메뉴 건너뛰기




Volumn 4, Issue 1, 2018, Pages

Fighting biofilms with lantibiotics and other groups of bacteriocins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCIN; CINNAMALDEHYDE; CIPROFLOXACIN; CITRIC ACID; DAPTOMYCIN; GALLIDERMIN; HYPOCHLORITE SODIUM; ISK 1; LACTICIN Q; LANTIBIOTIC; LYSOZYME; NISIN; NUKACIN; POLYMYXIN; UNCLASSIFIED DRUG;

EID: 85045917461     PISSN: None     EISSN: 20555008     Source Type: Journal    
DOI: 10.1038/s41522-018-0053-6     Document Type: Article
Times cited : (149)

References (176)
  • 1
    • 84982182003 scopus 로고    scopus 로고
    • Biofilms: An emergent form of bacterial life
    • Flemming, H. C. et al. Biofilms: An emergent form of bacterial life. Nat. Rev. Microbiol. 14, 563-575 (2016).
    • (2016) Nat. Rev. Microbiol. , vol.14 , pp. 563-575
    • Flemming, H.C.1
  • 2
    • 0036711963 scopus 로고    scopus 로고
    • Biofilms: Microbial life on surfaces
    • Donlan, R. Biofilms: microbial life on surfaces. Emerg. Infect. Dis. 8, 881-890 (2002).
    • (2002) Emerg. Infect. Dis. , vol.8 , pp. 881-890
    • Donlan, R.1
  • 3
    • 84893394600 scopus 로고    scopus 로고
    • Microscopic findings for the study of biofilms in food environments
    • Olszewska, M. Microscopic findings for the study of biofilms in food environments. Acta Biochim. Pol. 60, 531-537 (2013).
    • (2013) Acta Biochim. Pol. , vol.60 , pp. 531-537
    • Olszewska, M.1
  • 5
    • 84878998919 scopus 로고    scopus 로고
    • Bacterial biofilms: Development, dispersal, and therapeutic strategies in the dawn of the postantibiotic era
    • Kostakioti, M., Hadjifrangiskou, M. & Hultgren, S. J. Bacterial biofilms: development, dispersal, and therapeutic strategies in the dawn of the postantibiotic era. Cold Spring Harb. Perspect. Med. 3, a010306 (2013).
    • (2013) Cold Spring Harb. Perspect. Med. , vol.3 , pp. a010306
    • Kostakioti, M.1    Hadjifrangiskou, M.2    Hultgren, S.J.3
  • 6
    • 52349091962 scopus 로고    scopus 로고
    • Bacterial adhesion and biofilms on surfaces
    • Garrett, T. G., Bhakoo, M. & Zhang, Z. Bacterial adhesion and biofilms on surfaces. Prog. Nat. Sci. 18, 1049-1056 (2008).
    • (2008) Prog. Nat. Sci. , vol.18 , pp. 1049-1056
    • Garrett, T.G.1    Bhakoo, M.2    Zhang, Z.3
  • 8
    • 78650181025 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa biofilms in cystic fibrosis
    • Høiby, N., Ciofu, O. & Bjarnsholt, T. Pseudomonas aeruginosa biofilms in cystic fibrosis. Future Microbiol. 5, 1663-1674 (2010).
    • (2010) Future Microbiol. , vol.5 , pp. 1663-1674
    • Høiby, N.1    Ciofu, O.2    Bjarnsholt, T.3
  • 9
    • 22144463151 scopus 로고    scopus 로고
    • Biofilms and antibiotic therapy: Is there a role for combating bacterial resistance by the use of novel drug delivery systems?
    • Smith, A. W. Biofilms and antibiotic therapy: is there a role for combating bacterial resistance by the use of novel drug delivery systems? Adv. Drug. Deliv. Rev. 57, 1539-1550 (2005).
    • (2005) Adv. Drug. Deliv. Rev. , vol.57 , pp. 1539-1550
    • Smith, A.W.1
  • 10
    • 74649084320 scopus 로고    scopus 로고
    • A review of current and emergent biofilm control strategies
    • Simões, M., Simões, L. C. & Vieira, M. J. A review of current and emergent biofilm control strategies. LWT Food Sci. Technol. 43, 573-583 (2010).
    • (2010) LWT Food Sci. Technol. , vol.43 , pp. 573-583
    • Simões, M.1    Simões, L.C.2    Vieira, M.J.3
  • 11
    • 84907993181 scopus 로고    scopus 로고
    • Inhibition and destruction of Pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides
    • Dosler, S. & Karaaslan, E. Inhibition and destruction of Pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides. Peptides 62, 32-37 (2014).
    • (2014) Peptides , vol.62 , pp. 32-37
    • Dosler, S.1    Karaaslan, E.2
  • 12
    • 84869211892 scopus 로고    scopus 로고
    • In vitro activities of antibiotics and antimicrobial cationic peptides alone and in combination against methicillin-resistant Staphylococcus aureus biofilms
    • Mataraci, E. & Dosler, S. In vitro activities of antibiotics and antimicrobial cationic peptides alone and in combination against methicillin-resistant Staphylococcus aureus biofilms. Antimicrob. Agents Chemother. 56, 6366-6371 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 6366-6371
    • Mataraci, E.1    Dosler, S.2
  • 14
    • 84872488958 scopus 로고    scopus 로고
    • Bacteriocins-A viable alternative to antibiotics?
    • Cotter, P. D., Ross, R. P. & Hill, C. Bacteriocins-A viable alternative to antibiotics? Nat. Rev. Microbiol. 11, 95-105 (2013).
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 95-105
    • Cotter, P.D.1    Ross, R.P.2    Hill, C.3
  • 15
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D., Hill, C. & Ross, R. P. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 3, 777-788 (2005).
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 16
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • Chatterjee, C., Paul, M., Xie, L. & van der Donk, W. A. Biosynthesis and mode of action of lantibiotics. Chem. Rev. 105, 633-684 (2005).
    • (2005) Chem. Rev. , vol.105 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    Van Der Donk, W.A.4
  • 17
    • 65949089371 scopus 로고    scopus 로고
    • Lantibiotics: Mode of action, biosynthesis and bioengineering
    • Bierbaum, G. & Sahl, H. G. Lantibiotics: mode of action, biosynthesis and bioengineering. Curr. Pharm. Biotechnol. 10, 2-18 (2009).
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 2-18
    • Bierbaum, G.1    Sahl, H.G.2
  • 19
    • 65749104456 scopus 로고    scopus 로고
    • Dissecting structural and functional diversity of the lantibiotic mersacidin
    • Appleyard, A. N. et al. Dissecting structural and functional diversity of the lantibiotic mersacidin. Chem. Biol. 16, 490-498 (2009).
    • (2009) Chem. Biol. , vol.16 , pp. 490-498
    • Appleyard, A.N.1
  • 20
    • 45149121558 scopus 로고    scopus 로고
    • The generation of nisin variants with enhanced activity against specific gram-positive pathogens
    • Field, D., O'Connor, P. M., Cotter, P. D., Hill, C. & Ross, R. P. The generation of nisin variants with enhanced activity against specific gram-positive pathogens. Mol. Microbiol. 69, 218-230 (2008).
    • (2008) Mol. Microbiol. , vol.69 , pp. 218-230
    • Field, D.1    O'Connor, P.M.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 21
    • 84867326984 scopus 로고    scopus 로고
    • Bioengineered nisin a derivatives with enhanced activity against both gram positive and gram negative pathogens
    • e46884 1:CAS:528:DC%2BC38XhsFCitrvF 23056510 3466204
    • Field, D. et al. Bioengineered nisin a derivatives with enhanced activity against both gram positive and gram negative pathogens. PLoS One 7, e46884 (2012).
    • (2012) PLoS One , vol.7
    • Field, D.1
  • 22
    • 34648825064 scopus 로고    scopus 로고
    • Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-Terminal truncation
    • Rink, R. et al. Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-Terminal truncation. Appl. Environ. Microbiol. 73, 5809-5816 (2007).
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5809-5816
    • Rink, R.1
  • 23
    • 84862011041 scopus 로고    scopus 로고
    • Bioengineered nisin derivatives with enhanced activity in complex matrices
    • Rouse, S. et al. Bioengineered nisin derivatives with enhanced activity in complex matrices. Microb. Biotechnol. 5, 501-508 (2012).
    • (2012) Microb. Biotechnol. , vol.5 , pp. 501-508
    • Rouse, S.1
  • 24
    • 66949175869 scopus 로고    scopus 로고
    • Evaluation of essential and variable residues of nukacin ISK-1 by NNK scanning
    • Islam, M. R. et al. Evaluation of essential and variable residues of nukacin ISK-1 by NNK scanning. Mol. Microbiol. 72, 1438-1447 (2009).
    • (2009) Mol. Microbiol. , vol.72 , pp. 1438-1447
    • Islam, M.R.1
  • 25
    • 84879800778 scopus 로고    scopus 로고
    • Site-directed mutations in the lanthipeptide mutacin 1140
    • Chen, S. et al. Site-directed mutations in the lanthipeptide mutacin 1140. Appl. Environ. Microbiol. 79, 4015-4023 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4015-4023
    • Chen, S.1
  • 26
    • 0029093410 scopus 로고
    • Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering
    • Rollema, H. S., Kuipers, O. P., Both, P., de Vos, W. M. & Siezen, R. J. Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering. Appl. Environ. Microbiol. 61, 2873-2878 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2873-2878
    • Rollema, H.S.1    Kuipers, O.P.2    Both, P.3    De Vos, W.M.4    Siezen, R.J.5
  • 27
    • 3142701459 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants
    • Yuan, J., Zhang, Z. Z., Chen, X. Z., Yang, W. & Huan, L. D. Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants. Appl. Microbiol. Biotechnol. 64, 806-815 (2004).
