7:629-641.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 629-641
    • Chambers, H.F.1    Deleo, F.R.2
  • 6
    • 22544470014 scopus 로고    scopus 로고
    • War is peace-dispatches from the bacterial and phage killing fields
    • Comeau, A. M., and H. M. Krisch. 2005. War is peace-dispatches from the bacterial and phage killing fields. Curr. Opin. Microbiol. 8:488-494.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 488-494
    • Comeau, A.M.1    Krisch, H.M.2
  • 8
    • 0033861015 scopus 로고    scopus 로고
    • Comparative survival of faecal and human contaminants and use of Staphylococcus aureus as an effective indicator of human pollution
    • Gabutti, G., A. D. Donno, F. Bagordo, and M. T. Montagna. 2000. Comparative survival of faecal and human contaminants and use of Staphylococcus aureus as an effective indicator of human pollution. Mar. Pollut. Bull. 40:697-700.
    • (2000) Mar. Pollut. Bull. , vol.40 , pp. 697-700
    • Gabutti, G.1    Donno, A.D.2    Bagordo, F.3    Montagna, M.T.4
  • 9
    • 84862771127 scopus 로고    scopus 로고
    • A multi-beach study of Staphylococcus aureus, MRSA, and enterococci in seawater and beach sand
    • Goodwin, K. D., M. McNay, Y. Cao, D. Ebentier, M. Madison, and J. F. Griffith. 2012. A multi-beach study of Staphylococcus aureus, MRSA, and enterococci in seawater and beach sand. Water Res. 46:4195-4207.
    • (2012) Water Res. , vol.46 , pp. 4195-4207
    • Goodwin, K.D.1    McNay, M.2    Cao, Y.3    Ebentier, D.4    Madison, M.5    Griffith, J.F.6
  • 11
    • 33749005403 scopus 로고    scopus 로고
    • Staphylococcus aureus mutants with increased lysostaphin resistance
    • Gründling, A., D. M. Missiakas, and O. Schneewind. 2006. Staphylococcus aureus mutants with increased lysostaphin resistance. J. Bacteriol. 188:6286-6297.
    • (2006) J. Bacteriol. , vol.188 , pp. 6286-6297
    • Gründling, A.1    Missiakas, D.M.2    Schneewind, O.3
  • 12
    • 33748206790 scopus 로고    scopus 로고
    • Emergence and resurgence of meticillin-resistant Staphylococcus aureus as a public-health threat
    • Grundmann, H., M. Aires-de-Sousa, J. Boyce, and E. Tiemersma. 2006. Emergence and resurgence of meticillin-resistant Staphylococcus aureus as a public-health threat. Lancet 368:874-885.
    • (2006) Lancet , vol.368 , pp. 874-885
    • Grundmann, H.1    Aires-de-Sousa, M.2    Boyce, J.3    Tiemersma, E.4
  • 13
    • 0013483403 scopus 로고
    • Biosynthesis of the bacterial envelope polymers teichoic acid and teichuronic acid
    • A. N. Martonosi, ed., 2nd ed. Plenum Press, New York, NY.
    • Hancock, I. C., and J. Baddiley. 1985. Biosynthesis of the bacterial envelope polymers teichoic acid and teichuronic acid. Pp. 279-307 in A. N. Martonosi, ed. The enzymes of biological membranes, 2nd ed. Plenum Press, New York, NY.
    • (1985) The enzymes of biological membranes , pp. 279-307
    • Hancock, I.C.1    Baddiley, J.2
  • 15
    • 0033514996 scopus 로고    scopus 로고
    • Evolutionary relationships among diverse bacteriophages and prophages: all the world's a phage
    • Hendrix, R. W., M. C. Smith, R. N. Burns, M. E. Ford, and G. F. Hatfull. 1999. Evolutionary relationships among diverse bacteriophages and prophages: all the world's a phage. Proc. Natl. Acad. Sci. USA 96:2192-2197.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2192-2197
    • Hendrix, R.W.1    Smith, M.C.2    Burns, R.N.3    Ford, M.E.4    Hatfull, G.F.5
  • 16
    • 84856469570 scopus 로고    scopus 로고
    • Bacteriophages and Nanostructured Materials
    • A. I. Laskin, S. Sariaslani and G. M. Gadd, eds. Elsevier, San Diego, CA.
    • Hyman, P. 2012. Bacteriophages and Nanostructured Materials. Pp. 55-73 in A. I. Laskin, S. Sariaslani and G. M. Gadd, eds. Advanced in applied microbiology. Elsevier, San Diego, CA.
