메뉴 건너뛰기




Volumn 52, Issue 8, 2008, Pages 2734-2741

Mechanism and fitness costs of PR-39 resistance in Salmonella enterica serovar typhimurium LT2

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PR 39; TRANSPORT PROTEIN SBM A; UNCLASSIFIED DRUG;

EID: 48749128095     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.00205-08     Document Type: Article
Times cited : (66)

References (55)
  • 1
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Agerberth, B., J. Y. Lee, T. Bergman, M. Carlquist, H. G. Boman, V. Mutt, and H. Jornvall. 1991. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur. J. Biochem. 202:849-854.
    • (1991) Eur. J. Biochem , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.Y.2    Bergman, T.3    Carlquist, M.4    Boman, H.G.5    Mutt, V.6    Jornvall, H.7
  • 2
    • 0032870940 scopus 로고    scopus 로고
    • The biological cost of antibiotic resistance
    • Andersson, D. I., and B. R. Levin. 1999. The biological cost of antibiotic resistance. Curr. Opin. Microbiol. 2:489-493.
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 489-493
    • Andersson, D.I.1    Levin, B.R.2
  • 5
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman, H. G. 2003. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254:197-215.
    • (2003) J. Intern. Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 6
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman, H. G., B. Agerberth, and A. Boman. 1993. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61:2978-2984.
    • (1993) Infect. Immun , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 7
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P. P., and W. Wackernagel. 1995. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 9
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D., C. Hill, and R. P. Ross. 2005. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 3:777-788.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., and J. Chen. 2004. ATP-binding cassette transporters in bacteria. Annu. Rev. Biochem. 73:241-268.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 12
    • 0030760775 scopus 로고    scopus 로고
    • Phenotypic resistance to thrombin-induced platelet microbicidal protein in vitro is correlated with enhanced virulence in experimental endocarditis due to Staphylococcus aureus
    • Dhawan, V. K., M. R. Yeaman, A. L. Cheung, E. Kim, P. M. Sullam, and A. S. Bayer. 1997. Phenotypic resistance to thrombin-induced platelet microbicidal protein in vitro is correlated with enhanced virulence in experimental endocarditis due to Staphylococcus aureus. Infect. Immun. 65:3293-3299.
    • (1997) Infect. Immun , vol.65 , pp. 3293-3299
    • Dhawan, V.K.1    Yeaman, M.R.2    Cheung, A.L.3    Kim, E.4    Sullam, P.M.5    Bayer, A.S.6
  • 13
    • 0025527885 scopus 로고
    • Experimental studies of natural selection in bacteria
    • Dykhuizen, D. E. 1990. Experimental studies of natural selection in bacteria. Annu. Rev. Ecol. Syst. 21:373-398.
    • (1990) Annu. Rev. Ecol. Syst , vol.21 , pp. 373-398
    • Dykhuizen, D.E.1
  • 14
    • 0037930850 scopus 로고    scopus 로고
    • SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides
    • Frick, I. M., P. Akesson, M. Rasmussen, A. Schmidtchen, and L. Bjorck. 2003. SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides. J. Biol. Chem. 278:16561-16566.
    • (2003) J. Biol. Chem , vol.278 , pp. 16561-16566
    • Frick, I.M.1    Akesson, P.2    Rasmussen, M.3    Schmidtchen, A.4    Bjorck, L.5
  • 15
    • 0031009432 scopus 로고    scopus 로고
    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo, R. L., K. J. Kim, M. Bernfield, C. A. Kozak, M. Zanetti, L. Merluzzi, and R. Gennaro. 1997. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem. 272:13088-13093.
