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Volumn 6, Issue 5, 2010, Pages 491-498

Identification and molecular characterization of a new member of the Peritrophic membrane proteins from the meadow moth, Loxostege Sticticalis

Author keywords

Chitin binding activity; Loxostege sticticalis; Lsti99; Peritrophic membrane protein; Recombinant protein

Indexed keywords

HEXAPODA; LEPIDOPTERA; LOXOSTEGE STICTICALIS;

EID: 77956969910     PISSN: 14492288     EISSN: None     Source Type: Journal    
DOI: 10.7150/ijbs.6.491     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0030891189 scopus 로고    scopus 로고
    • Peritrophic matrix structure and function
    • Lehane MJ. Peritrophic matrix structure and function. Annu Rev Entomol. 1997; 42: 525-50.
    • (1997) Annu Rev Entomol , vol.42 , pp. 525-550
    • Lehane, M.J.1
  • 3
    • 0035377001 scopus 로고    scopus 로고
    • The peritrophic membrane of Spodoptera frugiperda: Secretion of peritrophins and role in immobilization and recycling digestive enzymes
    • Bolognesi R, Ribeiro AF, Terra WR, et al. The peritrophic membrane of Spodoptera frugiperda: secretion of peritrophins and role in immobilization and recycling digestive enzymes. Arch Insect Biochem Physiol. 2001; 47: 62-75.
    • (2001) Arch Insect Biochem Physiol , vol.47 , pp. 62-75
    • Bolognesi, R.1    Ribeiro, A.F.2    Terra, W.R.3
  • 4
    • 0036009748 scopus 로고    scopus 로고
    • Aedes aegypti peritrophic matrix and its interaction with heme during blood digestion
    • Pascoa V, Oliveira PL, Dansa-Petretski M, et al. Aedes aegypti peritrophic matrix and its interaction with heme during blood digestion. Insect Biochem Mol Biol. 2002; 32: 517-23.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 517-523
    • Pascoa, V.1    Oliveira, P.L.2    Dansa-Petretski, M.3
  • 5
    • 0036000565 scopus 로고    scopus 로고
    • Glucosamine: Fructose-6-phosphate aminotransferase: Gene characterization, chitin biosynthesis and peritrophic matrix formation in Aedes aegypti
    • Kato N, Dasgupta R, Smartt C, et al. Glucosamine: fructose-6-phosphate aminotransferase: gene characterization, chitin biosynthesis and peritrophic matrix formation in Aedes aegypti. Insect Mol Biol. 2002; 11: 207-16.
    • (2002) Insect Mol Biol , vol.11 , pp. 207-216
    • Kato, N.1    Dasgupta, R.2    Smartt, C.3
  • 6
    • 0030740231 scopus 로고    scopus 로고
    • Antibody-mediated inhibition of the growth of larvae from an insect causing sutaneous myiasis in a mammalian host
    • Casu R, Eisemann C, Pearson R, et al. Antibody-mediated inhibition of the growth of larvae from an insect causing sutaneous myiasis in a mammalian host. Proc Natl Acad Sci USA. 1997; 94: 8939-8944.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8939-8944
    • Casu, R.1    Eisemann, C.2    Pearson, R.3
  • 7
    • 20544437456 scopus 로고    scopus 로고
    • Identification and characterization of a novel peritrophic matrix protein, Ae-Aper50, and the microvillar membrane protein, AEG12, from the mosquito, Aedes aegypti
    • Shao L, Devenport M, Fujioka H, et al. Identification and characterization of a novel peritrophic matrix protein, Ae-Aper50, and the microvillar membrane protein, AEG12, from the mosquito, Aedes aegypti. Insect Biochem Mol Biol. 2005; 35: 947-59.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 947-959
    • Shao, L.1    Devenport, M.2    Fujioka, H.3
  • 8
    • 0029945647 scopus 로고    scopus 로고
    • Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina: CDNA and deduced amino acid sequences
    • Elvin C, Vuocolo T, Pearson R, et al. Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina: cDNA and deduced amino acid sequences. J Biol Chem. 1996; 271: 8925-35.
    • (1996) J Biol Chem , vol.271 , pp. 8925-8935
    • Elvin, C.1    Vuocolo, T.2    Pearson, R.3
  • 9
    • 0032004767 scopus 로고    scopus 로고
    • cDNA and deduced amino acid sequences of a peritrophic membrane glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina
    • Schorderet S, Pearson RD, Vuocolo T, et al. cDNA and deduced amino acid sequences of a peritrophic membrane glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina. Insect Biochem Mol Biol. 1998; 28: 99-111.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 99-111
    • Schorderet, S.1    Pearson, R.D.2    Vuocolo, T.3
  • 10
    • 0035805550 scopus 로고    scopus 로고
    • A novel family of chitin-binding proteins from insect type 2 peritrophic matrix. cDNA sequences, chitin binding activity, and cellular localization
    • Wijffels G, Eisemann C, Riding G, et al. A novel family of chitin-binding proteins from insect type 2 peritrophic matrix. cDNA sequences, chitin binding activity, and cellular localization. J Biol Chem. 2001; 276: 15527-36.