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 806-815
    • Yuan, J.1    Zhang, Z.Z.2    Chen, X.Z.3    Yang, W.4    Huan, L.D.5
  • 28
    • 77953791246 scopus 로고    scopus 로고
    • Spatial and temporal patterns of biocide action against Staphylococcus epidermidis biofilms
    • Davison, W. M., Pitts, B. & Stewart, P. S. Spatial and temporal patterns of biocide action against Staphylococcus epidermidis biofilms. Antimicrob. Agents Chemother. 54, 2920-2927 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2920-2927
    • Davison, W.M.1    Pitts, B.2    Stewart, P.S.3
  • 29
    • 84949809882 scopus 로고    scopus 로고
    • Bioengineering lantibiotics for therapeutic success
    • Field, D., Cotter, P. D., Hill, C. & Ross, R. P. Bioengineering lantibiotics for therapeutic success. Front. Microbiol. 6, 1363 (2015a).
    • (2015) Front. Microbiol. , vol.6 , pp. 1363
    • Field, D.1    Cotter, P.D.2    Hill, C.3    Ross, R.P.4
  • 30
    • 84948162012 scopus 로고    scopus 로고
    • Bioengineering of the model lantibiotic nisin
    • Field, D., Cotter, P. D., Ross, R. P. & Hill, C. Bioengineering of the model lantibiotic nisin. Bioengineered 6, 187-192 (2015b).
    • (2015) Bioengineered , vol.6 , pp. 187-192
    • Field, D.1    Cotter, P.D.2    Ross, R.P.3    Hill, C.4
  • 31
    • 84926052621 scopus 로고    scopus 로고
    • A bioengineered nisin derivative to control biofilms of Staphylococcus pseudintermedius
    • e0119684 25789988 4366236
    • Field, D. et al. A bioengineered nisin derivative to control biofilms of Staphylococcus pseudintermedius. PLoS One 10, e0119684 (2015c).
    • (2015) PLoS One , vol.10
    • Field, D.1
  • 32
    • 84966292088 scopus 로고    scopus 로고
    • In vitro activities of nisin and nisin derivatives alone and in combination with antibiotics against Staphylococcus biofilms
    • Field, D., O' Connor, R., Cotter, P. D., Ross, R. P. & Hill, C. In vitro activities of nisin and nisin derivatives alone and in combination with antibiotics against Staphylococcus biofilms. Front. Microbiol. 7, 508 (2016a).
    • (2016) Front. Microbiol. , vol.7 , pp. 508
    • Field, D.1    O'Connor, R.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 33
    • 34249086855 scopus 로고    scopus 로고
    • A novel lantibiotic acting on bacterial cell wall synthesis produced by the uncommon actinomycete Planomonospora sp
    • Castiglione, F. et al. A novel lantibiotic acting on bacterial cell wall synthesis produced by the uncommon actinomycete Planomonospora sp. Biochemistry 46, 5884-5895 (2007).
    • (2007) Biochemistry , vol.46 , pp. 5884-5895
    • Castiglione, F.1
  • 34
    • 33645119895 scopus 로고    scopus 로고
    • Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells in vitro
    • Maher, S. & McClean, S. Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells in vitro. Biochem. Pharmacol. 71, 1289-1298 (2006).
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 1289-1298
    • Maher, S.1    McClean, S.2
  • 35
    • 0038036874 scopus 로고    scopus 로고
    • In vitro assessment of the cytotoxicity of nisin, pediocin, and selected colicins on simian virus 40-Transfected human colon and Vero monkey kidney cells with trypan blue staining viability assays
    • Murinda, S. E., Rashid, K. A. & Roberts, R. F. In vitro assessment of the cytotoxicity of nisin, pediocin, and selected colicins on simian virus 40-Transfected human colon and Vero monkey kidney cells with trypan blue staining viability assays. J. Food Prot. 66, 847-853 (2003).
    • (2003) J. Food Prot. , vol.66 , pp. 847-853
    • Murinda, S.E.1    Rashid, K.A.2    Roberts, R.F.3
  • 36
    • 13844316746 scopus 로고    scopus 로고
    • Enterococcal cytolysin: A novel two component peptide system that serves as a bacterial defense against eukaryotic and prokaryotic cells
    • Cox, C. R., Coburn, P. S. & Gilmore, M. S. Enterococcal cytolysin: A novel two component peptide system that serves as a bacterial defense against eukaryotic and prokaryotic cells. Curr. Protein Pept. Sci. 6, 77-84 (2005).
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 77-84
    • Cox, C.R.1    Coburn, P.S.2    Gilmore, M.S.3
  • 37
    • 4644277619 scopus 로고    scopus 로고
    • Biofilm formation among methicillin-resistant Staphylococcus aureus isolates from patients with urinary tract infection
    • Ando, E., Monden, K., Mitsuhata, R., Kariyama, R. & Kumon, H. Biofilm formation among methicillin-resistant Staphylococcus aureus isolates from patients with urinary tract infection. Acta Med. Okayama. 58, 207-214 (2004).
    • (2004) Acta Med. Okayama. , vol.58 , pp. 207-214
    • Ando, E.1    Monden, K.2    Mitsuhata, R.3    Kariyama, R.4    Kumon, H.5
  • 38
    • 84886952387 scopus 로고    scopus 로고
    • Investigation of biofilm formation and its association with the molecular and clinical characteristics of Methicillin-resistant Staphylococcus aureus
    • Cha, J. O. et al. Investigation of biofilm formation and its association with the molecular and clinical characteristics of Methicillin-resistant Staphylococcus aureus. Osong. Public Health Res. Perspect. 4, 225-232 (2013).
    • (2013) Osong. Public Health Res. Perspect. , vol.4 , pp. 225-232
    • Cha, J.O.1
  • 39
    • 85005773700 scopus 로고    scopus 로고
    • Methicillin resistance and the biofilm phenotype in Staphylococcus aureus
    • McCarthy, H. et al. Methicillin resistance and the biofilm phenotype in Staphylococcus aureus. Front. Cell. Infect. Microbiol. 5, 1 (2015).
    • (2015) Front. Cell. Infect. Microbiol. , vol.5 , pp. 1
    • McCarthy, H.1
  • 40
    • 80052458914 scopus 로고    scopus 로고
    • Staphylococcus aureus and MRSA in cystic fibrosis
    • Goss, C. H. & Muhlebach, M. S. Staphylococcus aureus and MRSA in cystic fibrosis. J. Cyst. Fibros. 10, 298-306 (2011).
    • (2011) J. Cyst. Fibros. , vol.10 , pp. 298-306
    • Goss, C.H.1    Muhlebach, M.S.2
  • 42
    • 84965186589 scopus 로고    scopus 로고
    • Staphylococcus aureus biofilms: Recent developments in biofilm dispersal
    • Lister, J. L. & Horswill, A. R. Staphylococcus aureus biofilms: recent developments in biofilm dispersal. Front. Cell Infect. Microbiol. 4, 178 (2014).
    • (2014) Front. Cell Infect. Microbiol. , vol.4 , pp. 178
    • Lister, J.L.1    Horswill, A.R.2
  • 43
    • 84856393146 scopus 로고    scopus 로고
    • How Staphylococcus aureus biofilms develop their characteristic structure
    • Periasamy, S. et al. How Staphylococcus aureus biofilms develop their characteristic structure. Proc. Natl. Acad. Sci. USA 109, 1281-1286 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1281-1286
    • Periasamy, S.1
  • 44
    • 80053910254 scopus 로고    scopus 로고
    • Staphylococcus aureus biofilms: Properties, regulation, and roles in human disease
    • Archer, N. K. et al. Staphylococcus aureus biofilms: properties, regulation, and roles in human disease. Virulence 2, 445-459 (2011).
    • (2011) Virulence , vol.2 , pp. 445-459
    • Archer, N.K.1
  • 45
    • 84884367520 scopus 로고    scopus 로고
    • In vitro pharmacokinetics of antimicrobial cationic peptides alone and in combination with antibiotics against methicillin resistant Staphylococcus aureus biofilms
    • Dosler, S. & Mataraci, E. In vitro pharmacokinetics of antimicrobial cationic peptides alone and in combination with antibiotics against methicillin resistant Staphylococcus aureus biofilms. Peptides 49, 53-58 (2013).
    • (2013) Peptides , vol.49 , pp. 53-58
    • Dosler, S.1    Mataraci, E.2
  • 46
    • 84885919574 scopus 로고    scopus 로고
    • Effects of bacteriocins on methicillin-resistant Staphylococcus aureus biofilm
    • Okuda, K. et al. Effects of bacteriocins on methicillin-resistant Staphylococcus aureus biofilm. Antimicrob. Agents Chemother. 57, 5572-5579 (2013).
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 5572-5579
    • Okuda, K.1
  • 47
    • 0034330091 scopus 로고    scopus 로고
    • A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: Cloning of the structural gene and identification of the structure
    • Sashihara, T. et al. A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: cloning of the structural gene and identification of the structure. Biosci. Biotechnol. Biochem. 64, 2420-2428 (2000).
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2420-2428
    • Sashihara, T.1
  • 48
    • 79953197608 scopus 로고    scopus 로고
    • Lantibiotic transporter requires cooperative functioning of the peptidase domain and the ATP binding domain
    • Nishie, M. et al. Lantibiotic transporter requires cooperative functioning of the peptidase domain and the ATP binding domain. J. Biol. Chem. 286, 11163-11169 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 11163-11169
    • Nishie, M.1
  • 49
    • 34248172307 scopus 로고    scopus 로고
    • Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of gram-positive bacteria
    • Fujita, K. et al. Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of gram-positive bacteria. Appl. Environ. Microbiol. 73, 2871-2877 (2007).
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2871-2877
    • Fujita, K.1
  • 50
    • 84860376483 scopus 로고    scopus 로고
    • Expression and purification of lacticin Q by small ubiquitin-related modifier fusion in Escherichia coli
    • Ma, Q., Yu, Z., Han, B., Wang, Q. & Zhang, R. Expression and purification of lacticin Q by small ubiquitin-related modifier fusion in Escherichia coli. J. Microbiol. 50, 326-331 (2012).
