메뉴 건너뛰기




Volumn 287, Issue 23, 2012, Pages 18900-18912

Invariant gly residue is important for α-defensin folding, dimerization, and function: A case study of the human neutrophil α-defensin HNP1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE PEPTIDES; ANTI-BACTERIAL ACTIVITY; COLONY COUNTS; D-AMINO ACID; DEFENSINS; HUMAN NEUTROPHIL; IN-VIVO; INHIBITORY ACTIVITY; INHIBITORY CONCENTRATION; L-ALANINE; L-AMINO ACIDS; LETHAL DOSE; LETHAL FACTOR; MAIN CHAINS; NATIVE CHEMICAL LIGATION; SELF-ASSOCIATIONS; SIDE-CHAINS; STAPHYLOCOCCUS AUREUS; SURFACE PLASMONS; TORSION ANGLE; WILD TYPES;

EID: 84861724380     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.355255     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 78249233244 scopus 로고    scopus 로고
    • Antimicrobial peptides. The ancient arm of the human immune system
    • Wiesner, J., and Vilcinskas, A. (2010) Antimicrobial peptides. The ancient arm of the human immune system. Virulence 1, 440-464
    • (2010) Virulence , vol.1 , pp. 440-464
    • Wiesner, J.1    Vilcinskas, A.2
  • 2
    • 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
  • 3
    • 79960931881 scopus 로고    scopus 로고
    • Protecting the boundary. The sentinel role of host defense peptides in the skin
    • Bernard, J. J., and Gallo, R. L. (2011) Protecting the boundary. The sentinel role of host defense peptides in the skin. Cell Mol. Life Sci. 68, 2189-2199
    • (2011) Cell Mol. Life Sci. , vol.68 , pp. 2189-2199
    • Bernard, J.J.1    Gallo, R.L.2
  • 4
    • 0141799911 scopus 로고    scopus 로고
    • Defensins, antimicrobial peptides of innate immunity
    • Ganz, T. (2003) Defensins, antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 3, 710-720
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 5
    • 33645967168 scopus 로고    scopus 로고
    • Paneth cell defensins. Key effector molecules of innate immunity
    • Bevins, C. (2006) Paneth cell defensins. Key effector molecules of innate immunity. Biochem. Soc. Trans. 34, 263-266
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 263-266
    • Bevins, C.1
  • 6
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • DOI 10.1038/ni1206
    • Selsted, M. E, and Ouellette, A. J. (2005) Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6, 551-557 (Pubitemid 41710724)
    • (2005) Nature Immunology , vol.6 , Issue.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 8
    • 12944322216 scopus 로고    scopus 로고
    • Anthrax toxin: The long and winding road that leads to the kill
    • DOI 10.1016/j.tim.2004.12.004, PII S0966842X04002707
    • Abrami, L., Reig, N., and van der Goot, F. G. (2005) Anthrax toxin. The long and winding road that leads to the kill. Trends Microbiol. 13, 72-78 (Pubitemid 40174866)
    • (2005) Trends in Microbiology , vol.13 , Issue.2 , pp. 72-78
    • Abrami, L.1    Reig, N.2    Van Der, G.F.G.3
  • 9
    • 11244342346 scopus 로고    scopus 로고
    • Antibacterial activity and specificity of the six human α-defensins
    • DOI 10.1128/AAC.49.1.269-275.2005
    • Ericksen, B., Wu, Z., Lu, W., and Lehrer, R. I. (2005) Antibacterial activity and specificity of the six human α-defensins. Antimicrob. Agents Chemother. 49, 269-275 (Pubitemid 40065802)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.1 , pp. 269-275
    • Ericksen, B.1    Wu, Z.2    Lu, W.3    Lehrer, R.I.4
  • 10
    • 83655193502 scopus 로고    scopus 로고
    • α-Defensins in human innate immunity
    • Lehrer, R. I., and Lu, W. (2012) α-Defensins in human innate immunity. Immunol. Rev. 245, 84-112
    • (2012) Immunol. Rev. , vol.245 , pp. 84-112
    • Lehrer, R.I.1    Lu, W.2
  • 12
    • 0022395334 scopus 로고
    • Primary structures of three human neutrophil defensins
    • Selsted, M. E., Harwig, S. S., Ganz, T., Schilling, J. W., and Lehrer, R. I. (1985) Primary structures of three human neutrophil defensins. J. Clin. Invest. 76, 1436-1439 (Pubitemid 16193691)
