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Volumn 15, Issue 5, 2009, Pages 507-514

In-silico homology modeling of three isoforms of insect defensins from the dengue vector mosquito, Aedes aegypti (Linn., 1762)

Author keywords

Aedes aegypti; Defensins; Homology modeling; Modeller; Procheck

Indexed keywords

DEFENSIN; DEFENSIN A; DEFENSIN B; DEFENSIN C; INSECT PROTEIN; ISOPROTEIN; PROTEIN DERIVATIVE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 63249126030     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-008-0408-7     Document Type: Article
Times cited : (5)

References (44)
  • 1
    • 35748929379 scopus 로고    scopus 로고
    • Dengue
    • doi: 10.1016/S0140-6736(07)61687-0
    • Halstead SB (2007) Dengue. Lancet 370:1644-1652. doi: 10.1016/ S0140-6736(07)61687-0
    • (2007) Lancet , vol.370 , pp. 1644-1652
    • Halstead, S.B.1
  • 2
    • 0031823546 scopus 로고    scopus 로고
    • Dengue and dengue haemorrhagic fever
    • Gubler DJ (1998) Dengue and dengue haemorrhagic fever. Clin Microbiol Rev 11:480-496
    • (1998) Clin Microbiol Rev , vol.11 , pp. 480-496
    • Gubler, D.J.1
  • 3
    • 34948884135 scopus 로고    scopus 로고
    • Natural vertical transmission of dengue virus in Aedes albopictus (Diptera: Culicidae) in Kerala, a Southern Indian state
    • Thenmozhi V, Hiriyan J, Tewari SC, Samuel PP, Paramasivan R, Rajendran R et al (2007) Natural vertical transmission of dengue virus in Aedes albopictus (Diptera: Culicidae) in Kerala, a Southern Indian state. Jpn J Infect Dis 60:245-249
    • (2007) Jpn J Infect Dis , vol.60 , pp. 245-249
    • Thenmozhi, V.1    Hiriyan, J.2    Tewari, S.C.3    Samuel, P.P.4    Paramasivan, R.5    Rajendran, R.6
  • 4
    • 44249123310 scopus 로고    scopus 로고
    • ENTOMOLOGY: A mosquito goes global
    • doi: 10.1126/science.320.5878.954b. doi: 10.1126/science.320.5878.864
    • Enserink M (2008) ENTOMOLOGY: A mosquito goes global. Science 320:954b. doi: 10.1126/science.320.5878.954b. doi: 10.1126/science.320.5878.864
    • (2008) Science , vol.320
    • Enserink, M.1
  • 5
    • 36549076926 scopus 로고    scopus 로고
    • Infection with chikungunya virus in Italy: An outbreak in a temperate region
    • doi: 10.1016/S0140-6736(07)61779-6
    • Rezza G, Nicoletti L, Angelini R, Romi R, Finarelli AC, Panning M et al (2007) Infection with chikungunya virus in Italy: An outbreak in a temperate region. Lancet 370:1840-1846. doi: 10.1016/ S0140-6736(07)61779-6
    • (2007) Lancet , vol.370 , pp. 1840-1846
    • Rezza, G.1    Nicoletti, L.2    Angelini, R.3    Romi, R.4    Finarelli, A.C.5    Panning, M.6
  • 6
    • 21544446713 scopus 로고    scopus 로고
    • Eco-epidemiological analysis of dengue infection during an outbreak of dengue fever, India
    • doi: 10.1186/1743-422X-2-32
    • Chakravarthi A, Kumaria R (2005) Eco-epidemiological analysis of dengue infection during an outbreak of dengue fever, India. Virol J 2:32. doi: 10.1186/1743-422X-2-32
    • (2005) Virol J , vol.2 , pp. 32
    • Chakravarthi, A.1    Kumaria, R.2
  • 7
    • 0033591428 scopus 로고    scopus 로고
    • Phylogenetic perspectives in innate immunity
    • doi: 10.1126/science.284.5418.1313
    • Hoffmann JA, Kafatos FC, Janeway CA Jr, Ezekowitz RAB (1999) Phylogenetic perspectives in innate immunity. Science 248:1313-1318. doi: 10.1126/science.284.5418.1313
