메뉴 건너뛰기




Volumn 64, Issue 12, 1996, Pages 5000-5007

Candidacidal activity of recombinant human salivary histatin-5 and variants

Author keywords

[No Author keywords available]

Indexed keywords

HISTATIN; RECOMBINANT PROTEIN; SALIVA PROTEIN;

EID: 0029851698     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.64.12.5000-5007.1996     Document Type: Article
Times cited : (53)

References (43)
  • 3
    • 0026742166 scopus 로고
    • Structure and interactions of magainin antibiotic peptides in lipid biluyers: A solid-state nuclear magnetic resonance investigation
    • Bechlnger, B., M. Zaslo, and S, J. Opella. 1992, Structure and interactions of magainin antibiotic peptides in lipid biluyers: a solid-state nuclear magnetic resonance investigation. Biophys. J. 62:12-14.
    • (1992) Biophys. J. , vol.62 , pp. 12-14
    • Bechlnger, B.1    Zaslo, M.2    Opella, S.J.3
  • 4
    • 0028587077 scopus 로고
    • Biological activities and secondary structures of variant forms of human salivary cystatin SN produced in Escherichia coli
    • Bobek, L. A., N. Ramasubbu, X. Wing, T. R. Weaver, and M. J, Levine. 1994. Biological activities and secondary structures of variant forms of human salivary cystatin SN produced in Escherichia coli. Gene 151:303-308,
    • (1994) Gene , vol.151 , pp. 303-308
    • Bobek, L.A.1    Ramasubbu, N.2    Wing, X.3    Weaver, T.R.4    Levine, M.J.5
  • 5
    • 0027260527 scopus 로고
    • Expression of humim salivary hislatin and cystatin/histatin chimeric cDNAs in Kscherichia coli
    • Bobek, L A., H. Tsai, and M. J. Levine. 1993. Expression of humim salivary hislatin and cystatin/histatin chimeric cDNAs in Kscherichia coli. Crit. Rev. Oral Biol. Med, 4:581-5911,
    • (1993) Crit. Rev. Oral Biol. Med , vol.4 , pp. 581-5911
    • Bobek, L.A.1    Tsai, H.2    Levine, M.J.3
  • 6
    • 0027439749 scopus 로고
    • Efficient production of biologically active human salivary cystatins in Escherichia coli
    • Bobek, L. A., X. Wang, and M. J. Levine. 1993. Efficient production of biologically active human salivary cystatins in Escherichia coli. Gene 123: 203-210.
    • (1993) Gene , vol.123 , pp. 203-210
    • Bobek, L.A.1    Wang, X.2    Levine, M.J.3
  • 7
    • 0007176731 scopus 로고
    • Bactericidal effect of salivary histutin-5 on Porphyrononas gingivalis. abstr, no. 1751
    • Colon, J. O., T. Xu, and F. G. Oppenheim. 1993, Bactericidal effect of salivary histutin-5 on Porphyrononas gingivalis. abstr, no. 1751. J. Dent. Res. 72:322.
    • (1993) J. Dent. Res. , vol.72 , pp. 322
    • Colon, J.O.1    Xu, T.2    Oppenheim, F.G.3
  • 9
    • 0029450014 scopus 로고
    • Functional comparison of native and recombinant human salivary histatin I
    • Driscoll, J., Y. Zuo, T. Xu, J, R. Chol, R. F. Troxler, and F. G. Oppenheim. 1995. Functional comparison of native and recombinant human salivary histatin I. J, Dent. Res, 74:1837-1844.
    • (1995) J, Dent. Res , vol.74 , pp. 1837-1844
    • Driscoll, J.1    Zuo, Y.2    Xu, T.3    Chol, J.R.4    Troxler, R.F.5    Oppenheim, F.G.6
  • 10
    • 0342808059 scopus 로고    scopus 로고
    • Investigation of the anticandidal mechanism of histatins. abstr. no. 2724
    • Driscoll, J., Y. Zuo, T. Xu, R. F. Troxler, and F. O. Oppenheim. 1996. Investigation of the anticandidal mechanism of histatins. abstr. no. 2724, J. Dent. Res. 75:358.