    • (2012) Advanced in applied microbiology , pp. 55-73
    • Hyman, P.1
  • 17
    • 67650327619 scopus 로고    scopus 로고
    • Identification of ORF636 in phage phiSLT carrying Panton-Valentine leukocidin genes, acting as an adhesion protein for a poly(glycerophosphate) chain of lipoteichoic acid on the cell surface of Staphylococcus aureus
    • Kaneko, J., S. Narita-Yamada, Y. Wakabayashi, and Y. Kamio. 2009. Identification of ORF636 in phage phiSLT carrying Panton-Valentine leukocidin genes, acting as an adhesion protein for a poly(glycerophosphate) chain of lipoteichoic acid on the cell surface of Staphylococcus aureus. J. Bacteriol. 191:4674-4680.
    • (2009) J. Bacteriol. , vol.191 , pp. 4674-4680
    • Kaneko, J.1    Narita-Yamada, S.2    Wakabayashi, Y.3    Kamio, Y.4
  • 19
    • 62449220836 scopus 로고    scopus 로고
    • Phage host range and efficiency of plating
    • Kutter, E. 2009. Phage host range and efficiency of plating. Methods Mol. Biol. 501:141-149.
    • (2009) Methods Mol. Biol. , vol.501 , pp. 141-149
    • Kutter, E.1
  • 20
    • 17044437752 scopus 로고    scopus 로고
    • The complete genomes and proteomes of 27 Staphylococcus aureus bacteriophages
    • Kwan, T., J. Liu, M. DuBow, P. Gros, and J. Pelletier. 2005. The complete genomes and proteomes of 27 Staphylococcus aureus bacteriophages. Proc. Natl. Acad. Sci. USA 102:5174-5179.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5174-5179
    • Kwan, T.1    Liu, J.2    DuBow, M.3    Gros, P.4    Pelletier, J.5
  • 21
    • 84860389302 scopus 로고    scopus 로고
    • The next generation of bacteriophage therapy
    • Lu, T. K., and M. S. Koeris. 2011. The next generation of bacteriophage therapy. Curr. Opin. Microbiol. 14:524-531.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 524-531
    • Lu, T.K.1    Koeris, M.S.2
  • 23
    • 0036446878 scopus 로고    scopus 로고
    • Review: conformation and folding of novel beta-structural elements in viral fiber proteins: the triple beta-spiral and triple beta-helix
    • Mitraki, A., S. Miller, and M. J. van Raaij. 2002. Review: conformation and folding of novel beta-structural elements in viral fiber proteins: the triple beta-spiral and triple beta-helix. J. Struct. Biol. 137:236-247.
    • (2002) J. Struct. Biol. , vol.137 , pp. 236-247
    • Mitraki, A.1    Miller, S.2    van Raaij, M.J.3
  • 24
    • 0035808774 scopus 로고    scopus 로고
    • Structure-function relationship of cytokine induction by lipoteichoic acid from Staphylococcus aureus
    • Morath, S., A. Geyer, and T. Hartung. 2001. Structure-function relationship of cytokine induction by lipoteichoic acid from Staphylococcus aureus. J. Exp. Med. 193:393-397.
    • (2001) J. Exp. Med. , vol.193 , pp. 393-397
    • Morath, S.1    Geyer, A.2    Hartung, T.3
  • 26
    • 17644427061 scopus 로고    scopus 로고
    • Extracellular carbohydrate-containing polymers of a model biofilm-producing strain, Staphylococcus epidermidis RP62A
    • Sadovskaya, I., E. Vinogradov, S. Flahaut, G. Kogan, and S. Jabbouri. 2005. Extracellular carbohydrate-containing polymers of a model biofilm-producing strain, Staphylococcus epidermidis RP62A. Infect. Immun. 73:3007-3017.
    • (2005) Infect. Immun. , vol.73 , pp. 3007-3017
    • Sadovskaya, I.1    Vinogradov, E.2    Flahaut, S.3    Kogan, G.4    Jabbouri, S.5
  • 27
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V., S. L. Seymour, A. A. Patel, A. Loboda, W. H. Tang, S. P. Keating, et al. 2007. The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 6:1638-1655.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6
  • 28
    • 80055002173 scopus 로고    scopus 로고
    • Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe
    • Singh, A., D. Arutyunov, M. T. McDermott, C. M. Szymanski, and S. Evoy. 2011. Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe. Analyst 136:4780-4786.