    • (1999) Science , vol.248 , pp. 1313-1318
    • Hoffmann, J.A.1    Kafatos, F.C.2    Janeway Jr., C.A.3    Ezekowitz, R.A.B.4
  • 8
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria
    • doi: 10.1038/nrmicro1098
    • Brogden KA (2005) Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria. Nat Rev Microbiol 3:238-241. doi: 10.1038/ nrmicro1098
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-241
    • Brogden, K.A.1
  • 9
    • 0035118326 scopus 로고    scopus 로고
    • Innate immune responses of Aedes aegypti
    • doi: 10.1016/S0965-1748(00)00141-7
    • Lowenberger C (2001) Innate immune responses of Aedes aegypti. Insect Biochem Mol Biol 31:219-229. doi: 10.1016/S0965-1748(00)00141-7
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 219-229
    • Lowenberger, C.1
  • 10
    • 0032993170 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic polypeptides of amoeboid protozoa-effector molecules of primitive phagocytes
    • doi: 10.1016/S0145-305X(99)00010-5
    • Leippe M (1999) Antimicrobial and cytolytic polypeptides of amoeboid protozoa-effector molecules of primitive phagocytes. Dev Comp Immunol 23:267-279. doi: 10.1016/S0145-305X(99)00010-5
    • (1999) Dev Comp Immunol , vol.23 , pp. 267-279
    • Leippe, M.1
  • 11
    • 20244363184 scopus 로고
    • Insect immunity: Isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides
    • doi: 10.1073/pnas.86.1.262
    • Lambert J, Keppi E, Dimarcq J-L, Wicker C, Reichhart J-M, Dunbar B et al (1989) Insect immunity: Isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. Proc Natl Acad Sci USA 86:262-266. doi: 10.1073/pnas.86.1.262
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 262-266
    • Lambert, J.1    Keppi, E.2    Dimarcq, J.-L.3    Wicker, C.4    Reichhart, J.-M.5    Dunbar, B.6
  • 12
    • 0029125794 scopus 로고
    • Full sequence and characterization of two insect defensins: Immune peptides from the mosquito Aedes aegypti
    • doi: 10.1098/rspb.1995.0139
    • Chalk R, Albuquerque CM, Ham PJ, Townson H (1995) Full sequence and characterization of two insect defensins: Immune peptides from the mosquito Aedes aegypti. Proc R Soc Lond B Biol Sci 261(1361):217-221. doi: 10.1098/rspb.1995.0139
    • (1995) Proc R Soc Lond B Biol Sci , vol.261 , Issue.1361 , pp. 217-221
    • Chalk, R.1    Albuquerque, C.M.2    Ham, P.J.3    Townson, H.4
  • 13
    • 0029328605 scopus 로고
    • Insect immunity: Isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti
    • doi: 10.1016/0965-1748(95)00043-U
    • Lowenberger C, Bulet P, Charlet M, Hetru C, Hodgeman B, Christensen BM et al (1995) Insect immunity: Isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti. Insect Biochem Mol Biol 25(7):867-873. doi: 10.1016/0965-1748(95)00043-U
    • (1995) Insect Biochem Mol Biol , vol.25 , Issue.7 , pp. 867-873
    • Lowenberger, C.1    Bulet, P.2    Charlet, M.3    Hetru, C.4    Hodgeman, B.5    Christensen, B.M.6
  • 14
    • 0025372569 scopus 로고
    • All-D amino acid-containing channel-forming antibiotic peptides
    • doi: 10.1073/pnas.87.12.4761
    • Wade D, Boman A, Wahlin B, Drain CM, Andreu D, Boman HG et al (1990) All-D amino acid-containing channel-forming antibiotic peptides. Proc Natl Acad Sci USA 88:4761-4765. doi: 10.1073/pnas.87.12.4761
