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Volumn 46, Issue 13, 2009, Pages 2604-2612

Hyastatin, a glycine-rich multi-domain antimicrobial peptide isolated from the spider crab (Hyas araneus) hemocytes

Author keywords

Antifungal; Arthropod; Chitin binding; Crustacea; Decapod; Invertebrate immunology; Marine bioprospecting

Indexed keywords

CHITIN; GLYCINE; HYASTATIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 67650578608     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.05.002     Document Type: Article
Times cited : (68)

References (48)
  • 1
    • 0032560497 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and innate immunity. Do 'animalcules' have defence budgets?
    • Barra D., Simmaco M., and Boman H.G. Gene-encoded peptide antibiotics and innate immunity. Do 'animalcules' have defence budgets?. FEBS Lett. 430 (1998) 130-134
    • (1998) FEBS Lett. , vol.430 , pp. 130-134
    • Barra, D.1    Simmaco, M.2    Boman, H.G.3
  • 2
    • 0036071479 scopus 로고    scopus 로고
    • Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus
    • Bartlett T.C., Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S., and Warr G.W. Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar. Biotechnol. 4 (2002) 278-293
    • (2002) Mar. Biotechnol. , vol.4 , pp. 278-293
    • Bartlett, T.C.1    Cuthbertson, B.J.2    Shepard, E.F.3    Chapman, R.W.4    Gross, P.S.5    Warr, G.W.6
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 3 (2005) 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 5
    • 3142666037 scopus 로고    scopus 로고
    • A new class (penaeidin class 4) of antimicrobial peptides from the Atlantic white shrimp (Litopenaeus setiferus) exhibits target specificity and an independent proline-rich-domain function
    • Cuthbertson B.J., Büllesbach E.E., Fievet J., Bachère E., and Gross P.S. A new class (penaeidin class 4) of antimicrobial peptides from the Atlantic white shrimp (Litopenaeus setiferus) exhibits target specificity and an independent proline-rich-domain function. Biochem. J. 381 (2004) 79-86
    • (2004) Biochem. J. , vol.381 , pp. 79-86
    • Cuthbertson, B.J.1    Büllesbach, E.E.2    Fievet, J.3    Bachère, E.4    Gross, P.S.5
  • 6
    • 18144414957 scopus 로고    scopus 로고
    • Solution structure of synthetic penaedin-4 with structural and functional comparisons with penaeidin-3
    • Cuthbertson B.J., Yang Y., Bachère E., Büllesbach E.E., Gross P.S., and Aumelas A. Solution structure of synthetic penaedin-4 with structural and functional comparisons with penaeidin-3. J. Biol. Chem. 280 (2005) 16009-16018
    • (2005) J. Biol. Chem. , vol.280 , pp. 16009-16018
    • Cuthbertson, B.J.1    Yang, Y.2    Bachère, E.3    Büllesbach, E.E.4    Gross, P.S.5    Aumelas, A.6
  • 7
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda)
    • Destoumieux D., Bulet P., Loew D., Van Dorsselaer A., Rodriguez J., and Bachère E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J. Biol. Chem. 272 (1997) 28398-28406
    • (1997) J. Biol. Chem. , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van Dorsselaer, A.4    Rodriguez, J.5    Bachère, E.6
  • 8
    • 0034002081 scopus 로고    scopus 로고
    • Penaedins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge
    • Destoumieux D., Muñoz M., Cosseau C., Rodriguez J., Bulet P., Comps M., and Bachère E. Penaedins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. J. Cell Sci. 113 (2000) 461-469
    • (2000) J. Cell Sci. , vol.113 , pp. 461-469
    • Destoumieux, D.1    Muñoz, M.2    Cosseau, C.3    Rodriguez, J.4    Bulet, P.5    Comps, M.6    Bachère, E.7
  • 10
    • 43249103254 scopus 로고    scopus 로고
    • Plasticins: membrane-damaging peptides with "chameleon-like" properties
    • El Amri C., and Nicolas P. Plasticins: membrane-damaging peptides with "chameleon-like" properties. Cell. Mol. Life Sci. 65 (2008) 895-909