    • (2012) J. Microbiol. , vol.50 , pp. 326-331
    • Ma, Q.1    Yu, Z.2    Han, B.3    Wang, Q.4    Zhang, R.5
  • 51
    • 84906858151 scopus 로고    scopus 로고
    • Bovicin HC5 and nisin reduce Staphylococcus aureus adhesion to polystyrene and change the hydrophobicity profile and Gibbs free energy of adhesion
    • Pimentel-Filho Nde, J., Martins, M. C., Nogueira, G. B., Mantovani, H. C. & Vanetti, M. C. Bovicin HC5 and nisin reduce Staphylococcus aureus adhesion to polystyrene and change the hydrophobicity profile and Gibbs free energy of adhesion. Int. J. Food Microbiol. 190, 1-8 (2014).
    • (2014) Int. J. Food Microbiol. , vol.190 , pp. 1-8
    • Pimentel-Filho Nde, J.1    Martins, M.C.2    Nogueira, G.B.3    Mantovani, H.C.4    Vanetti, M.C.5
  • 52
    • 84865758140 scopus 로고    scopus 로고
    • Effects of nisin and lysozyme on growth inhibition and biofilm formation capacity of Staphylococcus aureus strains isolated from raw milk and cheese samples
    • Sudagidan, M. & Yemenicioǧlu, A. Effects of nisin and lysozyme on growth inhibition and biofilm formation capacity of Staphylococcus aureus strains isolated from raw milk and cheese samples. J. Food Prot. 75, 1627-1633 (2012).
    • (2012) J. Food Prot. , vol.75 , pp. 1627-1633
    • Sudagidan, M.1    Yemenicioǧlu, A.2
  • 53
    • 84868035975 scopus 로고    scopus 로고
    • Activity of gallidermin on Staphylococcus aureus and Staphylococcus epidermidis biofilms
    • Saising, J. et al. Activity of gallidermin on Staphylococcus aureus and Staphylococcus epidermidis biofilms. Antimicrob. Agents Chemother. 56, 5804-5810 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 5804-5810
    • Saising, J.1
  • 54
    • 67651246873 scopus 로고    scopus 로고
    • Staphylococcus epidermidis-The 'accidental' pathogen
    • Otto, M. Staphylococcus epidermidis-The 'accidental' pathogen. Nat. Rev. Microbiol. 7, 555-567 (2009).
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 555-567
    • Otto, M.1
  • 55
    • 84892993355 scopus 로고    scopus 로고
    • Staphylococcus epidermidis as the most frequent cause of nosocomial infections: Old and new fighting strategies
    • Gomes, F., Teixeira, P. & Oliveira, R. Staphylococcus epidermidis as the most frequent cause of nosocomial infections: old and new fighting strategies. Biofouling 30, 131-141 (2014).
    • (2014) Biofouling , vol.30 , pp. 131-141
    • Gomes, F.1    Teixeira, P.2    Oliveira, R.3
  • 56
    • 33845607284 scopus 로고    scopus 로고
    • Persister cells, dormancy and infectious disease
    • Lewis, K. Persister cells, dormancy and infectious disease. Nat. Rev. Microbiol. 5, 48-56 (2007).
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 48-56
    • Lewis, K.1
  • 57
    • 77955628762 scopus 로고    scopus 로고
    • Persister cells
    • Lewis, K. Persister cells. Annu. Rev. Microbiol. 64, 357-372 (2010).
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 357-372
    • Lewis, K.1
  • 58
    • 17144416850 scopus 로고    scopus 로고
    • Persister cells and the riddle of biofilm survival
    • Lewis, K. Persister cells and the riddle of biofilm survival. Biochemistry. (Mosc.). 70, 267-274 (2005).
    • (2005) Biochemistry. (Mosc.). , vol.70 , pp. 267-274
    • Lewis, K.1
  • 59
    • 45549104015 scopus 로고    scopus 로고
    • Multidrug tolerance of biofilms and persister cells
    • Lewis, K. Multidrug tolerance of biofilms and persister cells. Curr. Top. Microbiol. Immunol. 322, 107-131 (2008).
    • (2008) Curr. Top. Microbiol. Immunol. , vol.322 , pp. 107-131
    • Lewis, K.1
  • 60
    • 84876962863 scopus 로고    scopus 로고
    • Characterization of the biofilm forming ability of Staphylococcus pseudintermedius from dogs
    • Singh, A., Walker, M., Rousseau, J. & Weese, J. S. Characterization of the biofilm forming ability of Staphylococcus pseudintermedius from dogs. BMC Vet. Res. 9, 93 (2013).
    • (2013) BMC Vet. Res. , vol.9 , pp. 93
    • Singh, A.1    Walker, M.2    Rousseau, J.3    Weese, J.S.4
  • 62
    • 77956938332 scopus 로고    scopus 로고
    • Biofilm formation and the food industry, a focus on the bacterial outer surface
    • Houdt, V. & Michiels, C. W. Biofilm formation and the food industry, a focus on the bacterial outer surface. J. Appl. Microbiol. 109, 1117-1131 (2010).
    • (2010) J. Appl. Microbiol. , vol.109 , pp. 1117-1131
    • Houdt, V.1    Michiels, C.W.2
  • 63
    • 84945299639 scopus 로고    scopus 로고
    • Biofilm-forming abilities of Listeria monocytogenes serotypes isolated from different sources
    • e0137046 26360831 4567129
    • Doijad, S. P. et al. Biofilm-forming abilities of Listeria monocytogenes serotypes isolated from different sources. PLoS One 10, e0137046 (2015).
    • (2015) PLoS One , vol.10
    • Doijad, S.P.1
  • 64
    • 84958267920 scopus 로고    scopus 로고
    • Genes involved in Listeria monocytogenes biofilm formation at a simulated food processing plant temperature of 15°C
    • Piercey, M. J., Hingston, P. A. & Truelstrup Hansen, L. Genes involved in Listeria monocytogenes biofilm formation at a simulated food processing plant temperature of 15°C. Int. J. Food Microbiol. 223, 63-74 (2016).
    • (2016) Int. J. Food Microbiol. , vol.223 , pp. 63-74
    • Piercey, M.J.1    Hingston, P.A.2    Truelstrup Hansen, L.3
  • 65
    • 71049125198 scopus 로고    scopus 로고
    • Biofilm formation by Listeria monocytogenes on stainless steel surface and biotransfer potential
    • de Oliveira, M. M., Brugnera, D. F., Alves, E. & Piccoli, R. H. Biofilm formation by Listeria monocytogenes on stainless steel surface and biotransfer potential. Braz. J. Microbiol. 41, 97-106 (2010).
    • (2010) Braz. J. Microbiol. , vol.41 , pp. 97-106
    • De Oliveira, M.M.1    Brugnera, D.F.2    Alves, E.3    Piccoli, R.H.4
  • 66
    • 84880731515 scopus 로고    scopus 로고
    • Role of a GntR-family response regulator LbrA in Listeria monocytogenes biofilm formation
    • e70448 1:CAS:528:DC%2BC3sXht1ersb%2FM 23894658 3720924
    • Wassinger, A. et al. Role of a GntR-family response regulator LbrA in Listeria monocytogenes biofilm formation. PLoS One 8, e70448 (2013).
    • (2013) PLoS One , vol.8
    • Wassinger, A.1
  • 67
    • 33745464169 scopus 로고    scopus 로고
    • Listeria monocytogenes: Biofilm Formation and Persistence in Food-processing Environments
    • Møretrø, T. & Langsrud, S. Listeria monocytogenes: Biofilm Formation and Persistence in Food-processing Environments. Biofilms 1, 107-121 (2004).
    • (2004) Biofilms , vol.1 , pp. 107-121
    • Møretrø, T.1    Langsrud, S.2
  • 68
    • 85006829760 scopus 로고    scopus 로고
    • A bioengineered nisin derivative, M21A, in combination with food grade additives eradicates biofilms of Listeria monocytogenes
    • Smith, M. K. et al. A bioengineered nisin derivative, M21A, in combination with food grade additives eradicates biofilms of Listeria monocytogenes. Front. Microbiol. 7, 1939 (2016).
    • (2016) Front. Microbiol. , vol.7 , pp. 1939
    • Smith, M.K.1
  • 69
    • 79952004316 scopus 로고    scopus 로고
    • Resistance to benzalkonium chloride, peracetic acid and nisin during formation of mature biofilms by Listeria monocytogenes
    • Saá Ibusquiza, P., Herrera, J. J. & Cabo, M. L. Resistance to benzalkonium chloride, peracetic acid and nisin during formation of mature biofilms by Listeria monocytogenes. Food Microbiol. 28, 418-425 (2011).
    • (2011) Food Microbiol. , vol.28 , pp. 418-425
    • Saá Ibusquiza, P.1    Herrera, J.J.2    Cabo, M.L.3
  • 70
    • 85006635362 scopus 로고    scopus 로고
    • Inhibition of Listeria monocytogenes biofilms by bacteriocin-producing bacteria isolated from mushroom substrate
    • Bolocan, A. S. et al. Inhibition of Listeria monocytogenes biofilms by bacteriocin-producing bacteria isolated from mushroom substrate. J. Appl. Microbiol. 122, 279-293 (2017).
    • (2017) J. Appl. Microbiol. , vol.122 , pp. 279-293
    • Bolocan, A.S.1
  • 71
    • 74649085754 scopus 로고    scopus 로고
    • The effect of nisin on biofilm forming foodborne bacteria using microtiter plate method
    • Mahdavi, M., Jalali, M. & Kermanshahi, R. K. The effect of nisin on biofilm forming foodborne bacteria using microtiter plate method. Res. Pharm. Sci. 2, 113-118 (2007).
    • (2007) Res. Pharm. Sci. , vol.2 , pp. 113-118
    • Mahdavi, M.1    Jalali, M.2    Kermanshahi, R.K.3
  • 72
    • 84863271387 scopus 로고    scopus 로고
    • Effects of nisin and acid on the inactivation and recovery of Listeria monocytogenes biofilms treated by high hydrostatic pressure
    • Gou, J., Jung, L.-S., Lee, S.-H. & Ahn, J. Effects of nisin and acid on the inactivation and recovery of Listeria monocytogenes biofilms treated by high hydrostatic pressure. Food Sci. Biotechnol. 20, 1361-1366 (2011).