    • (1997) J. Biol. Chem , vol.272 , pp. 13088-13093
    • Gallo, R.L.1    Kim, K.J.2    Bernfield, M.3    Kozak, C.A.4    Zanetti, M.5    Merluzzi, L.6    Gennaro, R.7
  • 16
    • 0028092047 scopus 로고
    • Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds
    • Gallo, R. L., M. Ono, T. Povsic, C. Page, E. Eriksson, M. Klagsbrun, and M. Bernfield. 1994. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc. Natl. Acad. Sci. USA 91:11035-11039.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11035-11039
    • Gallo, R.L.1    Ono, M.2    Povsic, T.3    Page, C.4    Eriksson, E.5    Klagsbrun, M.6    Bernfield, M.7
  • 18
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson, G. H., B. Agerberth, J. Odeberg, T. Bergman, B. Olsson, and R. Salcedo. 1996. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238:325-332.
    • (1996) Eur. J. Biochem , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 19
    • 0033919460 scopus 로고    scopus 로고
    • A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • Guina, T., E. C. Yi, H. Wang, M. Hackett, and S. I. Miller. 2000. A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides. J. Bacteriol. 182:4077-4086.
    • (2000) J. Bacteriol , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 20
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • Gunn, J. S., and S. I. Miller. 1996. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J. Bacteriol. 178:6857-6864.
    • (1996) J. Bacteriol , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 21
    • 0033794504 scopus 로고    scopus 로고
    • Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar Typhimurium
    • Gunn, J. S., S. S. Ryan, J. C. Van Velkinburgh, R. K. Ernst, and S. I. Miller. 2000. Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar Typhimurium. Infect. Immun. 68:6139-6146.
    • (2000) Infect. Immun , vol.68 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburgh, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 22
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo, L., K. B. Lim, C. M. Poduje, M. Daniel, J. S. Gunn, M. Hackett, and S. I. Miller. 1998. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 95:189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Lim, K.B.2    Poduje, C.M.3    Daniel, M.4    Gunn, J.S.5    Hackett, M.6    Miller, S.I.7
  • 23
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 24
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E., and H. G. Sahl. 2006. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24:1551-1557.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 25
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert, K., R. Volkmer-Engert, T. Walter, and R. E. Hancock. 2005. High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23:1008-1012.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.4
  • 26
    • 0036851306 scopus 로고    scopus 로고
    • Bacterial strategies for overcoming host innate and adaptive immune responses
    • Hornef, M. W., M. J. Wick, M. Rhen, and S. Normark. 2002. Bacterial strategies for overcoming host innate and adaptive immune responses. Nat. Immunol. 3:1033-1040.
    • (2002) Nat. Immunol , vol.3 , pp. 1033-1040
    • Hornef, M.W.1    Wick, M.J.2    Rhen, M.3    Normark, S.4
  • 27
    • 0030976983 scopus 로고    scopus 로고
    • Chemoattractant properties of PR-39, a neutrophil antibacterial peptide
    • Huang, H. J., C. R. Ross, and F. Blecha. 1997. Chemoattractant properties of PR-39, a neutrophil antibacterial peptide. J. Leukoc. Biol. 61:624-629.
    • (1997) J. Leukoc. Biol , vol.61 , pp. 624-629
    • Huang, H.J.1    Ross, C.R.2    Blecha, F.3
  • 28
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam, D., L. Bandholtz, J. Nilsson, H. Wigzell, B. Christensson, B. Agerberth, and G. Gudmundsson. 2001. Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 7:180-185.
    • (2001) Nat. Med , vol.7 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3    Wigzell, H.4    Christensson, B.5    Agerberth, B.6    Gudmundsson, G.7
  • 30
    • 0031019137 scopus 로고    scopus 로고
    • Protamine-induced permeabilization of cell envelopes of gram-positive and gram-negative bacteria
    • Johansen, C., A. Verheul, L. Gram, T. Gill, and T. Abee. 1997. Protamine-induced permeabilization of cell envelopes of gram-positive and gram-negative bacteria. Appl. Environ. Microbiol. 63:1155-1159.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 1155-1159
    • Johansen, C.1    Verheul, A.2    Gram, L.3    Gill, T.4    Abee, T.5
  • 31
    • 0043159258 scopus 로고    scopus 로고
    • Alanylation of teichoic acids protects Staphylococcus aureus against Toll-like receptor 2-dependent host defense in a mouse tissue cage infection model
    • Kristian, S. A., X. Lauth, V. Nizet, F. Goetz, B. Neumeister, A. Peschel, and R. Landmann. 2003. Alanylation of teichoic acids protects Staphylococcus aureus against Toll-like receptor 2-dependent host defense in a mouse tissue cage infection model. J. Infect. Dis. 188:414-423.
