메뉴 건너뛰기




Volumn 26, Issue 1, 2015, Pages 160-170

Antimicrobial activity of bacteriophage endolysin produced in nicotiana benthamiana plants

Author keywords

Endolysin; Nicotiana benthamiana; Potato proteinase inhibitor I; Potato virus X; Transient expression; Vacuolar targeting

Indexed keywords

BACTERIAL PROTEIN; CP933 ENDOLYSIN; SIGNAL PEPTIDE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ENDOLYSIN; PROTEINASE; VIRAL PROTEIN;

EID: 84955593562     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1505.05060     Document Type: Article
Times cited : (16)

References (42)
  • 2
    • 33645227952 scopus 로고    scopus 로고
    • Bacteriophage endolysins as a novel class of antibacterial agent
    • Borysowski J, Weber-Dabrowska B, Gorski A. 2006. Bacteriophage endolysins as a novel class of antibacterial agent. Exp. Biol. Med. 231: 366-377.
    • (2006) Exp. Biol. Med , vol.231 , pp. 366-377
    • Borysowski, J.1    Weber-Dabrowska, B.2    Gorski, A.3
  • 3
    • 0026892978 scopus 로고
    • Potato virus X as a vector for gene expression in plants
    • Chapman S, Kavanagh T, Baulcombe D. 1992. Potato virus X as a vector for gene expression in plants. Plant J. 2: 549-557.
    • (1992) Plant J , vol.2 , pp. 549-557
    • Chapman, S.1    Kavanagh, T.2    Baulcombe, D.3
  • 4
    • 84891148781 scopus 로고    scopus 로고
    • The production of recombinant cationic α-helical antimicrobial peptides in plant cells induces the formation of protein bodies derived from the endoplasmic reticulum
    • Company N, Nadal A, La Paz J-L, Martínez S, Rasche S, Schillberg S, et al. 2014. The production of recombinant cationic α-helical antimicrobial peptides in plant cells induces the formation of protein bodies derived from the endoplasmic reticulum. Plant Biotechnol. J. 12: 81-92.
    • (2014) Plant Biotechnol. J , vol.12 , pp. 81-92
    • Company, N.1    Nadal, A.2    La Paz, J.-L.3    Martínez, S.4    Rasche, S.5    Schillberg, S.6
  • 5
    • 0035979785 scopus 로고    scopus 로고
    • Expression of the native cholera B toxin subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts
    • Daniell H, Lee SB, Panchal T, Wiebe PO. 2001. Expression of the native cholera B toxin subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts. J. Mol. Biol. 311: 1001-1009.
    • (2001) J. Mol. Biol , vol.311 , pp. 1001-1009
    • Daniell, H.1    Lee, S.B.2    Panchal, T.3    Wiebe, P.O.4
  • 7
    • 51349138721 scopus 로고    scopus 로고
    • Bacteriophage and peptidoglycan degrading enzymes with antimicrobial applications
    • Donovan DM. 2007. Bacteriophage and peptidoglycan degrading enzymes with antimicrobial applications. Recent Pat. Biotechnol. 1: 1-10.
    • (2007) Recent Pat. Biotechnol , vol.1 , pp. 1-10
    • Donovan, D.M.1
  • 8
    • 79953326993 scopus 로고    scopus 로고
    • Peptidoglycan hydrolase enzyme fusions are uniquely suited for treating multi-drug resistant pathogens
    • Donovan DM, Becker SC, Dong S, Baker JR, Foster-Frey JA, Pritchard DG. 2009. Peptidoglycan hydrolase enzyme fusions are uniquely suited for treating multi-drug resistant pathogens. Biotech. Int. 21: 6-10.
    • (2009) Biotech. Int , vol.21 , pp. 6-10
    • Donovan, D.M.1    Becker, S.C.2    Dong, S.3    Baker, J.R.4    Foster-Frey, J.A.5    Pritchard, D.G.6
  • 11
    • 77949555873 scopus 로고    scopus 로고
    • Excess costs and utilization associated with Staphylococcus aureus infection
    • Filice GA, Nyman JA, Lexau C. 2010. Excess costs and utilization associated with Staphylococcus aureus infection. Infect. Control Hosp. Epidemiol. 31: 365-367.
    • (2010) Infect. Control Hosp. Epidemiol , vol.31 , pp. 365-367
    • Filice, G.A.1    Nyman, J.A.2    Lexau, C.3
  • 12
    • 55049135817 scopus 로고    scopus 로고
    • Bacteriophage lysins as effective antibacterials
    • Fischetti VA. 2008. Bacteriophage lysins as effective antibacterials. Curr. Opin. Microbiol. 11: 393-400.