    • (2011) Food Sci. Biotechnol. , vol.20 , pp. 1361-1366
    • Gou, J.1    Jung, L.S.2    Lee, S.H.3    Ahn, J.4
  • 73
    • 84997206809 scopus 로고    scopus 로고
    • Synergistic nisin-polymyxin combinations for the control of Pseudomonas biofilm formation
    • Field, D., Seisling, N., Cotter, P. D., Ross, R. P. & Hill, C. Synergistic nisin-polymyxin combinations for the control of Pseudomonas biofilm formation. Front. Microbiol. 7, 1713 (2016b).
    • (2016) Front. Microbiol. , vol.7 , pp. 1713
    • Field, D.1    Seisling, N.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 74
    • 84926432199 scopus 로고    scopus 로고
    • The formation of biofilms by Pseudomonas aeruginosa: A review of the natural and synthetic compounds interfering with control mechanisms
    • Rasamiravaka, T., Labtani, Q., Duez, P. & El Jaziri, M. The formation of biofilms by Pseudomonas aeruginosa: A review of the natural and synthetic compounds interfering with control mechanisms. Biomed. Res. Int. 2015, 759348 (2015).
    • (2015) Biomed. Res. Int. , vol.2015 , pp. 759348
    • Rasamiravaka, T.1    Labtani, Q.2    Duez, P.3    El Jaziri, M.4
  • 75
    • 84891736535 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa biofilm: Potential therapeutic targets
    • Sharma, G. et al. Pseudomonas aeruginosa biofilm: potential therapeutic targets. Biologicals 42, 1-7 (2014).
    • (2014) Biologicals , vol.42 , pp. 1-7
    • Sharma, G.1
  • 76
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67, 593-656 (2003).
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 77
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 56, 395-411 (1992).
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1
  • 78
    • 0017119987 scopus 로고
    • Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides
    • Morrison, D. C. & Jacobs, D. M. Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides. Immunochemistry 13, 813-818 (1976).
    • (1976) Immunochemistry , vol.13 , pp. 813-818
    • Morrison, D.C.1    Jacobs, D.M.2
  • 79
    • 0029870193 scopus 로고    scopus 로고
    • Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A
    • Srimal, S., Surolia, N., Balasubramanian, S. & Surolia, A. Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A. Biochem. J. 315, 679-686 (1996).
    • (1996) Biochem. J. , vol.315 , pp. 679-686
    • Srimal, S.1    Surolia, N.2    Balasubramanian, S.3    Surolia, A.4
  • 80
    • 0031050613 scopus 로고    scopus 로고
    • The bacterial outer membrane as a drug barrier
    • Hancock, R. E. The bacterial outer membrane as a drug barrier. Trends Microbiol. 5, 37-42 (1997).
    • (1997) Trends Microbiol. , vol.5 , pp. 37-42
    • Hancock, R.E.1
  • 81
    • 0032739820 scopus 로고    scopus 로고
    • In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa
    • Giacometti, A., Cirioni, O., Barchiesi, F., Fortuna, M. & Scalise, G. In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa. J. Antimicrob. Chemother. 44, 641-645 (1999).
    • (1999) J. Antimicrob. Chemother. , vol.44 , pp. 641-645
    • Giacometti, A.1    Cirioni, O.2    Barchiesi, F.3    Fortuna, M.4    Scalise, G.5
  • 82
    • 77953860547 scopus 로고    scopus 로고
    • Nisin A and Polymyxin B as Synergistic inhibitors of Gram-positive and Gram-negative bacteria
    • Naghmouchi, K., Drider, D., Baah, J. & Teather, R. Nisin A and Polymyxin B as Synergistic inhibitors of Gram-positive and Gram-negative bacteria. Probiotics Antimicrob. Proteins 2, 98-103 (2010).
    • (2010) Probiotics Antimicrob. Proteins , vol.2 , pp. 98-103
    • Naghmouchi, K.1    Drider, D.2    Baah, J.3    Teather, R.4
  • 83
    • 79952107129 scopus 로고    scopus 로고
    • Antibacterial activity of class i and IIa bacteriocins combined with polymyxin e against resistant variants of Listeria monocytogenes and Escherichia coli
    • Naghmouchi, K., Belguesmia, Y., Baah, J., Teather, R. & Drider, D. Antibacterial activity of class I and IIa bacteriocins combined with polymyxin E against resistant variants of Listeria monocytogenes and Escherichia coli. Res. Microbiol. 162, 99-107 (2011).
    • (2011) Res. Microbiol. , vol.162 , pp. 99-107
    • Naghmouchi, K.1    Belguesmia, Y.2    Baah, J.3    Teather, R.4    Drider, D.5
  • 84
    • 34247237888 scopus 로고    scopus 로고
    • Dental plaque as a biofilm and a microbial community-implications for health and disease
    • S14 16934115 2147593
    • Marsh, P. D. Dental plaque as a biofilm and a microbial community-implications for health and disease. BMC Oral Health 6, S14 (2006).
    • (2006) BMC Oral Health , vol.6
    • Marsh, P.D.1
  • 87
    • 77949759705 scopus 로고    scopus 로고
    • Oral biofilm architecture on natural teeth
    • e9321 20195365 2827546
    • Zijnge, V. et al. Oral biofilm architecture on natural teeth. PLoS One 5, e9321 (2010).
    • (2010) PLoS One , vol.5
    • Zijnge, V.1
  • 89
    • 51949093305 scopus 로고    scopus 로고
    • Characteristics of biofilm formation by Streptococcus mutans in the presence of saliva
    • Ahn, S. J., Wen, Z. T., Brady, L. J. & Burne, R. A. Characteristics of biofilm formation by Streptococcus mutans in the presence of saliva. Infect. Immun. 76, 4259-4268 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 4259-4268
    • Ahn, S.J.1    Wen, Z.T.2    Brady, L.J.3    Burne, R.A.4
  • 90
    • 42149138458 scopus 로고    scopus 로고
    • Periodontitis is associated with a loss of colonization by Streptococcus sanguinis
    • Stingu, C. S., Eschrich, K., Rodloff, A. C., Schaumann, R. & Jentsch, H. Periodontitis is associated with a loss of colonization by Streptococcus sanguinis. J. Med. Microbiol. 57, 495-499 (2008).
    • (2008) J. Med. Microbiol. , vol.57 , pp. 495-499
    • Stingu, C.S.1    Eschrich, K.2    Rodloff, A.C.3    Schaumann, R.4    Jentsch, H.5
  • 91
    • 79953218389 scopus 로고    scopus 로고
    • Inhibition of Streptococcus mutans biofilm formation by Streptococcus salivarius FruA
    • Ogawa, A. et al. Inhibition of Streptococcus mutans biofilm formation by Streptococcus salivarius FruA. Appl. Environ. Microbiol. 77, 1572-1580 (2011).
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1572-1580
    • Ogawa, A.1
  • 92
    • 84927167545 scopus 로고    scopus 로고
    • Metabolic activity of Streptococcus mutans biofilms and gene expression during exposure to xylitol and sucrose
    • Decker, E. M., Klein, C., Schwindt, D. & von Ohle, C. Metabolic activity of Streptococcus mutans biofilms and gene expression during exposure to xylitol and sucrose. Int. J. Oral Sci. 6, 195-204 (2014).
    • (2014) Int. J. Oral Sci. , vol.6 , pp. 195-204
    • Decker, E.M.1    Klein, C.2    Schwindt, D.3    Von Ohle, C.4
  • 93
    • 77954868440 scopus 로고    scopus 로고
    • Damage of Streptococcus mutans biofilms by carolacton, a secondary metabolite from the myxobacterium Sorangium cellulosum
    • Kunze, B. et al. Damage of Streptococcus mutans biofilms by carolacton, a secondary metabolite from the myxobacterium Sorangium cellulosum. BMC Microbiol. 10, 199 (2010).
    • (2010) BMC Microbiol. , vol.10 , pp. 199
    • Kunze, B.1
  • 94
    • 85022178969 scopus 로고    scopus 로고
    • Effect of commonly prescribed liquid medications on Streptococcus mutans biofilm. An in vitro study
    • Clark, S. A., Vinson, L. A., Eckert, G. & Gregory, R. L. Effect of commonly prescribed liquid medications on Streptococcus mutans biofilm. An in vitro study. J. Clin. Pediatr. Dent. 41, 141-146 (2017).
    • (2017) J. Clin. Pediatr. Dent. , vol.41 , pp. 141-146
    • Clark, S.A.1    Vinson, L.A.2    Eckert, G.3    Gregory, R.L.4
  • 95
    • 84903318216 scopus 로고    scopus 로고
    • An in vitro study on the effect of free amino acids alone or in combination with nisin on biofilms as well as on planktonic bacteria of Streptococcus mutans
    • e99513 24936873 4060998
    • Tong, Z. et al. An in vitro study on the effect of free amino acids alone or in combination with nisin on biofilms as well as on planktonic bacteria of Streptococcus mutans. PLoS One 9, e99513 (2014).
    • (2014) PLoS One , vol.9
    • Tong, Z.1
  • 96
    • 84872462787 scopus 로고    scopus 로고
    • Sustainable inhibition efficacy of liposome-encapsulated nisin on insoluble glucan-biofilm synthesis by Streptococcus mutans
    • Yamakami, K. et al. Sustainable inhibition efficacy of liposome-encapsulated nisin on insoluble glucan-biofilm synthesis by Streptococcus mutans. Pharm. Biol. 51, 267-270 (2013).
    • (2013) Pharm. Biol. , vol.51 , pp. 267-270
    • Yamakami, K.1
  • 97
    • 79959188632 scopus 로고    scopus 로고
    • Antimicrobial penetration and efficacy in an in vitro oral biofilm model
    • Corbin, A., Pitts, B., Parker, A. & Stewart, P. S. Antimicrobial penetration and efficacy in an in vitro oral biofilm model. Antimicrob. Agents Chemother. 55, 3338-3344 (2011).