    • (2011) Analyst , vol.136 , pp. 4780-4786
    • Singh, A.1    Arutyunov, D.2    McDermott, M.T.3    Szymanski, C.M.4    Evoy, S.5
  • 29
    • 84863678359 scopus 로고    scopus 로고
    • Bacteriophage based probes for pathogen detection
    • Singh, A., D. Arutyunov, C. M. Szymanski, and S. Evoy. 2012. Bacteriophage based probes for pathogen detection. Analyst 137:3405-3421.
    • (2012) Analyst , vol.137 , pp. 3405-3421
    • Singh, A.1    Arutyunov, D.2    Szymanski, C.M.3    Evoy, S.4
  • 30
    • 77952890163 scopus 로고    scopus 로고
    • Antibacterial and biofilm removal activity of a podoviridae Staphylococcus aureus bacteriophage SAP-2 and a derived recombinant cell-wall-degrading enzyme
    • Son, J. S., S. J. Lee, S. Y. Jun, S. J. Yoon, S. H. Kang, H. R. Paik, et al. 2010. Antibacterial and biofilm removal activity of a podoviridae Staphylococcus aureus bacteriophage SAP-2 and a derived recombinant cell-wall-degrading enzyme. Appl. Microbiol. Biotechnol. 86:1439-1449.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1439-1449
    • Son, J.S.1    Lee, S.J.2    Jun, S.Y.3    Yoon, S.J.4    Kang, S.H.5    Paik, H.R.6
  • 31
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer
    • Steinbacher, S., R. Seckler, S. Miller, B. Steipe, R. Huber, and P. Reinemer. 1994. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265:383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 33
    • 75649132267 scopus 로고    scopus 로고
    • Wall teichoic acid function, biosynthesis, and inhibition
    • Swoboda, J. G., J. Campbell, T. C. Meredith, and S. Walker. 2010. Wall teichoic acid function, biosynthesis, and inhibition. ChemBioChem 11:35-45.
    • (2010) ChemBioChem , vol.11 , pp. 35-45
    • Swoboda, J.G.1    Campbell, J.2    Meredith, T.C.3    Walker, S.4
  • 34
    • 84883779719 scopus 로고    scopus 로고
    • Evaluating efficacy of bacteriophage therapy against Staphylococcus aureus infections using a silkworm larval infection model
    • Takemura-Uchiyama, I., J. Uchiyama, S. I. Kato, T. Inoue, T. Ujihara, N. Ohara, et al. 2013. Evaluating efficacy of bacteriophage therapy against Staphylococcus aureus infections using a silkworm larval infection model. FEMS Microbiol. Lett. 347:52-60.
    • (2013) FEMS Microbiol. Lett. , vol.347 , pp. 52-60
    • Takemura-Uchiyama, I.1    Uchiyama, J.2    Kato, S.I.3    Inoue, T.4    Ujihara, T.5    Ohara, N.6
  • 35
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura, K., D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar. 2011. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 36
    • 67651095737 scopus 로고    scopus 로고
    • Nanomaterials: viruses electrify battery research
    • Tarascon, J. M. 2009. Nanomaterials: viruses electrify battery research. Nat. Nanotechnol. 4:341-342.
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 341-342
    • Tarascon, J.M.1
  • 37
    • 46949111817 scopus 로고    scopus 로고
    • In silico and in vivo evaluation of bacteriophage φEF24C, a candidate for treatment of Enterococcus faecalis infections
    • Uchiyama, J., M. Rashel, I. Takemura, H. Wakiguchi, and S. Matsuzaki. 2008. In silico and in vivo evaluation of bacteriophage φEF24C, a candidate for treatment of Enterococcus faecalis infections. Appl. Environ. Microbiol. 74:4149-4163.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 4149-4163
    • Uchiyama, J.1    Rashel, M.2    Takemura, I.3    Wakiguchi, H.4    Matsuzaki, S.5
  • 38
    • 80055047527 scopus 로고    scopus 로고
    • Improved adsorption of an Enterococcus faecalis bacteriophage φ{symbol}EF24C with a spontaneous point mutation
    • Uchiyama, J., I. Takemura, M. Satoh, S. Kato, T. Ujihara, K. Akechi, et al. 2011. Improved adsorption of an Enterococcus faecalis bacteriophage φ{symbol}EF24C with a spontaneous point mutation. PLoS ONE 6:e26648.
    • (2011) PLoS ONE , vol.6
    • Uchiyama, J.1    Takemura, I.2    Satoh, M.3    Kato, S.4    Ujihara, T.5    Akechi, K.6
  • 40
    • 0037469628 scopus 로고    scopus 로고
    • Complete nucleotide sequence and molecular characterization of two lytic Staphylococcus aureus phages: 44AHJD and P68
    • Vybiral, D., M. Takác, M. Loessner, A. Witte, U. von Ahsen, and U. Bläsi. 2003. Complete nucleotide sequence and molecular characterization of two lytic Staphylococcus aureus phages: 44AHJD and P68. FEMS Microbiol. Lett. 219:275-283.
