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Volumn 31, Issue 5, 2010, Pages 777-785

The swaposin-like domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens

Author keywords

Antimicrobial proteins; Plant specific domain; SAPLIPs

Indexed keywords

AMINO ACID; ANTIINFECTIVE AGENT; ASPARTIC PROTEASE 1; ASPARTIC PROTEINASE; SURFACTANT PROTEIN B; UNCLASSIFIED DRUG;

EID: 77951252510     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.02.001     Document Type: Article
Times cited : (40)

References (51)
  • 1
    • 0036934796 scopus 로고    scopus 로고
    • Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco
    • Ann C.I., Fukusaki E., Kobayashi A. Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco. Planta 2002, 214:661-667.
    • (2002) Planta , vol.214 , pp. 661-667
    • Ann, C.I.1    Fukusaki, E.2    Kobayashi, A.3
  • 2
    • 0028908524 scopus 로고
    • An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B
    • Andersson M., Curstedt T., Jörnvalla H., Johansson J. An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett 1995, 362:328-332.
    • (1995) FEBS Lett , vol.362 , pp. 328-332
    • Andersson, M.1    Curstedt, T.2    Jörnvalla, H.3    Johansson, J.4
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 27144540463 scopus 로고    scopus 로고
    • Are innate immune signaling pathways in plants and animals conserved?
    • Ausubel F.M. Are innate immune signaling pathways in plants and animals conserved?. Nat Immunol 2005, 6:973-979.
    • (2005) Nat Immunol , vol.6 , pp. 973-979
    • Ausubel, F.M.1
  • 5
    • 0036006046 scopus 로고    scopus 로고
    • Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection
    • Berrocal-Lobo M., Segura A., Moreno M., López G., García-Olmedo F., Molina A. Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. Plant Physiol 2002, 128:951-961.
    • (2002) Plant Physiol , vol.128 , pp. 951-961
    • Berrocal-Lobo, M.1    Segura, A.2    Moreno, M.3    López, G.4    García-Olmedo, F.5    Molina, A.6
  • 6
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J Intern Med 2003, 254:197-215.
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 7
    • 22544463623 scopus 로고    scopus 로고
    • A short guided tour through functional and structural features of saposin-like proteins
    • Bruhn H. A short guided tour through functional and structural features of saposin-like proteins. Biochem J 2005, 389:249-257.
    • (2005) Biochem J , vol.389 , pp. 249-257
    • Bruhn, H.1
  • 8
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P., Stocklin R., Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 2004, 198:169-184.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 9
    • 0031457314 scopus 로고    scopus 로고
    • Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration
    • Chen F., Foolad M.R. Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration. Plant Mol Biol 1997, 35:821-831.
    • (1997) Plant Mol Biol , vol.35 , pp. 821-831
    • Chen, F.1    Foolad, M.R.2
  • 10
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: shaping the evolution of the plant immune response
    • Chisholm S.T., Coaker G., Day B., Staskawicz B.J. Host-microbe interactions: shaping the evolution of the plant immune response. Cell 2006, 124:803-814.
    • (2006) Cell , vol.124 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 11
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl J.L., Jones J.D. Plant pathogens and integrated defence responses to infection. Nature 2001, 411:826-833.
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 12
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies D.R. The structure and function of the aspartic proteinases. Annu Rev Phys Chem 1990, 19:189-215.
    • (1990) Annu Rev Phys Chem , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 13
    • 0032313424 scopus 로고    scopus 로고