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3338-3344
    • Corbin, A.1    Pitts, B.2    Parker, A.3    Stewart, P.S.4
  • 98
    • 81255157519 scopus 로고    scopus 로고
    • Impact of the broad-spectrum antimicrobial peptide, lacticin 3147, on Streptococcus mutans growing in a biofilm and in human saliva
    • Dobson, A., O'Connor, P. M., Cotter, P. D., Ross, R. P. & Hill, C. Impact of the broad-spectrum antimicrobial peptide, lacticin 3147, on Streptococcus mutans growing in a biofilm and in human saliva. J. Appl. Microbiol. 111, 1515-1523 (2011).
    • (2011) J. Appl. Microbiol. , vol.111 , pp. 1515-1523
    • Dobson, A.1    O'Connor, P.M.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 99
    • 84876668690 scopus 로고    scopus 로고
    • The effect of MTADN on 10 Enterococcus faecalis isolates and biofilm: An in vitro study
    • Tong, Z., Ling, J., Lin, Z., Li, X. & Mu, Y. The effect of MTADN on 10 Enterococcus faecalis isolates and biofilm: An in vitro study. J. Endod. 39, 674-678 (2013).
    • (2013) J. Endod. , vol.39 , pp. 674-678
    • Tong, Z.1    Ling, J.2    Lin, Z.3    Li, X.4    Mu, Y.5
  • 100
    • 84865776527 scopus 로고    scopus 로고
    • Enterococcus faecalis produces abundant extracellular structures containing DNA in the absence of cell lysis during early biofilm formation
    • Barnes, A. M., Ballering, K. S., Leibman, R. S., Wells, C. L. & Dunny, G. M. Enterococcus faecalis produces abundant extracellular structures containing DNA in the absence of cell lysis during early biofilm formation. mBio 3, e00193-00112 (2012).
    • (2012) MBio , vol.3 , pp. e00193-e00112
    • Barnes, A.M.1    Ballering, K.S.2    Leibman, R.S.3    Wells, C.L.4    Dunny, G.M.5
  • 101
    • 37249055056 scopus 로고    scopus 로고
    • Biofilm formation by enterococci
    • Mohamed, J. A. & Huang, D. B. Biofilm formation by enterococci. J. Med. Microbiol. 56, 1581-1588 (2007).
    • (2007) J. Med. Microbiol. , vol.56 , pp. 1581-1588
    • Mohamed, J.A.1    Huang, D.B.2
  • 102
    • 0346435112 scopus 로고    scopus 로고
    • Esp-independent biofilm formation by Enterococcus faecalis
    • Kristich, C. J., Li, Y. H., Cvitkovitch, D. G. & Dunny, G. M. Esp-independent biofilm formation by Enterococcus faecalis. J. Bacteriol. 186, 154-163 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 154-163
    • Kristich, C.J.1    Li, Y.H.2    Cvitkovitch, D.G.3    Dunny, G.M.4
  • 103
    • 34250162489 scopus 로고    scopus 로고
    • Biofilm formation of oral and endodontic Enterococcus faecalis
    • Duggan, J. M. & Sedgley, C. M. Biofilm formation of oral and endodontic Enterococcus faecalis. J. Endod. 33, 815-818 (2007).
    • (2007) J. Endod. , vol.33 , pp. 815-818
    • Duggan, J.M.1    Sedgley, C.M.2
  • 104
    • 85018177679 scopus 로고    scopus 로고
    • High-purity nisin alone or in combination with sodium hypochlorite is effective against planktonic and biofilm populations of Enterococcus faecalis
    • Kajwadkar, R. et al. High-purity nisin alone or in combination with sodium hypochlorite is effective against planktonic and biofilm populations of Enterococcus faecalis. J. Endod. 43, 989-994 (2017).
    • (2017) J. Endod. , vol.43 , pp. 989-994
    • Kajwadkar, R.1
  • 105
    • 69149109941 scopus 로고    scopus 로고
    • Actinomyces naeslundii in initial dental biofilm formation
    • Dige, I., Raarup, M. K., Nyengaard, J. R., Kilian, M. & Nyvad, B. Actinomyces naeslundii in initial dental biofilm formation. Microbiology 155, 2116-2126 (2009).
    • (2009) Microbiology , vol.155 , pp. 2116-2126
    • Dige, I.1    Raarup, M.K.2    Nyengaard, J.R.3    Kilian, M.4    Nyvad, B.5
  • 106
    • 9644259073 scopus 로고    scopus 로고
    • Identification of early microbial colonizers in human dental biofilm
    • Li, J. et al. Identification of early microbial colonizers in human dental biofilm. J. Appl. Microbiol. 97, 1311-1318 (2004).
    • (2004) J. Appl. Microbiol. , vol.97 , pp. 1311-1318
    • Li, J.1
  • 107
    • 80053910660 scopus 로고    scopus 로고
    • Bacterial interactions in dental biofilm
    • Huang, R., Li, M. & Gregory, R. L. Bacterial interactions in dental biofilm. Virulence 2, 435-444 (2011).
    • (2011) Virulence , vol.2 , pp. 435-444
    • Huang, R.1    Li, M.2    Gregory, R.L.3
  • 108
    • 0035257112 scopus 로고    scopus 로고
    • Endocarditis due to Actinomyces viscosus
    • Mardis, J. S. & Many, W. J. Jr. Endocarditis due to Actinomyces viscosus. South Med. J. 94, 240-243 (2001).
    • (2001) South Med. J. , vol.94 , pp. 240-243
    • Mardis, J.S.1    Many, W.J.2
  • 109
    • 84923871175 scopus 로고    scopus 로고
    • Combined effect of a mixture of tetracycline, acid, and detergent, and nisin against Enterococcus faecalis and Actinomyces viscosus biofilms
    • Balto, H. A., Shakoor, Z. A. & Kanfar, M. A. Combined effect of a mixture of tetracycline, acid, and detergent, and nisin against Enterococcus faecalis and Actinomyces viscosus biofilms. Saudi. Med. J. 36, 211-215 (2015).
    • (2015) Saudi. Med. J. , vol.36 , pp. 211-215
    • Balto, H.A.1    Shakoor, Z.A.2    Kanfar, M.A.3
  • 110
    • 85018424186 scopus 로고    scopus 로고
    • Enterococcus faecalis bacteriocin EntV inhibits hyphal morphogenesis, biofilm formation, and virulence of Candida albicans
    • Graham, C. E., Cruz, M. R., Garsin, D. A. & Lorenz, M. C. Enterococcus faecalis bacteriocin EntV inhibits hyphal morphogenesis, biofilm formation, and virulence of Candida albicans. Proc. Natl. Acad. Sci. USA 114, 4507-4512 (2017).
    • (2017) Proc. Natl. Acad. Sci. USA , vol.114 , pp. 4507-4512
    • Graham, C.E.1    Cruz, M.R.2    Garsin, D.A.3    Lorenz, M.C.4
  • 112
    • 77950675511 scopus 로고    scopus 로고
    • Candida infections of the genitourinary tract
    • Achkar, J. M. & Fries, B. C. Candida infections of the genitourinary tract. Clin. Microbiol. Rev. 23, 253-273 (2010).
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 253-273
    • Achkar, J.M.1    Fries, B.C.2
  • 113
    • 84940063644 scopus 로고    scopus 로고
    • Sonorensin: A new bacteriocin with potential of an anti-biofilm agent and a food biopreservative
    • Chopra, L., Singh, G., Kumar Jena, K. & Sahoo, D. K. Sonorensin: A new bacteriocin with potential of an anti-biofilm agent and a food biopreservative. Sci. Rep. 5, 13412 (2015).
    • (2015) Sci. Rep. , vol.5
    • Chopra, L.1    Singh, G.2    Kumar Jena, K.3    Sahoo, D.K.4
  • 114
    • 84899122716 scopus 로고    scopus 로고
    • Sonorensin: An antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93
    • Chopra, L., Singh, G., Choudhary, V. & Sahoo, D. K. Sonorensin: An antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93. Appl. Environ. Microbiol. 80, 2981-2990 (2014).
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 2981-2990
    • Chopra, L.1    Singh, G.2    Choudhary, V.3    Sahoo, D.K.4
  • 115
    • 84875769766 scopus 로고    scopus 로고
    • Combined treatments of enterocin AS-48 with biocides to improve the inactivation of methicillin-sensitive and methicillin-resistant Staphylococcus aureus planktonic and sessile cells
    • Caballero Gómez, N., Abriouel, H., Grande, M. J., Pérez Pulido, R. & Gálvez, A. Combined treatments of enterocin AS-48 with biocides to improve the inactivation of methicillin-sensitive and methicillin-resistant Staphylococcus aureus planktonic and sessile cells. Int. J. Food Microbiol. 163, 96-100 (2013a).
    • (2013) Int. J. Food Microbiol. , vol.163 , pp. 96-100
    • Caballero Gómez, N.1    Abriouel, H.2    Grande, M.J.3    Pérez Pulido, R.4    Gálvez, A.5
  • 116
    • 84897099450 scopus 로고    scopus 로고
    • Analysis of the promoters involved in enterocin AS-48 expression
    • e90603 24594763 3942455
    • Cebrián, R. et al. Analysis of the promoters involved in enterocin AS-48 expression. PLoS One 9, e90603 (2014).
    • (2014) PLoS One , vol.9
    • Cebrián, R.1
  • 117
    • 84937611659 scopus 로고    scopus 로고
    • The cyclic antibacterial peptide enterocin AS-48: Isolation, mode of action, and possible food applications
    • Grande Burgos, M. J., Pulido, R. P., Del Carmen López Aguayo, M., Gálvez, A. & Lucas, R. The cyclic antibacterial peptide enterocin AS-48: isolation, mode of action, and possible food applications. Int. J. Mol. Sci. 15, 22706-22727 (2014).
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 22706-22727
    • Grande Burgos, M.J.1    Pulido, R.P.2    Del Carmen López Aguayo, M.3    Gálvez, A.4    Lucas, R.5
  • 118
    • 84973527479 scopus 로고    scopus 로고
    • Anti-MRSA activities of enterocins DD28 and DD93 and evidences on their role in the inhibition of biofilm formation
    • Al-Atya, A. K. et al. Anti-MRSA activities of enterocins DD28 and DD93 and evidences on their role in the inhibition of biofilm formation. Front. Microbiol. 7, 817 (2016a).