    • (2003) J. Infect. Dis , vol.188 , pp. 414-423
    • Kristian, S.A.1    Lauth, X.2    Nizet, V.3    Goetz, F.4    Neumeister, B.5    Peschel, A.6    Landmann, R.7
  • 32
    • 0001313535 scopus 로고
    • The distribution of the numbers of mutants in bacterial populations
    • Lea, D. E., and C. A. Coulson. 1949. The distribution of the numbers of mutants in bacterial populations. J. Genetics 49:264-285.
    • (1949) J. Genetics , vol.49 , pp. 264-285
    • Lea, D.E.1    Coulson, C.A.2
  • 33
    • 0344875086 scopus 로고    scopus 로고
    • Fusidic acid-resistant mutants of Salmonella enterica serovar Typhimurium with low fitness in vivo are defective in RpoS induction
    • Macvanin, M., J. Bjorkman, S. Eriksson, M. Rhen, D. I. Andersson, and D. Hughes. 2003. Fusidic acid-resistant mutants of Salmonella enterica serovar Typhimurium with low fitness in vivo are defective in RpoS induction. Antimicrob. Agents Chemother. 47:3743-3749.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 3743-3749
    • Macvanin, M.1    Bjorkman, J.2    Eriksson, S.3    Rhen, M.4    Andersson, D.I.5    Hughes, D.6
  • 34
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: Obstacles and realistic outlook
    • Marr, A. K., W. J. Gooderham, and R. E. Hancock. 2006. Antibacterial peptides for therapeutic use: obstacles and realistic outlook. Curr. Opin. Pharmacol. 6:468-472.
    • (2006) Curr. Opin. Pharmacol , vol.6 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.3
  • 36
    • 10844266565 scopus 로고    scopus 로고
    • Experimental adaptation of Salmonella typhimurium to mice
    • Nilsson, A. I., E. Kugelberg, O. G. Berg, and D. I. Andersson. 2004. Experimental adaptation of Salmonella typhimurium to mice. Genetics 168:1119-1130.
    • (2004) Genetics , vol.168 , pp. 1119-1130
    • Nilsson, A.I.1    Kugelberg, E.2    Berg, O.G.3    Andersson, D.I.4
  • 39
    • 34248336587 scopus 로고    scopus 로고
    • Multiple mechanisms to ameliorate the fitness burden of mupirocin resistance in Salmonella typhimurium
    • Paulander, W., S. Maisnier-Patin, and D. I. Andersson. 2007. Multiple mechanisms to ameliorate the fitness burden of mupirocin resistance in Salmonella typhimurium. Mol. Microbiol. 64:1038-1048.
    • (2007) Mol. Microbiol , vol.64 , pp. 1038-1048
    • Paulander, W.1    Maisnier-Patin, S.2    Andersson, D.I.3
  • 40
    • 33645834508 scopus 로고    scopus 로고
    • Experimental evolution of resistance to an antimicrobial peptide
    • Perron, G. G., M. Zasloff, and G. Bell. 2006. Experimental evolution of resistance to an antimicrobial peptide. Proc. Biol. Sci. 273:251-256.
    • (2006) Proc. Biol. Sci , vol.273 , pp. 251-256
    • Perron, G.G.1    Zasloff, M.2    Bell, G.3
  • 41
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel, A. 2002. How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10:179-186.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 43
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel, A., M. Otto, R. W. Jack, H. Kalbacher, G. Jung, and F. Gotz. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274:8405-8410.