    • (1990) Proc Natl Acad Sci USA , vol.88 , pp. 4761-4765
    • Wade, D.1    Boman, A.2    Wahlin, B.3    Drain, C.M.4    Andreu, D.5    Boman, H.G.6
  • 15
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptid forms voltage-dependent channels in Micrococcus luteus
    • Cociancich S, Ghazi A, Hetru C, Hoffmann JA, Letelliers L (1993) Insect defensin, an inducible antibacterial peptid forms voltage-dependent channels in Micrococcus luteus. J Biol Chem 268(26):19239-19245
    • (1993) J Biol Chem , vol.268 , Issue.26 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, C.3    Hoffmann, J.A.4    Letelliers, L.5
  • 16
    • 34249744522 scopus 로고    scopus 로고
    • Prediction of 3-dimentional structure of salivary odorant binding protein-2 of Culex quinquefasciatus
    • Paramasivan R, Sivaperumal R, Dhananjeyan KJ, Thenmozhi V, Tyagi BK (2007) Prediction of 3-dimentional structure of salivary odorant binding protein-2 of Culex quinquefasciatus. In Silico Biol 7:1-6
    • (2007) In Silico Biol , vol.7 , pp. 1-6
    • Paramasivan, R.1    Sivaperumal, R.2    Dhananjeyan, K.J.3    Thenmozhi, V.4    Tyagi, B.K.5
  • 17
    • 0036133186 scopus 로고    scopus 로고
    • Molecular modeling of insect ferritins
    • Pham DQ-D (2000) Molecular modeling of insect ferritins. In Silico Biol 2:S31-44
    • (2000) In Silico Biol , vol.2
    • Pham, D.Q.-D.1
  • 18
    • 0033605260 scopus 로고    scopus 로고
    • Dengue virus NS3 serine protease
    • doi: 10.1074/jbc.274.9.5573
    • Krishna Murthy HM, Clum S, Padmanabhan R (1999) Dengue virus NS3 serine protease. J Biol Chem 274(9):5573-5580. doi: 10.1074/jbc.274.9.5573
    • (1999) J Biol Chem , vol.274 , Issue.9 , pp. 5573-5580
    • Krishna Murthy, H.M.1    Clum, S.2    Padmanabhan, R.3
  • 19
    • 0032930982 scopus 로고    scopus 로고
    • Homology model of the dengue 2 virus NS3 protease: Putative interactions with both substrate and NS2B cofactor
    • Brinkworth RI, Fairlie DP, Leung D, Young PR (1999) Homology model of the dengue 2 virus NS3 protease: Putative interactions with both substrate and NS2B cofactor. J Gen Virol 80:1167-1177
    • (1999) J Gen Virol , vol.80 , pp. 1167-1177
    • Brinkworth, R.I.1    Fairlie, D.P.2    Leung, D.3    Young, P.R.4
  • 20
    • 10344248922 scopus 로고    scopus 로고
    • Enzymatic characterization and homology model of a catalytically active recombinant West Nile Virus NS3 protease
    • doi: 10.1074/jbc.M406810200
    • Nall TA, Chappell KJ, Stoermer MJ, Fang N-X, Tyndall JDA, Young PR et al (2004) Enzymatic characterization and homology model of a catalytically active recombinant West Nile Virus NS3 protease. J Biol Chem 279(47):48535-48542. doi: 10.1074/jbc.M406810200
    • (2004) J Biol Chem , vol.279 , Issue.47 , pp. 48535-48542
    • Nall, T.A.1    Chappell, K.J.2    Stoermer, M.J.3    Fang, N.-X.4    Tyndall, J.D.A.5    Young, P.R.6
  • 21
    • 13244281716 scopus 로고    scopus 로고
    • Site-directed mutagenesis and kinetic studies of the West Nile Virus NS3 protease identify key enzyme-substrate interactions
    • doi: 10.1074/jbc.M409931200
    • Chappell KJ, Nall TA, Stoermer MJ, Fang N-X, Tyndall JDA, Fairlie DP et al (2005) Site-directed mutagenesis and kinetic studies of the West Nile Virus NS3 protease identify key enzyme-substrate interactions. J Biol Chem 280(4):2896-2903. doi: 10.1074/jbc.M409931200