    • (2016) Front. Microbiol. , vol.7 , pp. 817
    • Al-Atya, A.K.1
  • 119
    • 85041634586 scopus 로고    scopus 로고
    • Hyicin 4244, the first sactibiotic described in staphylococci, exhibits an anti-staphylococcal biofilm activity
    • Duarte, A. F. S. et al. Hyicin 4244, the first sactibiotic described in staphylococci, exhibits an anti-staphylococcal biofilm activity. Int. J. Antimicrob. Agents. https://doi.org/10.1016/j.ijantimicag.2017.06.025 (2017).
    • (2017) Int. J. Antimicrob. Agents
    • Duarte, A.F.S.1
  • 120
    • 84885811524 scopus 로고    scopus 로고
    • Comparative proteomic analysis of Listeria monocytogenes exposed to enterocin AS-48 in planktonic and sessile states
    • Caballero Gómez, N., Abriouel, H., Ennahar, S. & Gálvez, A. Comparative proteomic analysis of Listeria monocytogenes exposed to enterocin AS-48 in planktonic and sessile states. Int. J. Food Microbiol. 167, 202-207 (2013b).
    • (2013) Int. J. Food Microbiol. , vol.167 , pp. 202-207
    • Caballero Gómez, N.1    Abriouel, H.2    Ennahar, S.3    Gálvez, A.4
  • 121
    • 84856042214 scopus 로고    scopus 로고
    • Effect of enterocin AS-48 in combination with biocides on planktonic and sessile Listeria monocytogenes
    • Gómez, N. C., Abriouel, H., Grande, M. A., Pulido, R. P. & Gálvez, A. Effect of enterocin AS-48 in combination with biocides on planktonic and sessile Listeria monocytogenes. Food Microbiol. 30, 51-58 (2012).
    • (2012) Food Microbiol. , vol.30 , pp. 51-58
    • Gómez, N.C.1    Abriouel, H.2    Grande, M.A.3    Pulido, R.P.4    Gálvez, A.5
  • 122
    • 85002824950 scopus 로고    scopus 로고
    • Licheniocin 50.2 and bacteriocins from Lactococcus lactis subsp. lactis biovar. diacetylactis BGBU1-4 inhibit biofilms of coagulase negative staphylococci and Listeria monocytogenes clinical isolates
    • e0167995 27930711 5145223
    • Cirkovic, I. et al. Licheniocin 50.2 and bacteriocins from Lactococcus lactis subsp. lactis biovar. diacetylactis BGBU1-4 inhibit biofilms of coagulase negative staphylococci and Listeria monocytogenes clinical isolates. PLoS One 11, e0167995 (2016).
    • (2016) PLoS One , vol.11
    • Cirkovic, I.1
  • 124
    • 0029792827 scopus 로고    scopus 로고
    • Association of biofilm production of coagulase-negative staphylococci with expression of a specific polysaccharide intercellular adhesin
    • Mack, D., Haeder, M., Siemssen, N. & Laufs, R. Association of biofilm production of coagulase-negative staphylococci with expression of a specific polysaccharide intercellular adhesin. J. Infect. Dis. 174, 881-884 (1996).
    • (1996) J. Infect. Dis. , vol.174 , pp. 881-884
    • Mack, D.1    Haeder, M.2    Siemssen, N.3    Laufs, R.4
  • 125
    • 84904741340 scopus 로고    scopus 로고
    • Biofilm formation by coagulase-negative staphylococci: Impact on the efficacy of antimicrobials and disinfectants commonly used on dairy farms
    • Tremblay, Y. D., Caron, V., Blondeau, A., Messier, S. & Jacques, M. Biofilm formation by coagulase-negative staphylococci: impact on the efficacy of antimicrobials and disinfectants commonly used on dairy farms. Vet. Microbiol. 172, 511-518 (2014).
    • (2014) Vet. Microbiol. , vol.172 , pp. 511-518
    • Tremblay, Y.D.1    Caron, V.2    Blondeau, A.3    Messier, S.4    Jacques, M.5
  • 126
    • 58049189351 scopus 로고    scopus 로고
    • Bacterial biofilms with emphasis on coagulase-negative staphylococci
    • Oliveira, A. & Cunha, M. L. R. S. Bacterial biofilms with emphasis on coagulase-negative staphylococci. J. Venom. Anim. Toxins Incl. Trop. Dis. 14, 572-596 (2008).
    • (2008) J. Venom. Anim. Toxins Incl. Trop. Dis. , vol.14 , pp. 572-596
    • Oliveira, A.1    Cunha, M.L.R.S.2
  • 127
    • 84983448208 scopus 로고    scopus 로고
    • Effects of colistin and bacteriocins combinations on the in vitro growth of Escherichia coli strains from swine origin
    • Al-Atya, A. K. et al. Effects of colistin and bacteriocins combinations on the in vitro growth of Escherichia coli strains from swine origin. Probiotics Antimicrob. Proteins 8, 183-190 (2016b).
    • (2016) Probiotics Antimicrob. Proteins , vol.8 , pp. 183-190
    • Al-Atya, A.K.1
  • 128
    • 85011628978 scopus 로고    scopus 로고
    • The safe enterocin DD14 is a leaderless two-peptide bacteriocin with anti-Clostridium perfringens activity
    • Caly, D. L. et al. The safe enterocin DD14 is a leaderless two-peptide bacteriocin with anti-Clostridium perfringens activity. Int. J. Antimicrob. Agents 49, 282-289 (2017).
    • (2017) Int. J. Antimicrob. Agents , vol.49 , pp. 282-289
    • Caly, D.L.1
  • 130
    • 84867287307 scopus 로고    scopus 로고
    • Susceptibility of Gardnerella vaginalis biofilms to natural antimicrobials subtilosin, ϵ-poly-L-lysine, and lauramide arginine ethyl ester
    • Turovskiy, Y. et al. Susceptibility of Gardnerella vaginalis biofilms to natural antimicrobials subtilosin, ϵ-poly-L-lysine, and lauramide arginine ethyl ester. Dis. Obstet. Gynecol. 2012, 284762 (2012).
    • (2012) Dis. Obstet. Gynecol. , vol.2012 , pp. 284762
    • Turovskiy, Y.1
  • 131
    • 34547580161 scopus 로고    scopus 로고
    • Effect of biofilm phenotype on resistance of Gardnerella vaginalis to hydrogen peroxide and lactic acid
    • Patterson, J. L., Girerd, P. H., Karjane, N. W. & Jefferson, K. K. Effect of biofilm phenotype on resistance of Gardnerella vaginalis to hydrogen peroxide and lactic acid. Am. J. Obstet. Gynecol. 197, 170.e1-7 (2007).
    • (2007) Am. J. Obstet. Gynecol. , vol.197 , pp. 170e1-1707
    • Patterson, J.L.1    Girerd, P.H.2    Karjane, N.W.3    Jefferson, K.K.4
  • 132
    • 76449088351 scopus 로고    scopus 로고
    • Analysis of adherence, biofilm formation and cytotoxicity suggests a greater virulence potential of Gardnerella vaginalis relative to other bacterial-vaginosis-Associated anaerobes
    • Patterson, J. L., Stull-Lane, A., Girerd, P. H. & Jefferson, K. K. Analysis of adherence, biofilm formation and cytotoxicity suggests a greater virulence potential of Gardnerella vaginalis relative to other bacterial-vaginosis-Associated anaerobes. Microbiology 156, 392-399 (2010).
    • (2010) Microbiology , vol.156 , pp. 392-399
    • Patterson, J.L.1    Stull-Lane, A.2    Girerd, P.H.3    Jefferson, K.K.4
  • 133
    • 85001013318 scopus 로고    scopus 로고
    • Subtilosin prevents biofilm formation by inhibiting bacterial quorum sensing
    • Algburi, A. et al. Subtilosin prevents biofilm formation by inhibiting bacterial quorum sensing. Probiotics Antimicrob. Proteins 9, 81-90 (2017).
    • (2017) Probiotics Antimicrob. Proteins , vol.9 , pp. 81-90
    • Algburi, A.1
  • 134
    • 84876191394 scopus 로고    scopus 로고
    • Effects of the peptide pheromone plantaricin A and cocultivation with Lactobacillus sanfranciscensis DPPMA174 on the exoproteome and the adhesion capacity of Lactobacillus plantarum DC400
    • Calasso, M. et al. Effects of the peptide pheromone plantaricin A and cocultivation with Lactobacillus sanfranciscensis DPPMA174 on the exoproteome and the adhesion capacity of Lactobacillus plantarum DC400. Appl. Environ. Microbiol. 79, 2657-2669 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 2657-2669
    • Calasso, M.1
  • 135
    • 84996555433 scopus 로고    scopus 로고
    • Enterocin B3A-B3B produced by LAB collected from infant faeces: Potential utilization in the food industry for Listeria monocytogenes biofilm management
    • Al-Seraih, A. et al. Enterocin B3A-B3B produced by LAB collected from infant faeces: potential utilization in the food industry for Listeria monocytogenes biofilm management. Antonie Van Leeuwenhoek 110, 205-219 (2017).
    • (2017) Antonie van Leeuwenhoek , vol.110 , pp. 205-219
    • Al-Seraih, A.1
  • 136
    • 77953083340 scopus 로고    scopus 로고
    • Control of biofilm formation by poly-ethylene-co-vinyl acetate films incorporating nisin
    • Nostro, A. et al. Control of biofilm formation by poly-ethylene-co-vinyl acetate films incorporating nisin. Appl. Microbiol. Biotechnol. 87, 729-737 (2010).
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 729-737
    • Nostro, A.1
  • 137
    • 79953732148 scopus 로고    scopus 로고
    • Covalent immobilization of nisin on multi-walled carbon nanotubes: Superior antimicrobial and anti-biofilm properties
    • Qi, X. et al. Covalent immobilization of nisin on multi-walled carbon nanotubes: superior antimicrobial and anti-biofilm properties. Nanoscale 3, 1874-1880 (2011).