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 895-909
    • El Amri, C.1    Nicolas, P.2
  • 11
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., and Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462 (1999) 11-28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 12
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J. Biomol. NMR 9 (1997) 127-135
    • (1997) J. Biomol. NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 15
    • 14744272742 scopus 로고    scopus 로고
    • Armadillidin: a novel glycine-rich antibacterial peptide directed against gram-positive bacteria in the woodlouse Armadillidium vulgare (terrestrial isopod, Crustacean)
    • Herbinière J., Braquart-Varnier C., Grève P., Strub J.-M., Frère J., Van Dorsselaer A., and Martin G. Armadillidin: a novel glycine-rich antibacterial peptide directed against gram-positive bacteria in the woodlouse Armadillidium vulgare (terrestrial isopod, Crustacean). Dev. Comp. Immunol. 29 (2005) 489-499
    • (2005) Dev. Comp. Immunol. , vol.29 , pp. 489-499
    • Herbinière, J.1    Braquart-Varnier, C.2    Grève, P.3    Strub, J.-M.4    Frère, J.5    Van Dorsselaer, A.6    Martin, G.7
  • 16
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study
    • Holak T.A., Engstrom A., Kraulis P.J., Lindeberg G., Bennich H., Jones T.A., Gronenborn A.M., and Clore G.M. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27 (1988) 7620-7629
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engstrom, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, G.M.8
  • 17
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • Hwang P.M., and Vogel H.J. Structure-function relationships of antimicrobial peptides. Biochem. Cell Biol. 76 (1998) 235-246
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 18
    • 0027157001 scopus 로고
    • Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregrina (flesh fly) larvae
    • Iijima R., Kurata S., and Natori S. Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregrina (flesh fly) larvae. J. Biol. Chem. 268 (1993) 12055-12061
    • (1993) J. Biol. Chem. , vol.268 , pp. 12055-12061
    • Iijima, R.1    Kurata, S.2    Natori, S.3
  • 19
    • 25444460844 scopus 로고    scopus 로고
    • Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking
    • Iijima M., Hashimoto T., Matsuda Y., Nagai T., Yamano Y., Ichi T., Osaki T., and Kawabata S.-i. Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking. FEBS J. 272 (2005) 4774-4786
    • (2005) FEBS J. , vol.272 , pp. 4774-4786
    • Iijima, M.1    Hashimoto, T.2    Matsuda, Y.3    Nagai, T.4    Yamano, Y.5    Ichi, T.6    Osaki, T.7    Kawabata, S.-i.8
  • 20
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 14 (2002) 87-95
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 23
    • 58149295148 scopus 로고    scopus 로고
    • Differential expression profiling of components associated with exoskeletal hardening in crustaceans
    • Kuballa A.V., and Elizur A. Differential expression profiling of components associated with exoskeletal hardening in crustaceans. BMC Genomics 9 (2008) 575
    • (2008) BMC Genomics , vol.9 , pp. 575
    • Kuballa, A.V.1    Elizur, A.2
  • 24
    • 0029093121 scopus 로고
    • Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae
    • Lee S.Y., Moon H.J., Kurata S., Natori S., and Lee B.L. Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae. Biol. Pharm. Bull. 18 (1995) 1049-1052
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1049-1052
    • Lee, S.Y.1    Moon, H.J.2    Kurata, S.3    Natori, S.4    Lee, B.L.5
  • 26
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • Lemaitre B., Reichhart J.-M., and Hoffmann J.A. Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc. Natl. Acad. Sci. USA. 94 (1997) 14614-14619
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichhart, J.-M.2    Hoffmann, J.A.3