    • (1985) Journal of Clinical Investigation , vol.76 , Issue.4 , pp. 1436-1439
    • Selsted, M.E.1    Harwig, S.S.L.2    Ganz, T.3
  • 13
    • 0022402545 scopus 로고
    • Defensins. Natural peptide antibiotics of human neutrophils
    • Ganz, T., Selsted, M. E., Szklarek, D., Harwig, S. S., Daher, K., Bainton, D. F., and Lehrer, R. I. (1985) Defensins. Natural peptide antibiotics of human neutrophils. J. Clin. Invest. 76, 1427-1435 (Pubitemid 16193690)
    • (1985) Journal of Clinical Investigation , vol.76 , Issue.4 , pp. 1427-1435
    • Ganz, T.1    Selsted, M.E.2    Szklarek, D.3
  • 14
    • 0024370068 scopus 로고
    • Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family
    • Wilde, C. G., Griffith, J. E., Marra, M. N., Snable, J. L., and Scott, R. W. (1989) Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family. J. Biol. Chem. 264, 11200-11203 (Pubitemid 19168851)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.19 , pp. 11200-11203
    • Wilde, C.G.1    Griffith, J.E.2    Marra, M.N.3    Snable, J.L.4    Scott, R.W.5
  • 16
    • 0027390031 scopus 로고
    • Defensin-6 mRNA in human Paneth cells: Implications for antimicrobial peptides in host defense of the human bowel
    • DOI 10.1016/0014-5793(93)81160-2
    • Jones, D. E., and Bevins, C. L. (1993) Defensin-6 mRNA in human paneth cells. Implications for antimicrobial peptides in host defense of the human bowel. FEBS Lett. 315, 187-192 (Pubitemid 23015882)
    • (1993) FEBS Letters , vol.315 , Issue.2 , pp. 187-192
    • Jones, D.E.1    Bevins, C.L.2
  • 17
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones, D. E., and Bevins, C. L. (1992) Paneth cells of the human small intestine express an antimicrobial peptide gene. J. Biol. Chem. 267, 23216-23225
    • (1992) J. Biol. Chem. , vol.267 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 20
    • 0027423053 scopus 로고
    • Identification, classification, and analysis of beta-bulges in proteins
    • Chan, A. W., Hutchinson, E. G., Harris, D., and Thornton, J. M. (1993) Identification, classification, and analysis of β-bulges in proteins. Protein Sci. 2, 1574-1590 (Pubitemid 23294336)
    • (1993) Protein Science , vol.2 , Issue.10 , pp. 1574-1590
    • Chan, A.W.E.1    Hutchinson, E.G.2    Harris, D.3    Thornton, J.M.4
  • 21
    • 0026468973 scopus 로고
    • NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1
    • Pardi, A., Zhang, X. L., Selsted, M. E., Skalicky, J. J., and Yip, P. F. (1992) NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1. Biochemistry 31, 11357-11364
    • (1992) Biochemistry , vol.31 , pp. 11357-11364
    • Pardi, A.1    Zhang, X.L.2    Selsted, M.E.3    Skalicky, J.J.4    Yip, P.F.5
  • 23
    • 0025903814 scopus 로고
    • Crystal structure of defensin HNP-3, an amphiphilic dimer: Mechanisms of membrane permeabilization
    • Hill, C. P., Yee, J., Selsted, M. E., and Eisenberg, D. (1991) Crystal structure of defensin HNP-3, an amphiphilic dimer. Mechanisms of membrane permeabilization. Science 251, 1481-1485 (Pubitemid 121000438)
    • (1991) Science , vol.251 , Issue.5000 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 24
    • 0037420319 scopus 로고    scopus 로고
    • Productive folding of human neutrophil α-defensins in vitro without the pro-peptide
    • DOI 10.1021/ja0294257
    • Wu, Z., Powell, R., and Lu, W. (2003) Productive folding of human neutrophil α-defensins in vitro without the propeptide. J. Am. Chem. Soc. 125, 2402-2403 (Pubitemid 36512221)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.9 , pp. 2402-2403
    • Wu, Z.1    Powell, R.2    Lu, W.3
  • 25
    • 0026652575 scopus 로고
    • Cationic defensins arise from charge-neutralized propeptides. A mechanism for avoiding leukocyte autocytotoxicity?