    • (1996) J. Dent. Res. , vol.75 , pp. 358
    • Driscoll, J.1    Zuo, Y.2    Xu, T.3    Troxler, R.F.4    Oppenheim, F.O.5
  • 11
    • 0342501927 scopus 로고    scopus 로고
    • Salivary histatin-3 and histatin-5 exhibit specific binding to yeast cell membranes, abstr. no, 2723
    • Edgerfon, M., T. Lo, and P. A. Raj, 1996. Salivary histatin-3 and histatin-5 exhibit specific binding to yeast cell membranes, abstr. no, 2723. J. Dent. Res. 75:358.
    • (1996) J. Dent. Res. , vol.75 , pp. 358
    • Edgerfon, M.1    Lo, T.2    Raj, P.A.3
  • 12
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfleld, N., and G. D. Fasman. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfleld, N.1    Fasman, A.G.D.2
  • 13
    • 0016685754 scopus 로고
    • Fractionation of human parotid salivary proteins and the isolation of an histidine-rich acidic peptide which shows high affinity for hydroxyapatilc surfaces
    • Hay, D. I. 1975. Fractionation of human parotid salivary proteins and the isolation of an histidine-rich acidic peptide which shows high affinity for hydroxyapatilc surfaces. Arch. Oral Biol. 20:553-558.
    • (1975) Arch. Oral Biol. , vol.20 , pp. 553-558
    • Hay, D.I.1
  • 14
    • 0003663169 scopus 로고
    • Hoefer Scientific Instruments, San Francisco
    • Hoefer Scientific Instruments. 1994. Protein elctrophoresis applications guide. Hoefer Scientific Instruments, San Francisco.
    • (1994) Protein Elctrophoresis Applications Guide
  • 15
    • 0042928303 scopus 로고
    • Properties of the membrane modifying polypeptidc antibiotics alamethicin and trichotoxin A-40
    • W. Voelter and G, Weitzel (ed.). Walter de Gruyter, Berlin
    • Jung, G., H. Bruckner, and H, Schmilt. 1981. Properties of the membrane modifying polypeptidc antibiotics alamethicin and trichotoxin A-40. p. 75114. In W. Voelter and G, Weitzel (ed.). Structure and activity of natural peptides. Walter de Gruyter, Berlin,
    • (1981) Structure and Activity of Natural Peptides , pp. 75114
    • Jung, G.1    Bruckner, H.2    Schmilt, H.3
  • 17
    • 2442760190 scopus 로고
    • Effects of human salivary histatin-5 on Aetimomyees species, abstr. on. 1595
    • Kalpidis, C. D., T. Xu, and F. G. Oppenheim. 1992. Effects of human salivary histatin-5 on Aetimomyees species, abstr. on. 1595. J. Dent. Res. 71:305.
    • (1992) J. Dent. Res. , vol.71 , pp. 305
    • Kalpidis, C.D.1    Xu, T.2    Oppenheim, F.G.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bactcriophagc T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bactcriophagc T4. Nature (London) 227:680-585,
    • (1970) Nature (London) , vol.227 , pp. 680-1585
    • Laemmli, U.K.1
  • 19
    • 0026811864 scopus 로고
    • One-step purification of histidine-rich polypeptides from human parotid saliva and determination of anti-candidal activity
    • Lal, K., R. P. Santarpla III, L. Xu, F. Manssuri, and J. J. Pollock. 1992. One-step purification of histidine-rich polypeptides from human parotid saliva and determination of anti-candidal activity. Oral Microbiol, Immunol. 7:44-50.
    • (1992) Oral Microbiol, Immunol. , vol.7 , pp. 44-50
    • Lal, K.1    Santarpla III, R.P.2    Xu, L.3    Manssuri, F.4    Pollock, J.J.5
  • 20
    • 0021280786 scopus 로고
    • Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutam
    • Mackay, B. J., L. Denepltrya, V. J. Lacuno, S. B. Krost, and J. J. Pollock. 1984. Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutam. Infect. Immun. 44:695-701.
    • (1984) Infect. Immun. , vol.44 , pp. 695-701
    • Mackay, B.J.1    Denepltrya, L.2    Lacuno, V.J.3    Krost, S.B.4    Pollock, J.J.5
  • 21
    • 0023875642 scopus 로고
    • A two-dimensional NMR study of the antimierobial peptide magainin 2
    • 2l. Marion, D., M. Zaslof, and A. Bax. 1988 A two-dimensional NMR study of the antimierobial peptide magainin 2. FEBS Lett. 227:21-26.
    • (1988) FEBS Lett. , vol.227 , pp. 21-26
    • Marion, D.1    Zaslof, M.2    Bax, A.3
  • 22
    • 84985641154 scopus 로고
    • Synthesis and conformation of a polyoxyelhylene-bound undecapeplide of the alamethicin helis and (2-methylalanyl-ahinine)
    • Mayr, W., R. Oekonomopulos, and G. Jung. 1979. Synthesis and conformation of a polyoxyelhylene-bound undecapeplide of the alamethicin helis and (2-methylalanyl-ahinine). Biopolymers 18:425-450.
    • (1979) Biopolymers , vol.18 , pp. 425-450
    • Mayr, W.1    Oekonomopulos, R.2    Jung, G.3
  • 23
    • 0024572967 scopus 로고
    • Genetics of human salivary proteins
    • Minaguchi, K., and A. Bennick. 1989. Genetics of human salivary proteins. J. Dent. Res. 68:2-15.
    • (1989) J. Dent. Res. , vol.68 , pp. 2-15
    • Minaguchi, K.1    Bennick, A.2
  • 24
    • 0025781077 scopus 로고
    • Inhibitory effects of human salivary bistatins and lysozyme or coaggregation between Porphyronmonas glagivalis and.Strepiococcus nittis
    • Murakami, Y., H. Nagata, A. Amano, M, Takagaki, S, Shizukulshi, A. Tsunemilsu, and S, Almoto. 1991. Inhibitory effects of human salivary bistatins and lysozyme or coaggregation between Porphyronmonas glagivalis and.Strepiococcus nittis. Infccl, Immun. 59:3284-3286.
    • (1991) Infccl, Immun. , vol.59 , pp. 3284-3286
    • Murakami, Y.1    Nagata, H.2    Amano, A.3    Takagaki, M.4    Shizukulshi, S.5    Tsunemilsu, A.6    Almoto, S.7
  • 27
    • 0026948107 scopus 로고
    • Biological role of An arginine residue present in a histidine-rich peptide which inhibits hemagglutination of Porplyeomons gingivalls
    • Murakami, Y., H. Tamagawa, S. Shlzukulshi, A, Tsunemltsu, and S, Almoto. 1992. Biological role of An arginine residue present in a histidine-rich peptide which inhibits hemagglutination of Porplyeomons gingivalls. FEMS Microbiol. Lett. 98:201-204.
    • (1992) FEMS Microbiol. Lett. , vol.98 , pp. 201-204
    • Murakami, Y.1    Tamagawa, H.2    Shlzukulshi, S.3    Tsunemltsu, A.4    Almoto, S.5
  • 28
    • 85085845841 scopus 로고
    • 5Gly-Ala-Aib-Pro-Ala-Aib-Aih-Glu-(OBzl)-Ciln-OMe with respect to alamethiein
    • 5Gly-Ala-Aib-Pro-Ala-Aib-Aih-Glu-(OBzl)-Ciln-OMe with respect to alamethiein. Biopolymers 19:2103-214.
    • (1960) Biopolymers , vol.19 , pp. 2103-2214
    • Oekonomopulos, R.1    Jung, G.2
  • 29
    • 0002853655 scopus 로고
    • Salivary histidine-rich proteins
    • J. O. Tenovuo (ed.), CRC' Press, Inc., Boca Raton, Fla.
    • Oppenheim, F. G. 1989. Salivary histidine-rich proteins, p. 151-160. In J. O. Tenovuo (ed.), Human saliva: clinical chemistry and microbiology, vol. 1. CRC' Press, Inc., Boca Raton, Fla.
    • (1989) Human Saliva: Clinical Chemistry and Microbiology , vol.1 , pp. 151-160