    • Fungicidal and binding properties of three plant peptides
    • De Lucca A.J., Jacks T.J., Broekaert J. Fungicidal and binding properties of three plant peptides. Mycopathologia 1998, 144:87-91.
    • (1998) Mycopathologia , vol.144 , pp. 87-91
    • De Lucca, A.J.1    Jacks, T.J.2    Broekaert, J.3
  • 14
    • 0034623993 scopus 로고    scopus 로고
    • The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage
    • Egas C., Lavoura N., Resende R., Brito R., Pires E., Pedroso de Lima M., et al. The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage. J Biol Chem 2000, 275:38190-38196.
    • (2000) J Biol Chem , vol.275 , pp. 38190-38196
    • Egas, C.1    Lavoura, N.2    Resende, R.3    Brito, R.4    Pires, E.5    Pedroso de Lima, M.6
  • 15
    • 0033214046 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA encoding cardosin A, an RGD-containing plant aspartic proteinase
    • Faro C., Ramalho-Santos M., Vieira M., Mendes A., Simões I., Andrade R., et al. Cloning and characterization of cDNA encoding cardosin A, an RGD-containing plant aspartic proteinase. J Biol Chem 1999, 274:28724-28729.
    • (1999) J Biol Chem , vol.274 , pp. 28724-28729
    • Faro, C.1    Ramalho-Santos, M.2    Vieira, M.3    Mendes, A.4    Simões, I.5    Andrade, R.6
  • 16
    • 0032553435 scopus 로고    scopus 로고
    • Transport and activation of the vacuolar aspartic proteinase phytepsin in barley (Hordeum vulgare L.)
    • Glathe S., Kervinen J., Nimtz M., Li G.H., Tobin G.J., Copeland T.D., et al. Transport and activation of the vacuolar aspartic proteinase phytepsin in barley (Hordeum vulgare L.). J Biol Chem 1998, 273:31230-31236.
    • (1998) J Biol Chem , vol.273 , pp. 31230-31236
    • Glathe, S.1    Kervinen, J.2    Nimtz, M.3    Li, G.H.4    Tobin, G.J.5    Copeland, T.D.6
  • 17
    • 0032856481 scopus 로고    scopus 로고
    • Purification and properties of an aspartic protease from potato tuber that is inhibited by a basic chitinase
    • Guevara M.G., Oliva C.R., Machinandiarena M., Daleo G.R. Purification and properties of an aspartic protease from potato tuber that is inhibited by a basic chitinase. Physiol Plant 1999, 106:164-169.
    • (1999) Physiol Plant , vol.106 , pp. 164-169
    • Guevara, M.G.1    Oliva, C.R.2    Machinandiarena, M.3    Daleo, G.R.4
  • 18
    • 0034944619 scopus 로고    scopus 로고
    • Purification and characterization of an aspartic protease from potato leaves
    • Guevara M.G., Daleo G.R., Oliva C.R. Purification and characterization of an aspartic protease from potato leaves. Physiol Plant 2001, 112:321-326.
    • (2001) Physiol Plant , vol.112 , pp. 321-326
    • Guevara, M.G.1    Daleo, G.R.2    Oliva, C.R.3
  • 19
    • 0036246831 scopus 로고    scopus 로고
    • An aspartic protease with antifungal activity is induced after infection and wounding in intercellular fluids of potato tubers
    • Guevara M.G., Oliva C.R., Huarte M., Daleo G.R. An aspartic protease with antifungal activity is induced after infection and wounding in intercellular fluids of potato tubers. Eur J Plant Pathol 2002, 108:131-137.
    • (2002) Eur J Plant Pathol , vol.108 , pp. 131-137
    • Guevara, M.G.1    Oliva, C.R.2    Huarte, M.3    Daleo, G.R.4
  • 20
    • 12144266872 scopus 로고    scopus 로고
    • Potato aspartic proteases: induction, antimicrobial activity and substrate specificity
    • Guevara M.G., Verissimo P., Pires E., Faro C., Daleo G.R. Potato aspartic proteases: induction, antimicrobial activity and substrate specificity. J Plant Pathol 2004, 86:233-238.
    • (2004) J Plant Pathol , vol.86 , pp. 233-238
    • Guevara, M.G.1    Verissimo, P.2    Pires, E.3    Faro, C.4    Daleo, G.R.5
  • 21
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., Peitsch M. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.2
  • 22
    • 0028108664 scopus 로고
    • Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity
    • Guruprasad K., Törmäkangas K., Kervinen J., Blundell T.L. Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity. FEBS Lett 1994, 352:131-136.
    • (1994) FEBS Lett , vol.352 , pp. 131-136
    • Guruprasad, K.1    Törmäkangas, K.2    Kervinen, J.3    Blundell, T.L.4
  • 23
    • 0033565640 scopus 로고    scopus 로고
    • Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
    • Kervinen J., Tobin G.J., Costa J., Waugh D.S., Wlodawer A., Zdanov A. Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J 1999, 18:980-988.
    • (1999) EMBO J , vol.18 , pp. 980-988
    • Kervinen, J.1    Tobin, G.J.2    Costa, J.3    Waugh, D.S.4    Wlodawer, A.5    Zdanov, A.6
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 33746067918 scopus 로고    scopus 로고
    • Antimicrobial activity of potato aspartic proteases (StAPs) involves membrane permeabilization
    • Mendieta J.R., Pagano M.R., Muñoz F.F., Daleo G.R., Guevara M.G. Antimicrobial activity of potato aspartic proteases (StAPs) involves membrane permeabilization. Microbiology 2006, 152:2039-2047.
    • (2006) Microbiology , vol.152 , pp. 2039-2047
    • Mendieta, J.R.1    Pagano, M.R.2    Muñoz, F.F.3    Daleo, G.R.4    Guevara, M.G.5
  • 28
    • 0345120944 scopus 로고    scopus 로고
    • Plant aspartic proteinases: enzymes on the way to a function
    • Mutlu A., Gal S. Plant aspartic proteinases: enzymes on the way to a function. Physiol Plant 1999, 105:569-576.
    • (1999) Physiol Plant , vol.105 , pp. 569-576
    • Mutlu, A.1    Gal, S.2
  • 29
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: analysis and visualization of genetic variation
    • Nicholas K.B., Nicholas H.B., Deerfield D.W. GeneDoc: analysis and visualization of genetic variation. EMB News 1997, 4:14.
    • (1997) EMB News , vol.4 , pp. 14
    • Nicholas, K.B.1    Nicholas, H.B.2    Deerfield, D.W.3
  • 30
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley B.R., Kirsch D.R., Morris N.R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 1980, 105:361-363.
    • (1980) Anal Biochem , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 31
    • 0038266942 scopus 로고    scopus 로고
    • Construction, expression and characterization of a chimaeric mammalian-plant aspartic proteinase
    • Payie K.G., Tanaka T., Gal S., Yada R.Y. Construction, expression and characterization of a chimaeric mammalian-plant aspartic proteinase. Biochem J 2003, 372:671-678.
    • (2003) Biochem J , vol.372 , pp. 671-678
    • Payie, K.G.1    Tanaka, T.2    Gal, S.3    Yada, R.Y.4
  • 32
    • 0031257393 scopus 로고    scopus 로고
    • Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L.
    • Ramalho-Santos J., Pissarra M., Veríssimo P., Pereira S., Salema R., Pires E., et al. Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L. Planta 1997, 203:204-212.
    • (1997) Planta , vol.203 , pp. 204-212
    • Ramalho-Santos, J.1    Pissarra, M.2    Veríssimo, P.3    Pereira, S.4    Salema, R.5    Pires, E.6
  • 35
    • 29644442279 scopus 로고    scopus 로고
    • Antimicrobial activity of native and synthetic surfactant protein B peptides
    • Ryan M.A., Akinbi H.T., Serrano A.G., Perez-Gil J., Wu H., McCormack F.X., et al. Antimicrobial activity of native and synthetic surfactant protein B peptides. J Immunol 2006, 176:416-425.
    • (2006) J Immunol , vol.176 , pp. 416-425
    • Ryan, M.A.1    Akinbi, H.T.2    Serrano, A.G.3    Perez-Gil, J.4    Wu, H.5    McCormack, F.X.6
  • 36
    • 0030220455 scopus 로고    scopus 로고
    • Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein
    • Schaller A., Ryan C.A. Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein. Plant Mol Biol 1996, 31:1073-1077.
    • (1996) Plant Mol Biol , vol.31 , pp. 1073-1077
    • Schaller, A.1    Ryan, C.A.2
  • 37