    • (2011) Nanoscale , vol.3 , pp. 1874-1880
    • Qi, X.1
  • 138
    • 84915790922 scopus 로고    scopus 로고
    • Inhibitory effects of nisin-coated multi-walled carbon nanotube sheet on biofilm formation from Bacillus anthracisspores
    • Dong, X., McCoy, E., Zhang, M. & Yang, L. Inhibitory effects of nisin-coated multi-walled carbon nanotube sheet on biofilm formation from Bacillus anthracisspores. J. Environ. Sci. (China) 26, 2526-2534 (2014).
    • (2014) J. Environ. Sci. (China) , vol.26 , pp. 2526-2534
    • Dong, X.1    McCoy, E.2    Zhang, M.3    Yang, L.4
  • 139
    • 34250771554 scopus 로고    scopus 로고
    • Phenotypic and functional characterization of Bacillus anthracis biofilms
    • Lee, K. et al. Phenotypic and functional characterization of Bacillus anthracis biofilms. Microbiology 153, 1693-1701 (2007).
    • (2007) Microbiology , vol.153 , pp. 1693-1701
    • Lee, K.1
  • 140
    • 84925517694 scopus 로고    scopus 로고
    • Nisin incorporated with 2,3-dihydroxybenzoic acid in nanofibers inhibits biofilm formation by a methicillin-resistant strain of Staphylococcus aureus
    • Ahire, J. J. & Dicks, L. M. Nisin incorporated with 2,3-dihydroxybenzoic acid in nanofibers inhibits biofilm formation by a methicillin-resistant strain of Staphylococcus aureus. Probiotics. Antimicrob. Proteins 7, 52-59 (2015).
    • (2015) Probiotics. Antimicrob. Proteins , vol.7 , pp. 52-59
    • Ahire, J.J.1    Dicks, L.M.2
  • 141
    • 79952815718 scopus 로고    scopus 로고
    • Optimized grafting of antimicrobial peptides on stainless steel surface and biofilm resistance tests
    • Héquet, A., Humblot, V., Berjeaud, J. M. & Pradier, C. M. Optimized grafting of antimicrobial peptides on stainless steel surface and biofilm resistance tests. Colloids Surf. B Biointerfaces 84, 301-309 (2011).
    • (2011) Colloids Surf. B Biointerfaces , vol.84 , pp. 301-309
    • Héquet, A.1    Humblot, V.2    Berjeaud, J.M.3    Pradier, C.M.4
  • 142
    • 84931287886 scopus 로고    scopus 로고
    • Comparison of antibacterial effects between antimicrobial peptide and bacteriocins isolated from Lactobacillus plantarum on three common pathogenic bacteria
    • Ming, L., Zhang, Q., Yang, L. & Huang, J. A. Comparison of antibacterial effects between antimicrobial peptide and bacteriocins isolated from Lactobacillus plantarum on three common pathogenic bacteria. Int. J. Clin. Exp. Med. 8, 5806-5811 (2015).
    • (2015) Int. J. Clin. Exp. Med. , vol.8 , pp. 5806-5811
    • Ming, L.1    Zhang, Q.2    Yang, L.3    Huang, J.A.4
  • 143
    • 84866035866 scopus 로고    scopus 로고
    • Isolation and identification of a bacteriocin with antibacterial and antibiofilm activity from Citrobacter freundii
    • Shanks, R. M., Dashiff, A., Alster, J. S. & Kadouri, D. E. Isolation and identification of a bacteriocin with antibacterial and antibiofilm activity from Citrobacter freundii. Arch. Microbiol. 194, 575-587 (2012).
    • (2012) Arch. Microbiol. , vol.194 , pp. 575-587
    • Shanks, R.M.1    Dashiff, A.2    Alster, J.S.3    Kadouri, D.E.4
  • 144
    • 84943817547 scopus 로고    scopus 로고
    • Antibiotic resistance related to biofilm formation in Klebsiella pneumoniae
    • Vuotto, C., Longo, F., Balice, M. P., Donelli, G. & Varaldo, P. E. Antibiotic resistance related to biofilm formation in Klebsiella pneumoniae. Pathogens 3, 743-758 (2014).
    • (2014) Pathogens , vol.3 , pp. 743-758
    • Vuotto, C.1    Longo, F.2    Balice, M.P.3    Donelli, G.4    Varaldo, P.E.5
  • 145
    • 84862668535 scopus 로고    scopus 로고
    • Biofilm formation of Klebsiella pneumoniae on urethral catheters requires either type 1 or type 3 fimbriae
    • Stahlhut, S. G., Struve, C., Krogfelt, K. A. & Reisner, A. Biofilm formation of Klebsiella pneumoniae on urethral catheters requires either type 1 or type 3 fimbriae. Fems. Immunol. Med. Microbiol. 65, 350-359 (2012).
    • (2012) Fems. Immunol. Med. Microbiol. , vol.65 , pp. 350-359
    • Stahlhut, S.G.1    Struve, C.2    Krogfelt, K.A.3    Reisner, A.4
  • 146
    • 84975818576 scopus 로고    scopus 로고
    • The inhibitory effect of bacteriocin produced by Lactobacillus acidophilus ATCC 4356 and Lactobacillus plantarum ATCC 8014 on planktonic cells and biofilms of Serratia marcescens
    • Vahedi Shahandashti, R., Kasra Kermanshahi, R. & Ghadam, P. The inhibitory effect of bacteriocin produced by Lactobacillus acidophilus ATCC 4356 and Lactobacillus plantarum ATCC 8014 on planktonic cells and biofilms of Serratia marcescens. Turk. J. Med. Sci. 46, 1188-1196 (2016).
    • (2016) Turk. J. Med. Sci. , vol.46 , pp. 1188-1196
    • Vahedi Shahandashti, R.1    Kasra Kermanshahi, R.2    Ghadam, P.3
  • 147
    • 84858295091 scopus 로고    scopus 로고
    • Serratia marcescens strains implicated in adverse transfusion reactions form biofilms in platelet concentrates and demonstrate reduced detection by automated culture
    • Greco-Stewart, V. S. et al. Serratia marcescens strains implicated in adverse transfusion reactions form biofilms in platelet concentrates and demonstrate reduced detection by automated culture. Vox. Sang. 102, 212-220 (2012).
    • (2012) Vox. Sang. , vol.102 , pp. 212-220
    • Greco-Stewart, V.S.1
  • 148
    • 84859848167 scopus 로고    scopus 로고
    • Inhibition of quorum sensing regulated biofilm formation in Serratia marcescens causing nosocomial infections
    • Bakkiyaraj, D., Sivasankar, C. & Pandian, S. K. Inhibition of quorum sensing regulated biofilm formation in Serratia marcescens causing nosocomial infections. Bioorg. Med. Chem. Lett. 22, 3089-3094 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 3089-3094
    • Bakkiyaraj, D.1    Sivasankar, C.2    Pandian, S.K.3
  • 149
    • 84973121735 scopus 로고    scopus 로고
    • Control of Listeria monocytogenes biofilms on industrial surfaces by the bacteriocin-producing Lactobacillus sakei CRL1862
    • Pérez-Ibarreche, M., Castellano, P., Leclercq, A. & Vignolo, G. Control of Listeria monocytogenes biofilms on industrial surfaces by the bacteriocin-producing Lactobacillus sakei CRL1862. FEMS Microbiol. Lett. https://doi.org/10.1093/femsle/fnw118 (2016).
    • (2016) FEMS Microbiol. Lett.
    • Pérez-Ibarreche, M.1    Castellano, P.2    Leclercq, A.3    Vignolo, G.4
  • 150
    • 40449123710 scopus 로고    scopus 로고
    • Influence of peroxyacetic acid and nisin and coculture with Enterococcus faecium on Listeria monocytogenes biofilm formation
    • Minei, C. C., Gomes, B. C., Ratti, R. P., D'Angelis, C. E. & De Martinis, E. C. Influence of peroxyacetic acid and nisin and coculture with Enterococcus faecium on Listeria monocytogenes biofilm formation. J. Food Prot. 71, 634-638 (2008).
    • (2008) J. Food Prot. , vol.71 , pp. 634-638
    • Minei, C.C.1    Gomes, B.C.2    Ratti, R.P.3    D'Angelis, C.E.4    De Martinis, E.C.5
  • 151
    • 84949551412 scopus 로고    scopus 로고
    • In vitro evaluation of bacteriocins activity against Listeria monocytogenes biofilm formation
    • Camargo, A. C., de Paula, O. A., Todorov, S. D. & Nero, L. A. In vitro evaluation of bacteriocins activity against Listeria monocytogenes biofilm formation. Appl. Biochem. Biotechnol. 178, 1239-1251 (2016).
    • (2016) Appl. Biochem. Biotechnol. , vol.178 , pp. 1239-1251
    • Camargo, A.C.1    De Paula, O.A.2    Todorov, S.D.3    Nero, L.A.4
  • 152
    • 84941422465 scopus 로고    scopus 로고
    • Inhibitory effects of Lactobacillus fermentum on microbial growth and biofilm formation
    • Rybalchenko, O. V., Bondarenko, V. M., Orlova, O. G., Markov, A. G. & Amasheh, S. Inhibitory effects of Lactobacillus fermentum on microbial growth and biofilm formation. Arch. Microbiol. 197, 1027-1032 (2015).
    • (2015) Arch. Microbiol. , vol.197 , pp. 1027-1032
    • Rybalchenko, O.V.1    Bondarenko, V.M.2    Orlova, O.G.3    Markov, A.G.4    Amasheh, S.5
  • 153
    • 0034870709 scopus 로고    scopus 로고
    • Biofilm formation by the fungal pathogen Candida albicans: Development, architecture, and drug resistance
    • Chandra, J. et al. Biofilm formation by the fungal pathogen Candida albicans: development, architecture, and drug resistance. J. Bacteriol. 183, 5385-5394 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 5385-5394
    • Chandra, J.1
  • 154
    • 85016287158 scopus 로고    scopus 로고
    • A novel small molecule inhibitor of Candida albicans biofilm formation, filamentation and virulence with low potential for the development of resistance
    • Pierce, C. G. et al. A novel small molecule inhibitor of Candida albicans biofilm formation, filamentation and virulence with low potential for the development of resistance. NPJ Biofilms Micro. 1, 15012 (2015).