    • (2005) J Biol Chem , vol.280 , Issue.4 , pp. 2896-2903
    • Chappell, K.J.1    Nall, T.A.2    Stoermer, M.J.3    Fang, N.-X.4    Tyndall, J.D.A.5    Fairlie, D.P.6
  • 22
    • 22144472217 scopus 로고    scopus 로고
    • Domain based homology modeling and mapping of the conformational epitopes of envelope glycoprotein of West Nile virus
    • doi: 10.1007/s00894-005-0272-7
    • Vijayasri S, Agrawal S (2005) Domain based homology modeling and mapping of the conformational epitopes of envelope glycoprotein of West Nile virus. J Mol Model 11(3):248-255. doi: 10.1007/s00894-005-0272-7
    • (2005) J Mol Model , vol.11 , Issue.3 , pp. 248-255
    • Vijayasri, S.1    Agrawal, S.2
  • 23
    • 33750066620 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics study of West Nile Virus NS3 protease: A molecular basis for the catalytic activity increased by the NS2B cofactor
    • doi: 10.1002/prot.21129
    • Zhou H, Singh NJ, Kim KS (2006) Homology modeling and molecular dynamics study of West Nile Virus NS3 protease: A molecular basis for the catalytic activity increased by the NS2B cofactor. Proteins 65:692-701. doi: 10.1002/prot.21129
    • (2006) Proteins , vol.65 , pp. 692-701
    • Zhou, H.1    Singh, N.J.2    Kim, K.S.3
  • 24
    • 0035812694 scopus 로고    scopus 로고
    • Protein Structure Prediction and Structural Genomics
    • doi: 10.1126/science.1065659
    • Baker D, Sali A (2001) Protein Structure Prediction and Structural Genomics. Science 294:93-96. doi: 10.1126/science.1065659
    • (2001) Science , vol.294 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 25
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli DJ, Hunter HN, Aseyev V, Starner TD, Wiencek JM, McCray Jr. PB, Tack BF, Vogel HJ (2002) The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J Biol Chem 277:8279-8289
    • (2002) J Biol Chem , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray Jr., P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 27
    • 33947383052 scopus 로고    scopus 로고
    • Modelling study of dimerization in mammalian defensins
    • doi: 10.1186/1471-2105-7-S5-S17
    • Suresh A, Verma C (2006) Modelling study of dimerization in mammalian defensins. BMC Bioinformatics 7(Suppl 5):S17. doi: 10.1186/ 1471-2105-7-S5-S17
    • (2006) BMC Bioinformatics , vol.7 , Issue.SUPPL. 5
    • Suresh, A.1    Verma, C.2
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • doi: 10.1093/nar/22.22.4673
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680. doi: 10.1093/nar/22.22.4673
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • doi: 10.1016/S0076-6879(96)66024-8
    • Higgins DG, Thompson JD, Gibson TJ (1996) Using CLUSTAL for multiple sequence alignments. Methods Enzymol 266:383-402. doi: 10.1016/ S0076-6879(96)66024-8
    • (1996) Methods Enzymol , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 31
    • 0003437299 scopus 로고    scopus 로고
    • Distributed by the author. Department of Genomic Studies, University of Washington, Seattle
    • Felsentein J (2004) PHYLIP (Phylogeny Inference Package) version 3.6. Distributed by the author. Department of Genomic Studies, University of Washington, Seattle.