    • (2003) FEMS Microbiol. Lett. , vol.219 , pp. 275-283
    • Vybiral, D.1    Takác, M.2    Loessner, M.3    Witte, A.4    von Ahsen, U.5    Bläsi, U.6
  • 41
    • 39749094420 scopus 로고    scopus 로고
    • Structure of the receptor-binding protein of bacteriophage det7: a podoviral tail spike in a myovirus
    • Walter, M., C. Fiedler, R. Grassl, M. Biebl, R. Rachel, X. L. Hermo-Parrado, et al. 2008. Structure of the receptor-binding protein of bacteriophage det7: a podoviral tail spike in a myovirus. J. Virol. 82:2265-2273.
    • (2008) J. Virol. , vol.82 , pp. 2265-2273
    • Walter, M.1    Fiedler, C.2    Grassl, R.3    Biebl, M.4    Rachel, R.5    Hermo-Parrado, X.L.6
  • 42
    • 78649504169 scopus 로고    scopus 로고
    • Orally administered P22 phage tailspike protein reduces salmonella colonization in chickens: prospects of a novel therapy against bacterial infections
    • Waseh, S., P. Hanifi-Moghaddam, R. Coleman, M. Masotti, S. Ryan, M. Foss, et al. 2010. Orally administered P22 phage tailspike protein reduces salmonella colonization in chickens: prospects of a novel therapy against bacterial infections. PLoS ONE 5:e13904.
    • (2010) PLoS ONE , vol.5
    • Waseh, S.1    Hanifi-Moghaddam, P.2    Coleman, R.3    Masotti, M.4    Ryan, S.5    Foss, M.6
  • 43
    • 22144446352 scopus 로고    scopus 로고
    • Coevolutionary arms races between bacteria and bacteriophage
    • Weitz, J. S., H. Hartman, and S. A. Levin. 2005. Coevolutionary arms races between bacteria and bacteriophage. Proc. Natl. Acad. Sci. USA 102:9535-9540.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9535-9540
    • Weitz, J.S.1    Hartman, H.2    Levin, S.A.3
  • 44
    • 77951581144 scopus 로고    scopus 로고
    • Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM
    • Xia, G., L. Maier, P. Sanchez-Carballo, M. Li, M. Otto, O. Holst, et al. 2010. Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM. J. Biol. Chem. 285:13405-13415.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13405-13415
    • Xia, G.1    Maier, L.2    Sanchez-Carballo, P.3    Li, M.4    Otto, M.5    Holst, O.6
  • 45
    • 79960416809 scopus 로고    scopus 로고
    • Wall teichoic Acid-dependent adsorption of staphylococcal siphovirus and myovirus
    • Xia, G., R. M. Corrigan, V. Winstel, C. Goerke, A. Gründling, and A. Peschel. 2011. Wall teichoic Acid-dependent adsorption of staphylococcal siphovirus and myovirus. J. Bacteriol. 193:4006-4009.
    • (2011) J. Bacteriol. , vol.193 , pp. 4006-4009
    • Xia, G.1    Corrigan, R.M.2    Winstel, V.3    Goerke, C.4    Gründling, A.5    Peschel, A.6
  • 46
    • 65549169054 scopus 로고    scopus 로고
    • Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike
    • Xiang, Y., P. G. Leiman, L. Li, S. Grimes, D. L. Anderson, and M. G. Rossmann. 2009. Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Mol. Cell 34:375-386.
    • (2009) Mol. Cell , vol.34 , pp. 375-386
    • Xiang, Y.1    Leiman, P.G.2    Li, L.3    Grimes, S.4    Anderson, D.L.5    Rossmann, M.G.6
  • 47
    • 10644246690 scopus 로고    scopus 로고
    • Alteration of tail fiber protein gp38 enables T2 phage to infect Escherichia coli O157:H7
    • Yoichi, M., M. Abe, K. Miyanaga, H. Unno, and Y. Tanji. 2005. Alteration of tail fiber protein gp38 enables T2 phage to infect Escherichia coli O157:H7. J. Biotechnol. 115:101-107.
    • (2005) J. Biotechnol. , vol.115 , pp. 101-107
    • Yoichi, M.1    Abe, M.2    Miyanaga, K.3    Unno, H.4    Tanji, Y.5


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