    • (2001) J Biol Chem , vol.276 , pp. 15527-15536
    • Wijffels, G.1    Eisemann, C.2    Riding, G.3
  • 11
    • 0037310390 scopus 로고    scopus 로고
    • Identification of an immunoprotective mucin-like protein, peritrophin-55, from the peritrophic matrix of Lucilia cuprina larvae
    • Tellam RL, Vuocolo T, Eisemann C, et al. Identification of an immunoprotective mucin-like protein, peritrophin-55, from the peritrophic matrix of Lucilia cuprina larvae. Insect Biochem Mol Biol. 2003; 33: 239-52.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 239-252
    • Tellam, R.L.1    Vuocolo, T.2    Eisemann, C.3
  • 12
    • 0030985902 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of a novel invertebrate intestinal mucin cDNA
    • Wang P, Granados RR. Molecular cloning and sequencing of a novel invertebrate intestinal mucin cDNA. J Biol Chem. 1997; 272: 16663-9.
    • (1997) J Biol Chem , vol.272 , pp. 16663-16669
    • Wang, P.1    Granados, R.R.2
  • 13
    • 0035377371 scopus 로고    scopus 로고
    • Molecular structure of the peritrophic membrane (PM): Identification of potential PM target sites for insect control
    • Wang P, Granados RR. Molecular structure of the peritrophic membrane (PM): identification of potential PM target sites for insect control. Arch Insect Biochem Physiol. 2001; 47: 110-8.
    • (2001) Arch Insect Biochem Physiol , vol.47 , pp. 110-118
    • Wang, P.1    Granados, R.R.2
  • 14
    • 0032504233 scopus 로고    scopus 로고
    • A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression and characterization
    • Shen Z, Jacobs-Lorena M. A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression and characterization. J Biol Chem. 1998; 273: 17665-70.
    • (1998) J Biol Chem , vol.273 , pp. 17665-17670
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 15
    • 17444401719 scopus 로고    scopus 로고
    • Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae
    • Devenport M, Fujioka H, Donnelly M, et al. Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae. Cell Tissue Res. 2005; 320: 175-85.
    • (2005) Cell Tissue Res , vol.320 , pp. 175-185
    • Devenport, M.1    Fujioka, H.2    Donnelly, M.3
  • 16
    • 0035954586 scopus 로고    scopus 로고
    • Identification and molecular characterization of a peritrophin gene, peritrophin-48, from the myiasis fly Chrysomya bezziana
    • Vuocolo T, Eisemann CH, Pearson RD, et al. Identification and molecular characterization of a peritrophin gene, peritrophin-48, from the myiasis fly Chrysomya bezziana. Insect Biochem Mol Biol. 2001; 31: 919-32.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 919-932
    • Vuocolo, T.1    Eisemann, C.H.2    Pearson, R.D.3
  • 17
    • 0036890738 scopus 로고    scopus 로고
    • Proventriculus-specific cDNAs characterized from the tsetse, Glossina morsitans morsitans
    • Hao Z, Aksoy S. Proventriculus-specific cDNAs characterized from the tsetse, Glossina morsitans morsitans. Insect Biochem Mol Biol. 2002; 32: 1663-71.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1663-1671
    • Hao, Z.1    Aksoy, S.2
  • 18
    • 0043166470 scopus 로고    scopus 로고
    • Characterization of an intestinal mucin from the peritrophic matrix of the diamondback moth, Plutella xylostella
    • Sarauer BL, Gillott C, Hegedust D. Characterization of an intestinal mucin from the peritrophic matrix of the diamondback moth, Plutella xylostella. Insect Mol Biol. 2003; 12: 333-43.
    • (2003) Insect Mol Biol , vol.12 , pp. 333-343
    • Sarauer, B.L.1    Gillott, C.2    Hegedust, D.3
  • 19
    • 4744351644 scopus 로고    scopus 로고
    • Modeling the structure of the type I peritrophic matrix: Characterization of a Mamestra configurata intestinal mucin and a novel peritrophin containing 19 chitin binding domains
    • Shi X, Chamankhah M, Visal-Shah S, et al. Modeling the structure of the type I peritrophic matrix: characterization of a Mamestra configurata intestinal mucin and a novel peritrophin containing 19 chitin binding domains. Insect Biochem Mol Biol. 2004; 34: 1101-15.
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 1101-1115
    • Shi, X.1    Chamankhah, M.2    Visal-Shah, S.3
  • 20
    • 77956956904 scopus 로고    scopus 로고
    • A Method of rapid and efficient isolation of highly specific antibodies from an antiserum against a pool of proteins
    • Zhang X, Li J, Guo W, et al. A Method of rapid and efficient isolation of highly specific antibodies from an antiserum against a pool of proteins. Acta Agri boreali-sinica. 2008; 23: 111-3.
    • (2008) Acta Agri Boreali-sinica , vol.23 , pp. 111-113
    • Zhang, X.1    Li, J.2    Guo, W.3
  • 21
    • 77955175530 scopus 로고    scopus 로고