    • Oppenheim, F.G.1
  • 31
    • 0022623229 scopus 로고
    • The primary structure and functional charactcrization of the neutral histidine-rich polypeptide from human parotid secretion
    • Oppenheim, F. G., Y. C. Yang, R. D. Diamond, D. Hyslop, G. D. Offner, and R. F. Troxler, 1986. The primary structure and functional charactcrization of the neutral histidine-rich polypeptide from human parotid secretion. J. Biol. Chem. 261:1177-1182.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1177-1182
    • Oppenheim, F.G.1    Yang, Y.C.2    Diamond, R.D.3    Hyslop, D.4    Offner, G.D.5    Troxler, R.F.6
  • 32
    • 0021263092 scopus 로고
    • Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida athicans
    • Pollock, J. J., L. Denepltiya, B. J. Mackay, and V. J, lacono. I984. Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida athicans. Infect. Immun. 44:702-707.
    • (1984) Infect. Immun. , vol.44 , pp. 702-707
    • Pollock, J.J.1    Denepltiya, L.2    Mackay, B.J.3    Lacono, V.J.4
  • 33
    • 0025237388 scopus 로고
    • Salivary Histatin-5: Dependence of sequence, chain length helical conformation for candidcidal activity
    • Raj, P. A., M. Edgerton, and M. J. Levine. 1990. Salivary Histatin-5: dependence of sequence, chain length, and helical conformation for candidcidal activity. J. Biol. Chem. 265:3898-3905.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3898-3905
    • Raj, P.A.1    Edgerton, M.2    Levine, M.J.3
  • 34
    • 0028321505 scopus 로고
    • Membrane-induced helical conformation of an active candidacidal fragment of salivary hislatins
    • Raj, P. A., S. Soni, and M. J. Levine. 1994. Membrane-induced helical conformation of an active candidacidal fragment of salivary hislatins. J. Biol. Chem, 269:9610-9619.
    • (1994) J. Biol. Chem , vol.269 , pp. 9610-9619
    • Raj, P.A.1    Soni, S.2    Levine, M.J.3
  • 36
  • 38
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. R., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.R.1    Johnson, K.S.2
  • 40
    • 0023134246 scopus 로고
    • Antigenic differences between mannoproteins of germ tubes and blaslospores of Candida alibicans
    • Sundstrom, P. M., E. J. Nlchols, and G. E. Kenny. 1987, Antigenic differences between mannoproteins of germ tubes and blaslospores of Candida alibicans. Infect. Immun. 55:616-620.
    • (1987) Infect. Immun. , vol.55 , pp. 616-620
    • Sundstrom, P.M.1    Nlchols, E.J.2    Kenny, G.E.3
  • 42
    • 0025733707 scopus 로고
    • Anticandidal activity of major human salivary histatins
    • Xu, T., S. M. Levltz, R. D. Diamond, and F. G. Oppenheim, 1991. Anticandidal activity of major human salivary histatins. Infect. Immun. 59:2549-2554.
    • (1991) Infect. Immun. , vol.59 , pp. 2549-2554
    • Xu, T.1    Levltz, S.M.2    Diamond, R.D.3    Oppenheim, F.G.4
  • 43
    • 0029101209 scopus 로고
    • Recombinunt histalns: Functional domain duplication enhances candidacidal activity
    • Zuo, V., T. Xu, R. F. Troxler, J. U, J. Urlicoll, and F. G. Oppenheim. 1995. Recombinunt histalns: functional domain duplication enhances candidacidal activity. Gene 161:87-91.
    • (1995) Gene , vol.161 , pp. 87-91
    • Zuo, V.1    Xu, T.2    Troxler, R.F.3    U, J.4    Urlicoll, J.5    Oppenheim, F.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.