    • (2004) PHYLIP (Phylogeny Inference Package) Version 3.6
    • Felsentein, J.1
  • 32
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8:275-282
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 33
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • doi: 10.1006/jmbi.1993.1626
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779-815. doi: 10.1006/ jmbi.1993.1626
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • doi: 10.1107/S0021889892009944
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291. doi: 10.1107/S0021889892009944
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 0028892389 scopus 로고
    • Are proteins ideal mixtures of amino acids? Analysis of energy parameter sets
    • Godzik A, Kolinski A, Skolnick J (1995) Are proteins ideal mixtures of amino acids? Analysis of energy parameter sets. Protein Sci 4(10):2107-2117
    • (1995) Protein Sci , vol.4 , Issue.10 , pp. 2107-2117
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 37
    • 0030584681 scopus 로고    scopus 로고
    • Knowledge-based potentials for protein folding: What can we learn from known protein structures?
    • doi: 10.1016/S0969-2126(96)00041-X
    • Godzik A (1996) Knowledge-based potentials for protein folding: What can we learn from known protein structures? Structure 4(4):363-366. doi: 10.1016/S0969-2126(96)00041-X
    • (1996) Structure , vol.4 , Issue.4 , pp. 363-366
    • Godzik, A.1
  • 38
    • 0031300844 scopus 로고    scopus 로고
    • Multiple model approach-dealing with alignment ambiguities in protein modeling
    • Pawlowski K, Jaroszewski L, Bierzynski A, Godzik A (1997) Multiple model approach-dealing with alignment ambiguities in protein modeling. Pac Symp Biocomput 1997:328-339
    • (1997) Pac Symp Biocomput , vol.1997 , pp. 328-339
    • Pawlowski, K.1    Jaroszewski, L.2    Bierzynski, A.3    Godzik, A.4
  • 39
    • 0005922294 scopus 로고    scopus 로고
    • Multiple model approach: Exploring the limits of comparative modeling
    • doi: 10.1007/s008940050087
    • Jaroszewski L, Pawlowski K, Godzik A (1998) Multiple model approach: exploring the limits of comparative modeling. J Mol Model 4:294-309. doi: 10.1007/s008940050087
    • (1998) J Mol Model , vol.4 , pp. 294-309
    • Jaroszewski, L.1    Pawlowski, K.2    Godzik, A.3
  • 40
    • 0029644729 scopus 로고
    • Refined three-dimensional solution structure of insect defensin A
    • doi: 10.1016/S0969-2126(01)00177-0
    • Cornet B, Bonmatin JM, Hetru C, Hoffmann JA, Ptak M, Vovelle F (1995) Refined three-dimensional solution structure of insect defensin A. Structure 3:435-448. doi: 10.1016/S0969-2126(01)00177-0
    • (1995) Structure , vol.3 , pp. 435-448
    • Cornet, B.1    Bonmatin, J.M.2    Hetru, C.3    Hoffmann, J.A.4    Ptak, M.5    Vovelle, F.6
  • 41
    • 0025195471 scopus 로고
    • 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin
    • doi: 10.1016/0014-5793(90)81206-4
    • Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F et al (1990) 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin. FEBS Lett 269:413-420. doi: 10.1016/0014-5793(90)81206-4
    • (1990) FEBS Lett , vol.269 , pp. 413-420
    • Hanzawa, H.1    Shimada, I.2    Kuzuhara, T.3    Komano, H.4    Kohda, D.5    Inagaki, F.6
  • 43
    • 15044362791 scopus 로고    scopus 로고
    • Homology modeling
    • In: Bourne PE, Weissig H (eds) Wiley-Liss, New York
    • Krieger E, Nabuurs SB, Vriend G (2003) Homology modeling. In: Bourne PE, Weissig H (eds) Structural bioinformatics. Wiley-Liss, New York, pp 507-521
    • (2003) Structural Bioinformatics , pp. 507-521
    • Krieger, E.1    Nabuurs, S.B.2    Vriend, G.3


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