    • (2015) NPJ Biofilms Micro. , vol.1
    • Pierce, C.G.1
  • 155
    • 84919458250 scopus 로고    scopus 로고
    • The effect of five probiotic lactobacilli strains on the growth and biofilm formation of Streptococcus mutans
    • Lin, X., Chen, X., Chen, Y., Jiang, W. & Chen, H. The effect of five probiotic lactobacilli strains on the growth and biofilm formation of Streptococcus mutans. Oral Dis. 21, e128-e134 (2015).
    • (2015) Oral Dis. , vol.21 , pp. e128-e134
    • Lin, X.1    Chen, X.2    Chen, Y.3    Jiang, W.4    Chen, H.5
  • 156
    • 84926435429 scopus 로고    scopus 로고
    • Discovery and development of NVB302, a semisynthetic antibiotic for treatment of Clostridium difficile infection
    • (eds Osbourn, A., Goss, R. J. & Carter, G. T.) Ch. 24 (John Wiley & Sons, 2014).
    • Boakes, S. & Dawson, M. J. Discovery and development of NVB302, a semisynthetic antibiotic for treatment of Clostridium difficile infection. in Natural Products: Discourse, Diversity, and Design 1st edn, Vol. 1 (eds Osbourn, A., Goss, R. J. & Carter, G. T.) Ch. 24 (John Wiley & Sons, 2014).
    • Natural Products: Discourse, Diversity, and Design 1st Edn , vol.1
    • Boakes, S.1    Dawson, M.J.2
  • 157
    • 84867330679 scopus 로고    scopus 로고
    • New horizons for host defense peptides and lantibiotics
    • Dawson, M. J. & Scott, R. W. New horizons for host defense peptides and lantibiotics. Curr. Opin. Pharmacol. 12, 545-550 (2012).
    • (2012) Curr. Opin. Pharmacol. , vol.12 , pp. 545-550
    • Dawson, M.J.1    Scott, R.W.2
  • 158
    • 34250622074 scopus 로고    scopus 로고
    • Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118
    • Corr, S. C. et al. Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118. Proc. Natl. Acad. Sci. USA 104, 7617-7621 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7617-7621
    • Corr, S.C.1
  • 159
    • 84866179166 scopus 로고    scopus 로고
    • Influence of adhesion and bacteriocin production by Lactobacillus salivarius on the intestinal epithelial cell transcriptional response
    • O'Callaghan, J., Buttó, L. F., MacSharry, J., Nally, K. & O'Toole, P. W. Influence of adhesion and bacteriocin production by Lactobacillus salivarius on the intestinal epithelial cell transcriptional response. Appl. Environ. Microbiol. 78, 5196-5203 (2012).
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 5196-5203
    • O'Callaghan, J.1    Buttó, L.F.2    MacSharry, J.3    Nally, K.4    O'Toole, P.W.5
  • 160
    • 70349131189 scopus 로고    scopus 로고
    • Persistence of colicinogenic Escherichia coli in the mouse gastrointestinal tract
    • Gillor, O., Giladi, I. & Riley, M. A. Persistence of colicinogenic Escherichia coli in the mouse gastrointestinal tract. BMC Microbiol. 9, 165 (2009).
    • (2009) BMC Microbiol. , vol.9 , pp. 165
    • Gillor, O.1    Giladi, I.2    Riley, M.A.3
  • 161
    • 85022194226 scopus 로고    scopus 로고
    • Bacteriocin production: A relatively unharnessed probiotic trait?
    • Hegarty, J. W., Guinane, C. M., Ross, R. P., Hill, C. & Cotter, P. D. Bacteriocin production: A relatively unharnessed probiotic trait? F1000Res. 5, 2587 (2016).
    • (2016) F1000Res. , vol.5 , pp. 2587
    • Hegarty, J.W.1    Guinane, C.M.2    Ross, R.P.3    Hill, C.4    Cotter, P.D.5
  • 163
    • 85014963888 scopus 로고    scopus 로고
    • Critical review on biofilm methods
    • Azeredo, J. et al. Critical review on biofilm methods. Crit. Rev. Microbiol. 43, 313-351 (2017).
    • (2017) Crit. Rev. Microbiol. , vol.43 , pp. 313-351
    • Azeredo, J.1
  • 164
    • 84865428411 scopus 로고    scopus 로고
    • Characterization of polymyxin B-induced nephrotoxicity: Implications for dosing regimen design
    • Abdelraouf, K. et al. Characterization of polymyxin B-induced nephrotoxicity: implications for dosing regimen design. Antimicrob. Agents Chemother. 56, 4625-4629 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 4625-4629
    • Abdelraouf, K.1
  • 165
    • 79960941561 scopus 로고    scopus 로고
    • Selection of resistant bacteria at very low antibiotic concentrations
    • e1002158 1:CAS:528:DC%2BC3MXhtVGqsL7P 21811410 3141051
    • Gullberg, E. et al. Selection of resistant bacteria at very low antibiotic concentrations. PLoS Pathog. 7, e1002158 (2011).
    • (2011) PLoS Pathog. , vol.7
    • Gullberg, E.1
  • 166
    • 84900836776 scopus 로고    scopus 로고
    • Selection of antibiotic resistance at very low antibiotic concentrations
    • Sandegren, L. Selection of antibiotic resistance at very low antibiotic concentrations. Ups. J. Med. Sci. 119, 103-107 (2014).
    • (2014) Ups. J. Med. Sci. , vol.119 , pp. 103-107
    • Sandegren, L.1
  • 167
    • 47749155981 scopus 로고    scopus 로고
    • Antibiotics and antibiotic resistance genes in natural environments
    • Martínez, J. L. Antibiotics and antibiotic resistance genes in natural environments. Science 321, 365-367 (2008).
    • (2008) Science , vol.321 , pp. 365-367
    • Martínez, J.L.1
  • 168
    • 0031724859 scopus 로고    scopus 로고
    • Effects of subinhibitory concentrations of antibiotics on alpha-Toxin (HLA) gene expression of methicillin-sensitive and methicillin-resistant Staphylococcus aureus isolates
    • Ohlsen, K. et al. Effects of subinhibitory concentrations of antibiotics on alpha-Toxin (hla) gene expression of methicillin-sensitive and methicillin-resistant Staphylococcus aureus isolates. Antimicrob. Agents Chemother. 42, 2817-2823 (1998).
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2817-2823
    • Ohlsen, K.1
  • 169
    • 23044484981 scopus 로고    scopus 로고
    • Secretion of proteases by Pseudomonas aeruginosa biofilms xposed to ciprofloxacin
    • Ołdak, E. & Trafny, E. A. Secretion of proteases by Pseudomonas aeruginosa biofilms xposed to ciprofloxacin. Antimicrob. Agents Chemother. 49, 3281-3288 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3281-3288
    • Ołdak, E.1    Trafny, E.A.2
  • 170
    • 79952065856 scopus 로고    scopus 로고
    • The role of bacteria in the caries process: Ecological perspectives
    • Takahashi, N. & Nyvad, B. The role of bacteria in the caries process: ecological perspectives. J. Dent. Res. 90, 294-303 (2011).
    • (2011) J. Dent. Res. , vol.90 , pp. 294-303
    • Takahashi, N.1    Nyvad, B.2
  • 171
    • 1842867893 scopus 로고    scopus 로고
    • A mixed-bacteria ecological approach to understanding the role of the oral bacteria in dental caries causation: An alternative to Streptococcus mutans and the specific-plaque hypothesis
    • Kleinberg, I. A mixed-bacteria ecological approach to understanding the role of the oral bacteria in dental caries causation: An alternative to Streptococcus mutans and the specific-plaque hypothesis. Crit. Rev. Oral Biol. Med. 13, 108-125 (2002).
    • (2002) Crit. Rev. Oral Biol. Med. , vol.13 , pp. 108-125
    • Kleinberg, I.1
  • 172
    • 32044449165 scopus 로고    scopus 로고
    • Bacteriocin (mutacin) production by Streptococcus mutans genome sequence reference strain UA159: Elucidation of the antimicrobial repertoire by genetic dissection
    • Hale, J. D., Ting, Y. T., Jack, R. W., Tagg, J. R. & Heng, N. C. Bacteriocin (mutacin) production by Streptococcus mutans genome sequence reference strain UA159: elucidation of the antimicrobial repertoire by genetic dissection. Appl. Environ. Microbiol. 71, 7613-7617 (2005).
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7613-7617
    • Hale, J.D.1    Ting, Y.T.2    Jack, R.W.3    Tagg, J.R.4    Heng, N.C.5
  • 173
    • 3142715216 scopus 로고    scopus 로고
    • Transcriptional analysis of mutacin i (mutA) gene expression in planktonic and biofilm cells of Streptococcus mutans using fluorescent protein and glucuronidase reporters
    • Kreth, J., Merritt, J., Bordador, C., Shi, W. & Qi, F. Transcriptional analysis of mutacin I (mutA) gene expression in planktonic and biofilm cells of Streptococcus mutans using fluorescent protein and glucuronidase reporters. Oral. Microbiol. Immunol. 19, 252-256 (2004).
    • (2004) Oral. Microbiol. Immunol. , vol.19 , pp. 252-256
    • Kreth, J.1    Merritt, J.2    Bordador, C.3    Shi, W.4    Qi, F.5
  • 174
    • 46049097957 scopus 로고    scopus 로고
    • Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans
    • Kreth, J., Zhang, Y. & Herzberg, M. C. Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans. J. Bacteriol. 190, 4632-4640 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 4632-4640
    • Kreth, J.1    Zhang, Y.2    Herzberg, M.C.3
  • 176
    • 84919711600 scopus 로고    scopus 로고
    • Quorum sensing inhibitors as anti-biofilm agents
    • Brackman, G. & Coenye, T. Quorum sensing inhibitors as anti-biofilm agents. Curr. Pharm. Des. 21, 5-11 (2015).
    • (2015) Curr. Pharm. Des. , vol.21 , pp. 5-11
    • Brackman, G.1    Coenye, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.