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 393-400
    • Fischetti, V.A.1
  • 13
    • 77955557492 scopus 로고    scopus 로고
    • Bacteriophage endolysins: A novel antiinfective to control gram-positive pathogens
    • Fischetti VA. 2010. Bacteriophage endolysins: a novel antiinfective to control gram-positive pathogens. Int. J. Med. Microbiol. 300: 357-362.
    • (2010) Int. J. Med. Microbiol , vol.300 , pp. 357-362
    • Fischetti, V.A.1
  • 15
    • 77955084973 scopus 로고    scopus 로고
    • Comparative efficiency of subcellular targeting signals for expression of a toxic protein in sugarcane
    • Jackson MA, Nutt KA, Hassall R, Rae AL. 2010. Comparative efficiency of subcellular targeting signals for expression of a toxic protein in sugarcane. Funct. Plant Biol. 37: 785-793.
    • (2010) Funct. Plant Biol , vol.37 , pp. 785-793
    • Jackson, M.A.1    Nutt, K.A.2    Hassall, R.3    Rae, A.L.4
  • 17
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions
    • Jauh G-Y, Phillips TE, Rogers JC. 1999. Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 11: 1867-1882.
    • (1999) Plant Cell , vol.11 , pp. 1867-1882
    • Jauh, G.-Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 20
    • 54849422795 scopus 로고    scopus 로고
    • Expression and functional characterization of the plant antimicrobial snakin- 1 and defensin recombinant proteins. Protein Expr
    • Kovalskaya N, Hammond RW. 2009. Expression and functional characterization of the plant antimicrobial snakin- 1 and defensin recombinant proteins. Protein Expr. Purif. 63: 12-17.
    • (2009) Purif , vol.63 , pp. 12-17
    • Kovalskaya, N.1    Hammond, R.W.2
  • 21
    • 84860916050 scopus 로고    scopus 로고
    • Antibacterial and antifungal activity of a snakin-defensin hybrid protein expressed in tobacco and potato plants
    • Kovalskaya N, Zhao Y, Hammond RW. 2011. Antibacterial and antifungal activity of a snakin-defensin hybrid protein expressed in tobacco and potato plants. Open Plant Sci. J. 5: 29-42.
    • (2011) Open Plant Sci. J , vol.5 , pp. 29-42
    • Kovalskaya, N.1    Zhao, Y.2    Hammond, R.W.3
  • 22
    • 57549086266 scopus 로고    scopus 로고
    • Use of Potato virus X (PVX)- based vectors for gene expression and virus-induced gene silencing (VIGS)
    • Lacomme C, Chapman S. 2008. Use of Potato virus X (PVX)- based vectors for gene expression and virus-induced gene silencing (VIGS). Curr. Protoc. Microbiol. 8: 161.1.1-161.1.13.
    • (2008) Curr. Protoc. Microbiol , vol.8
    • Lacomme, C.1    Chapman, S.2
  • 23
    • 46049083590 scopus 로고    scopus 로고
    • Viral vectors for production of recombinant proteins in plants
    • Lico C, Chen Q, Santi L. 2008. Viral vectors for production of recombinant proteins in plants. J. Cell. Physiol. 216: 366-377.
    • (2008) J. Cell. Physiol , vol.216 , pp. 366-377
    • Lico, C.1    Chen, Q.2    Santi, L.3
  • 24
    • 0037224191 scopus 로고    scopus 로고
    • Synergistic lethal effect of a combination of phage lytic enzymes with different activities on penicillin-sensitive and -resistant Streptococcus pneumoniae strains. Antimicrob
    • Loeffler JM, Fischetti VA. 2003. Synergistic lethal effect of a combination of phage lytic enzymes with different activities on penicillin-sensitive and -resistant Streptococcus pneumoniae strains. Antimicrob. Agents Chemother. 47: 375-377.
    • (2003) Agents Chemother , vol.47 , pp. 375-377
    • Loeffler, J.M.1    Fischetti, V.A.2
  • 25
    • 0035824437 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase
    • Loeffler JM, Nelson D, Fischetti VA. 2001. Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science 294: 2170-2172.
    • (2001) Science , vol.294 , pp. 2170-2172
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 26
    • 0036000259 scopus 로고    scopus 로고