  • 27
    • 0041322755 scopus 로고    scopus 로고
    • Helical structure of dermaseptin B2 in a membrane-mimetic environment
    • Lequin O., Bruston F., Convert O., Chassaing G., and Nicolas P. Helical structure of dermaseptin B2 in a membrane-mimetic environment. Biochemistry 42 (2003) 10311-10323
    • (2003) Biochemistry , vol.42 , pp. 10311-10323
    • Lequin, O.1    Bruston, F.2    Convert, O.3    Chassaing, G.4    Nicolas, P.5
  • 29
    • 0038460892 scopus 로고    scopus 로고
    • Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana
    • Lorenzini D.M., Silva Jr. P.I., Fogaça A.C., Bulet P., and Daffre S. Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana. Dev. Comp. Immunol. 27 (2003) 781-791
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 781-791
    • Lorenzini, D.M.1    Silva Jr., P.I.2    Fogaça, A.C.3    Bulet, P.4    Daffre, S.5
  • 30
    • 0034672657 scopus 로고    scopus 로고
    • Original involvement of antimicrobial peptides in mussel innate immunity
    • Mitta G., Vandenbulcke F., and Roch P. Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Lett. 486 (2000) 185-190
    • (2000) FEBS Lett. , vol.486 , pp. 185-190
    • Mitta, G.1    Vandenbulcke, F.2    Roch, P.3
  • 32
    • 33846991985 scopus 로고    scopus 로고
    • Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins
    • Nair D.G., Fry B.G., Alewood P., Kumar P.P., and Kini R.M. Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins. Biochem. J. 402 (2007) 93-104
    • (2007) Biochem. J. , vol.402 , pp. 93-104
    • Nair, D.G.1    Fry, B.G.2    Alewood, P.3    Kumar, P.P.4    Kini, R.M.5
  • 33
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus): isolation and chemical structure
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., and Iwanaga S. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus): isolation and chemical structure. J. Biol. Chem. 263 (1988) 16709-16713
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6
  • 34
    • 0033754189 scopus 로고    scopus 로고
    • Antimicrobial peptides isolated from insects
    • Otvos Jr. L. Antimicrobial peptides isolated from insects. J. Pept. Sci. 6 (2000) 497-511
    • (2000) J. Pept. Sci. , vol.6 , pp. 497-511
    • Otvos Jr., L.1
  • 35
    • 0033674821 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastoris
    • Park C.J., Park C.B., Hong S.-S., Lee H.-S., Lee S.Y., and Kim S.C. Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastoris. Plant Mol. Biol. 44 (2000) 187-197
    • (2000) Plant Mol. Biol. , vol.44 , pp. 187-197
    • Park, C.J.1    Park, C.B.2    Hong, S.-S.3    Lee, H.-S.4    Lee, S.Y.5    Kim, S.C.6
  • 36
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucl. Acids Res. 29 (2001) 2002-2007
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2002-2007
    • Pfaffl, M.W.1
  • 37
    • 34547901383 scopus 로고    scopus 로고
    • Molecular cloning of crustins from the hemocytes of Brazilian penaeid shrimps
    • Rosa R.D., Bandeira P.T., and Barracco M.A. Molecular cloning of crustins from the hemocytes of Brazilian penaeid shrimps. FEMS Microbiol. Lett. 274 (2007) 287-290
    • (2007) FEMS Microbiol. Lett. , vol.274 , pp. 287-290
    • Rosa, R.D.1    Bandeira, P.T.2    Barracco, M.A.3
  • 38
    • 0029020955 scopus 로고
    • A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antimicrobial activity
    • Saito T., Kawabata S., Shigenaga T., Takayenoki Y., Cho J., Nakajima H., Hirata M., and Iwanaga S. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antimicrobial activity. J. Biochem. 117 (1995) 1131-1137
    • (1995) J. Biochem. , vol.117 , pp. 1131-1137
    • Saito, T.1    Kawabata, S.2    Shigenaga, T.3    Takayenoki, Y.4    Cho, J.5    Nakajima, H.6    Hirata, M.7    Iwanaga, S.8
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 40
    • 0025644655 scopus 로고