    • Diapause termination, post-diapause development and reproduction in the beet webworm, Loxostege sticticalis (Lepidoptera: Pyralidae)
    • Jiang XF, Huang SH, Luo LZ, et al. Diapause termination, post-diapause development and reproduction in the beet webworm, Loxostege sticticalis (Lepidoptera: Pyralidae). J Insect Physiol. 2010; 56:1325-31.
    • (2010) J Insect Physiol , vol.56 , pp. 1325-1331
    • Jiang, X.F.1    Huang, S.H.2    Luo, L.Z.3
  • 22
    • 1242322069 scopus 로고    scopus 로고
    • Identification of two new peritrophic membrane proteins from larval Trichoplusia ni: Structural characteristics and their functions in the protease rich insect gut
    • Wang P, Li G, Granados RR. Identification of two new peritrophic membrane proteins from larval Trichoplusia ni: structural characteristics and their functions in the protease rich insect gut. Insect Biochem Mol Biol. 2004; 34: 215-27.
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 215-227
    • Wang, P.1    Li, G.2    Granados, R.R.3
  • 23
    • 26244457216 scopus 로고    scopus 로고
    • A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni
    • Guo W, Li G, Pang Y, et al. A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni. Insect Biochem Mol Biol. 2005; 35: 1224-34.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 1224-1234
    • Guo, W.1    Li, G.2    Pang, Y.3
  • 24
    • 48249103129 scopus 로고    scopus 로고
    • Expression of EGFP-spider dragline silk fusion protein in BmN cells and larvae of silkworm showed the solubility is primary limit for dragline proteins yield
    • Zhang Y, Hu J, Miao Y, et al. Expression of EGFP-spider dragline silk fusion protein in BmN cells and larvae of silkworm showed the solubility is primary limit for dragline proteins yield. Mol Biol Rep. 2008; 35: 329-35.
    • (2008) Mol Biol Rep , vol.35 , pp. 329-335
    • Zhang, Y.1    Hu, J.2    Miao, Y.3
  • 25
    • 0344305750 scopus 로고    scopus 로고
    • Granados RR. Rapid and efficient isolation of highly specific antibodies from an antiserum against a pool of proteins
    • Wang P, Granados RR. Rapid and efficient isolation of highly specific antibodies from an antiserum against a pool of proteins. Biotech Histochem. 2003; 78: 201-5.
    • (2003) Biotech Histochem , vol.78 , pp. 201-205
    • Wang, P.1
  • 26
    • 0033975247 scopus 로고    scopus 로고
    • Calcofluor disrupts the midgut defense system in insects
    • Wang P, Granados RR. Calcofluor disrupts the midgut defense system in insects. Insect Biochem Mol Biol. 2000; 30:135-43.
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 135-143
    • Wang, P.1    Granados, R.R.2
  • 27
    • 21244495294 scopus 로고    scopus 로고
    • Molecular characterization and expression of prothoracicotropic hormone during development and pupal diapause in the cotton bollworm, Helicoverpa armigera
    • Wei ZJ, Zhang QR, Kang L, et al. Molecular characterization and expression of prothoracicotropic hormone during development and pupal diapause in the cotton bollworm, Helicoverpa armigera. J Insect Physiol. 2005; 51: 691-700
    • (2005) J Insect Physiol , vol.51 , pp. 691-700
    • Wei, Z.J.1    Zhang, Q.R.2    Kang, L.3
  • 28
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • Altschul SF, Gish W, Miller W, et al. Basic local alignment search tool. J Mol Biol. 1990; 215: 403-10.
    • (1990) J Mol Biol , vol.215 , pp. 403-410
    • Altschul, S.F.1    Gish, W.2    Miller, W.3
  • 29
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen JD, Nielsen H, von Heijne G, et al. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol. 2004; 340: 783-95.
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3
  • 30
    • 0031809552 scopus 로고    scopus 로고
    • Net Oglyc: Prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility
    • Hansen JE, Lund O, Tolstrup N, et al. Net Oglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility. Glycoconjugate J. 1998; 15: 115-30.
    • (1998) Glycoconjugate J , vol.15 , pp. 115-130
    • Hansen, J.E.1    Lund, O.2    Tolstrup, N.3
  • 31
    • 0036084361 scopus 로고    scopus 로고
    • The PROSITE database, its status in 2002
    • Falquet L, Pagni M, Bucher P, et al. The PROSITE database, its status in 2002. Nucleic Acids Res. 2002; 30: 235-8.
    • (2002) Nucleic Acids Res , vol.30 , pp. 235-238
    • Falquet, L.1    Pagni, M.2    Bucher, P.3
  • 32
    • 0030990106 scopus 로고    scopus 로고
    • An intestinal mucin is the target substrate for a baculovirus enhancin
    • Wang P, Granados RR. An intestinal mucin is the target substrate for a baculovirus enhancin. Proc Natl Acad Sci USA. 1997; 94: 6977-82.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6977-6982
    • Wang, P.1    Granados, R.R.2


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