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 2003, 31:3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 39
    • 2942512921 scopus 로고    scopus 로고
    • Structure and function of plant aspartic proteinases
    • Simões I., Faro C. Structure and function of plant aspartic proteinases. FEBS Lett 2004, 271:2067-2075.
    • (2004) FEBS Lett , vol.271 , pp. 2067-2075
    • Simões, I.1    Faro, C.2
  • 41
    • 0032751756 scopus 로고    scopus 로고
    • Permeabilization of fungal membranes by plant defensins inhibits fungal growth
    • Thevissen K., Terras F.R., Broekaert W.F. Permeabilization of fungal membranes by plant defensins inhibits fungal growth. Appl Environ Microbiol 1999, 65:5451-5458.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5451-5458
    • Thevissen, K.1    Terras, F.R.2    Broekaert, W.F.3
  • 42
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 11:4673-4680.
    • (1994) Nucleic Acids Res , vol.11 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 0034808250 scopus 로고    scopus 로고
    • A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum
    • Törmäkangas K., Hadlington J.L., Pimpl P., Hillmer S., Brandizzi F., Teeri T.H., et al. A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. Plant Cell 2001, 13:2021-2032.
    • (2001) Plant Cell , vol.13 , pp. 2021-2032
    • Törmäkangas, K.1    Hadlington, J.L.2    Pimpl, P.3    Hillmer, S.4    Brandizzi, F.5    Teeri, T.H.6
  • 44
    • 0027494660 scopus 로고
    • Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes
    • Vaccaro A.M., Tatti M., Ciaffoni F., Salvioli R., Maras B., Barca A. Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes. FEBS Lett 1993, 336:159-162.
    • (1993) FEBS Lett , vol.336 , pp. 159-162
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Maras, B.5    Barca, A.6
  • 46
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: from phenotypes to molecular mechanisms
    • van der Hoorn R.A. Plant proteases: from phenotypes to molecular mechanisms. Annu Rev Plant Biol 2008, 59:191-223.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 191-223
    • van der Hoorn, R.A.1
  • 47
    • 0034982756 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculus L.
    • Vieira M., Pissarra J., Verissimo P., Castanheira P., Costa Y., Pires E., et al. Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculus L. Plant Mol Biol 2001, 45:529-539.
    • (2001) Plant Mol Biol , vol.45 , pp. 529-539
    • Vieira, M.1    Pissarra, J.2    Verissimo, P.3    Castanheira, P.4    Costa, Y.5    Pires, E.6
  • 48
    • 0034254495 scopus 로고    scopus 로고
    • Bactericidal and tumoricidal activities of synthetic peptides derived from granulysin
    • Wang Z., Choice E., Kaspar A., Hanson D., Okada S., Lyu S.C., et al. Bactericidal and tumoricidal activities of synthetic peptides derived from granulysin. J Immunol 2000, 165:1486-1490.
    • (2000) J Immunol , vol.165 , pp. 1486-1490
    • Wang, Z.1    Choice, E.2    Kaspar, A.3    Hanson, D.4    Okada, S.5    Lyu, S.C.6
  • 49
    • 1842614199 scopus 로고    scopus 로고
    • An extracellular aspartic protease functions in Arabidopsis disease resistance signaling
    • Xia Y., Suzuki H., Borevitz J., Blount J., Guo Z., Patel K., et al. An extracellular aspartic protease functions in Arabidopsis disease resistance signaling. EMBO J 2004, 23:980-988.
    • (2004) EMBO J , vol.23 , pp. 980-988
    • Xia, Y.1    Suzuki, H.2    Borevitz, J.3    Blount, J.4    Guo, Z.5    Patel, K.6
  • 50
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: more than just microbicidal
    • Yang D., Biragyn A., Kwak L.W., Oppenheim J.J. Mammalian defensins in immunity: more than just microbicidal. Trends Immunol 2002, 23:291-296.
    • (2002) Trends Immunol , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 51
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


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