    • Michaelson, D., Rayner, J., Couto, M., and Ganz, T. (1992) Cationic defensins arise from charge-neutralized propeptides. A mechanism for avoiding leukocyte autocytotoxicity? J. Leukoc. Biol. 51, 634-639
    • (1992) J. Leukoc. Biol. , vol.51 , pp. 634-639
    • Michaelson, D.1    Rayner, J.2    Couto, M.3    Ganz, T.4
  • 26
    • 0028898423 scopus 로고
    • The proregion of human neutrophil defensin contains a motif that is essential for normal subcellular sorting
    • Liu, L., and Ganz, T. (1995) The proregion of human neutrophil defensin contains a motif that is essential for normal subcellular sorting. Blood 85, 1095-1103
    • (1995) Blood , vol.85 , pp. 1095-1103
    • Liu, L.1    Ganz, T.2
  • 28
    • 0038345623 scopus 로고    scopus 로고
    • From pro defensins to defensins: Synthesis and characterization of human neutrophil pro α-defensin-1 and its mature domain
    • DOI 10.1034/j.1399-3011.2003.00068.x
    • Wu, Z., Prahl, A., Powell, R., Ericksen, B., Lubkowski, J., and Lu, W. (2003) From pro defensins to defensins. Synthesis and characterization of human neutrophil pro-α-defensin-1 and its mature domain. J. Pept. Res. 62, 53-62 (Pubitemid 36819302)
    • (2003) Journal of Peptide Research , vol.62 , Issue.2 , pp. 53-62
    • Wu, Z.1    Prahl, A.2    Powell, R.3    Ericksen, B.4    Lubkowski, J.5    Lu, W.6
  • 31
    • 2542627454 scopus 로고    scopus 로고
    • Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor
    • Min, D. H., Tang, W. J., and Mrksich, M. (2004) Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor. Nat. Biotechnol. 22, 717-723
    • (2004) Nat. Biotechnol. , vol.22 , pp. 717-723
    • Min, D.H.1    Tang, W.J.2    Mrksich, M.3
  • 32
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite. Programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 38
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 39
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson, P. E., and Kent, S. B. (2000) Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69, 923-960
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 40
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P. E., Muir, T. W., Clark-Lewis, I., and Kent, S. B. (1994) Synthesis of proteins by native chemical ligation. Science 266, 776-779 (Pubitemid 24359280)
    • (1994) Science , vol.266 , Issue.5186 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.H.4
  • 41
    • 33751545243 scopus 로고    scopus 로고
    • Crystal structures of human α-defensins HNP4, HD5, and HD6
    • DOI 10.1110/ps.062336606
    • Szyk, A., Wu, Z., Tucker, K., Yang, D., Lu, W., and Lubkowski, J. (2006) Crystal structures of human α-defensins HNP4, HD5, and HD6. Protein Sci. 15, 2749-2760 (Pubitemid 44833756)
    • (2006) Protein Science , vol.15 , Issue.12 , pp. 2749-2760
    • Szyk, A.1    Wu, Z.2    Tucker, K.3    Yang, D.4    Lu, W.5    Lubkowski, J.6
  • 45
    • 52049114697 scopus 로고    scopus 로고
    • The conserved salt bridge in human α-defensin 5 is required for its precursor processing and proteolytic stability
    • Rajabi, M., de Leeuw, E., Pazgier, M., Li, J., Lubkowski, J., and Lu, W. (2008) The conserved salt bridge in human α-defensin 5 is required for its precursor processing and proteolytic stability. J. Biol. Chem. 283, 21509-21518
    • (2008) J. Biol. Chem. , vol.283 , pp. 21509-21518
    • Rajabi, M.1    De Leeuw, E.2    Pazgier, M.3    Li, J.4    Lubkowski, J.5    Lu, W.6
  • 47
    • 33748807728 scopus 로고    scopus 로고
    • Structural and functional characterization of the conserved salt bridge in mammalian paneth cell α-defensins: Solution structures of mouse cryptdin-4 and (E15D)-cryptdin-4
    • DOI 10.1074/jbc.M604992200