    • Expression of biotin-binding proteins, avidin and streptavidin, in plant tissues using plant vacuolar targeting sequences
    • Murray C, Sutherland PW, Phung MM, Lester MT, Marshall RK, Christeller JT. 2002. Expression of biotin-binding proteins, avidin and streptavidin, in plant tissues using plant vacuolar targeting sequences. Transgenic Res. 11: 199-214.
    • (2002) Transgenic Res , vol.11 , pp. 199-214
    • Murray, C.1    Sutherland, P.W.2    Phung, M.M.3    Lester, M.T.4    Marshall, R.K.5    Christeller, J.T.6
  • 28
    • 3843065569 scopus 로고    scopus 로고
    • Bacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysis
    • Orito Y, Morita M, Hori K, Unno H, Tanji Y. 2004. Bacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysis. Appl. Microbiol. Biotechnol. 65: 105-109.
    • (2004) Appl. Microbiol. Biotechnol , vol.65 , pp. 105-109
    • Orito, Y.1    Morita, M.2    Hori, K.3    Unno, H.4    Tanji, Y.5
  • 31
    • 37449031844 scopus 로고    scopus 로고
    • The pinholin of lambdoid phage 21: Control of lysis by membrane depolarization
    • Park T, Struck DK, Dankenbring CA, Young R. 2007. The pinholin of lambdoid phage 21: control of lysis by membrane depolarization. J. Bacteriol. 189: 9135-9139.
    • (2007) J. Bacteriol , vol.189 , pp. 9135-9139
    • Park, T.1    Struck, D.K.2    Dankenbring, C.A.3    Young, R.4
  • 33
    • 35348839572 scopus 로고    scopus 로고
    • Efficient elimination of multidrugresistant Staphylococcus aureus by cloned lysin derived from bacteriophage phi MR11
    • Rashel M, Uchiyama J, Ujihara T, Uehara Y, Kuramoto S, Sugihara S, et al. 2007. Efficient elimination of multidrugresistant Staphylococcus aureus by cloned lysin derived from bacteriophage phi MR11. J. Infect. Dis. 196: 1237-1247.
    • (2007) J. Infect. Dis , vol.196 , pp. 1237-1247
    • Rashel, M.1    Uchiyama, J.2    Ujihara, T.3    Uehara, Y.4    Kuramoto, S.5    Sugihara, S.6
  • 34
  • 35
    • 0033808851 scopus 로고    scopus 로고
    • The Nterminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells
    • São-José C, Parreira R, Vieira G, Santos MA. 2000. The Nterminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells. J. Bacteriol. 182: 5823-5831.
    • (2000) J. Bacteriol , vol.182 , pp. 5823-5831
    • São-José, C.1    Parreira, R.2    Vieira, G.3    Santos, M.A.4
  • 38
    • 2642552973 scopus 로고    scopus 로고
    • The P domain of novovirus capsid protein forms dimer and binds to histoblood group antigen receptors
    • Tan M, Hegde RS, Jiang X. 2004. The P domain of novovirus capsid protein forms dimer and binds to histoblood group antigen receptors. J. Virol. 78: 6233-6242.
    • (2004) J. Virol , vol.78 , pp. 6233-6242
    • Tan, M.1    Hegde, R.S.2    Jiang, X.3
  • 40
    • 0037310365 scopus 로고    scopus 로고
    • Sizing the holin lesion with an endolysin-beta-galactosidase fusion
    • Wang I-N, Deaton J, Young R. 2003. Sizing the holin lesion with an endolysin-beta-galactosidase fusion. J. Bacteriol. 185: 779-787.
    • (2003) J. Bacteriol , vol.185 , pp. 779-787
    • Wang, I.-N.1    Deaton, J.2    Young, R.3
  • 41
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • Wang I-N, Smith DL, Young R. 2000. Holins: the protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54: 799-825.
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 799-825
    • Wang, I.-N.1    Smith, D.L.2    Young, R.3
  • 42
    • 2342634418 scopus 로고    scopus 로고
    • A signal-arrest release sequence mediates export and control of the phage P1 endolysin
    • Xu M, Struck DK, Deaton J, Wang I-N, Young RY. 2004. A signal-arrest release sequence mediates export and control of the phage P1 endolysin. Proc. Natl. Acad. Sci. USA 101: 6415-6420.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6415-6420
    • Xu, M.1    Struck, D.K.2    Deaton, J.3    Wang, I.-N.4    Young, R.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.