    • (1999) J. Biol. Chem , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 44
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers, J. P., and R. E. Hancock. 2003. The relationship between peptide structure and antibacterial activity. Peptides 24:1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 45
    • 21844451165 scopus 로고    scopus 로고
    • Survivability of vancomycin resistant enterococci and fitness cost of vancomycin resistance acquisition
    • Ramadhan, A. A., and E. Hegedus. 2005. Survivability of vancomycin resistant enterococci and fitness cost of vancomycin resistance acquisition. J. Clin. Pathol. 58:744-746.
    • (2005) J. Clin. Pathol , vol.58 , pp. 744-746
    • Ramadhan, A.A.1    Hegedus, E.2
  • 46
    • 0029045349 scopus 로고
    • The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein
    • Salomón, R. A., and R. N. Farias. 1995. The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein. J. Bacteriol. 177:3323-3325.
    • (1995) J. Bacteriol , vol.177 , pp. 3323-3325
    • Salomón, R.A.1    Farias, R.N.2
  • 47
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer, W. M., X. Qu, A. J. Waring, and R. I. Lehrer. 1998. Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc. Natl. Acad. Sci. USA 95:1829-1833.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 48
    • 0030032395 scopus 로고    scopus 로고
    • Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide
    • Shi, J., C. R. Ross, M. M. Chengappa, M. J. Sylte, D. S. McVey, and F. Blecha. 1996. Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide. Antimicrob. Agents Chemother. 40:115-121.
    • (1996) Antimicrob. Agents Chemother , vol.40 , pp. 115-121
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Sylte, M.J.4    McVey, D.S.5    Blecha, F.6
  • 49
    • 0344080624 scopus 로고    scopus 로고
    • Phylogeny, processing and expression of the rat cathelicidin rCRAMP: A model for innate antimicrobial peptides
    • Termén, S., M. Tollin, B. Olsson, T. Svenberg, B. Agerberth, and G. H. Gudmundsson. 2003. Phylogeny, processing and expression of the rat cathelicidin rCRAMP: a model for innate antimicrobial peptides. Cell Mol. Life Sci. 60:536-549.
    • (2003) Cell Mol. Life Sci , vol.60 , pp. 536-549
    • Termén, S.1    Tollin, M.2    Olsson, B.3    Svenberg, T.4    Agerberth, B.5    Gudmundsson, G.H.6
  • 51
    • 0028209167 scopus 로고
    • In vitro resistance to platelet microbicidal protein correlates with endocarditis source among bacteremic staphylococcal and streptococcal isolates
    • Wu, T., M. R. Yeaman, and A. S. Bayer. 1994. In vitro resistance to platelet microbicidal protein correlates with endocarditis source among bacteremic staphylococcal and streptococcal isolates. Antimicrob. Agents Chemother. 38:729-732.
    • (1994) Antimicrob. Agents Chemother , vol.38 , pp. 729-732
    • Wu, T.1    Yeaman, M.R.2    Bayer, A.S.3
  • 53
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou, M., and R. L. Gallo. 2002. Cathelicidins, essential gene-encoded mammalian antibiotics. J. Mol. Med. 80:549-561.
    • (2002) J. Mol. Med , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 54
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 55
    • 0030727475 scopus 로고    scopus 로고
    • Salmonella infection increases porcine antibacterial peptide concentrations in serum
    • Zhang, G., C. R. Ross, S. S. Dritz, J. C. Nietfeld, and F. Blecha. 1997. Salmonella infection increases porcine antibacterial peptide concentrations in serum. Clin. Diagn. Lab. Immunol. 4:774-777.
    • (1997) Clin. Diagn. Lab. Immunol , vol.4 , pp. 774-777
    • Zhang, G.1    Ross, C.R.2    Dritz, S.S.3    Nietfeld, J.C.4    Blecha, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.