    • Rosengren, K. J., Daly, N. L., Fornander, L. M., Jönsson, L. M., Shirafuji, Y., Qu, X., Vogel, H. J., Ouellette, A. J., and Craik, D. J. (2006) Structural and functional characterization of the conserved salt bridge in mammalian paneth cell α-defensins. Solution structures of mouse Cryptdin-4 and (E15D)-Cryptdin-4. J. Biol. Chem. 281, 28068-28078 (Pubitemid 44414520)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 28068-28078
    • Rosengren, K.J.1    Daly, N.L.2    Fornander, L.M.3    Jonsson, L.M.H.4    Shirafuji, Y.5    Qu, X.6    Vogel, H.J.7    Ouellette, A.J.8    Craik, D.J.9
  • 51
    • 34548045312 scopus 로고    scopus 로고
    • Unifying themes in host defence effector polypeptides
    • DOI 10.1038/nrmicro1744, PII NRMICRO1744
    • Yeaman, M. R., and Yount, N. Y. (2007) Unifying themes in host defense effector polypeptides. Nat. Rev. Microbiol. 5, 727-740 (Pubitemid 47278866)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.9 , pp. 727-740
    • Yeaman, M.R.1    Yount, N.Y.2
  • 52
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith, C. K., Withka, J. M., and Regan, L. (1994) A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry 33, 5510-5517
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 53
    • 27944493960 scopus 로고    scopus 로고
    • Effects of the terminal charges in human neutrophil α-defensin 2 on its bactericidal and membrane activity
    • DOI 10.1016/j.peptides.2005.06.002, PII S0196978105002962
    • Xie, C., Zeng, P., Ericksen, B., Wu, Z., Lu, W. Y., and Lu, W. (2005) Effects of the terminal charges in human neutrophil α-defensin 2 on its bactericidal and membrane activity. Peptides 26, 2377-2383 (Pubitemid 41676707)
    • (2005) Peptides , vol.26 , Issue.12 , pp. 2377-2383
    • Xie, C.1    Zeng, P.2    Ericksen, B.3    Wu, Z.4    Lu, W.-Y.5    Lu, W.6
  • 54
    • 34547120485 scopus 로고    scopus 로고
    • Toward understanding the cationicity of defensins: Arg and Lys versus their noncoded analogs
    • DOI 10.1074/jbc.M611003200
    • Zou, G., de Leeuw, E., Li, C., Pazgier, M., Li, C., Zeng, P., Lu, W. Y., Lubkowski, J., and Lu, W. (2007) Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs. J. Biol. Chem. 282, 19653-19665 (Pubitemid 47100066)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 19653-19665
    • Zou, G.1    De Leeuw, E.2    Li, C.3    Pazgier, M.4    Li, C.5    Zeng, P.6    Lu, W.-Y.7    Lubkowski, J.8    Lu, W.9
  • 56
    • 65449140989 scopus 로고    scopus 로고
    • Anionic amino acids near the pro-α-defensin N terminus mediate inhibition of bactericidal activity in mouse procryptdin-4
    • Figueredo, S. M., Weeks, C. S., Young, S. K., and Ouellette, A. J. (2009) Anionic amino acids near the pro-α-defensin N terminus mediate inhibition of bactericidal activity in mouse procryptdin-4. J. Biol. Chem. 284, 6826-6831
    • (2009) J. Biol. Chem. , vol.284 , pp. 6826-6831
    • Figueredo, S.M.1    Weeks, C.S.2    Young, S.K.3    Ouellette, A.J.4
  • 57
    • 70350461418 scopus 로고    scopus 로고
    • Electropositive charge in α-defensin bactericidal activity. Functional effects of Lys for Arg substitutions vary with the peptide primary structure
    • Llenado, R. A., Weeks, C. S., Cocco, M. J., and Ouellette, A. J. (2009) Electropositive charge in α-defensin bactericidal activity. Functional effects of Lys for Arg substitutions vary with the peptide primary structure. Infect. Immun. 77, 5035-5043
    • (2009) Infect. Immun. , vol.77 , pp. 5035-5043
    • Llenado, R.A.1    Weeks, C.S.2    Cocco, M.J.3    Ouellette, A.J.4
  • 58
    • 0026597444 scopus 로고
    • Free R value.Anovel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R value.Anovel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.