    • Antimicrobial tachyplesin peptide precursor. cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus)
    • Shigenaga T., Muta T., Toh Y., Tokunaga F., and Iwanaga S. Antimicrobial tachyplesin peptide precursor. cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus). J. Biol. Chem. 265 (1990) 21350-21354
    • (1990) J. Biol. Chem. , vol.265 , pp. 21350-21354
    • Shigenaga, T.1    Muta, T.2    Toh, Y.3    Tokunaga, F.4    Iwanaga, S.5
  • 41
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • Silva Jr. P.I., Daffre S., and Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J. Biol. Chem. 275 (2000) 33464-33470
    • (2000) J. Biol. Chem. , vol.275 , pp. 33464-33470
    • Silva Jr., P.I.1    Daffre, S.2    Bulet, P.3
  • 42
    • 40849102419 scopus 로고    scopus 로고
    • Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans
    • Smith V.J., Fernandes J.M.O., Kemp G.D., and Hauton C. Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans. Dev. Comp. Immunol. 32 (2008) 758-772
    • (2008) Dev. Comp. Immunol. , vol.32 , pp. 758-772
    • Smith, V.J.1    Fernandes, J.M.O.2    Kemp, G.D.3    Hauton, C.4
  • 43
    • 58649108749 scopus 로고    scopus 로고
    • Characterization of crustins from the hemocytes of the spider crab, Hyas araneus, and the red king crab, Paralithodes camtschaticus
    • Sperstad S.V., Haug T., Paulsen V., Rode T.M., Strandskog G., Solem S.T., Styrvold O.B., and Stensvåg K. Characterization of crustins from the hemocytes of the spider crab, Hyas araneus, and the red king crab, Paralithodes camtschaticus. Dev. Comp. Immunol. 33 (2009) 583-591
    • (2009) Dev. Comp. Immunol. , vol.33 , pp. 583-591
    • Sperstad, S.V.1    Haug, T.2    Paulsen, V.3    Rode, T.M.4    Strandskog, G.5    Solem, S.T.6    Styrvold, O.B.7    Stensvåg, K.8
  • 44
    • 36549087177 scopus 로고    scopus 로고
    • Arasin 1, a proline-arginine rich antimicrobial peptide isolated from the spider crab, Hyas araneus
    • Stensvåg K., Haug T., Sperstad S.V., Rekdal Ø., Indrevoll B., and Styrvold O.B. Arasin 1, a proline-arginine rich antimicrobial peptide isolated from the spider crab, Hyas araneus. Dev. Comp. Immunol. 32 (2008) 275-285
    • (2008) Dev. Comp. Immunol. , vol.32 , pp. 275-285
    • Stensvåg, K.1    Haug, T.2    Sperstad, S.V.3    Rekdal, Ø.4    Indrevoll, B.5    Styrvold, O.B.6
  • 45
    • 4644311383 scopus 로고    scopus 로고
    • Antimicrobial peptides from marine invertebrates
    • Tincu J.A., and Taylor S.W. Antimicrobial peptides from marine invertebrates. Antimicrob. Agents Chemother. 48 (2004) 3645-3654
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3645-3654
    • Tincu, J.A.1    Taylor, S.W.2
  • 46
    • 0028509254 scopus 로고
    • TREECON for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment
    • Van de Peer Y., and de Wachter R. TREECON for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment. Comput. Appl. Biosci. 10 (1994) 569-570
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 569-570
    • Van de Peer, Y.1    de Wachter, R.2
  • 47
    • 0141591738 scopus 로고    scopus 로고
    • Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide
    • Yang Y., Poncet J., Garnier J., Zatylny C., Bachère E., and Aumelas A. Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. J. Biol. Chem. 278 (2003) 36859-36867
    • (2003) J. Biol. Chem. , vol.278 , pp. 36859-36867
    • Yang, Y.1    Poncet, J.2    Garnier, J.3    Zatylny, C.4    Bachère, E.5    Aumelas, A.6
  • 48
    • 33845643045 scopus 로고    scopus 로고
    • Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis
    • Zhang J., Li F., Wang Z., and Xiang J. Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis. J. Biotechnol. 127 (2007) 605-614
    • (2007) J. Biotechnol. , vol.127 , pp. 605-614
    • Zhang, J.1    Li, F.2    Wang, Z.3    Xiang, J.4


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