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Volumn 39, Issue 2, 2009, Pages 125-134

The Anopheles gambiae adult midgut peritrophic matrix proteome

Author keywords

Anopheles gambiae; Mosquito; Peritrophic matrix; Proteome

Indexed keywords

INSECT PROTEIN; PROTEOME; SCLEROPROTEIN;

EID: 60549116151     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2008.10.010     Document Type: Article
Times cited : (107)

References (52)
  • 1
    • 0026742343 scopus 로고
    • The role of the mosquito peritrophic membrane in bloodmeal digestion and infectivity of Plasmodium species
    • Billingsley P.F., and Rudin W. The role of the mosquito peritrophic membrane in bloodmeal digestion and infectivity of Plasmodium species. J. Parasitol. 78 (1992) 430-440
    • (1992) J. Parasitol. , vol.78 , pp. 430-440
    • Billingsley, P.F.1    Rudin, W.2
  • 2
    • 36348954396 scopus 로고    scopus 로고
    • A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm
    • Broehan G., Zimoch L., Wessels A., Ertas B., and Merzendorfer H. A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm. J. Exp. Biol. 210 (2007) 3636-3643
    • (2007) J. Exp. Biol. , vol.210 , pp. 3636-3643
    • Broehan, G.1    Zimoch, L.2    Wessels, A.3    Ertas, B.4    Merzendorfer, H.5
  • 3
    • 20544450751 scopus 로고    scopus 로고
    • The peritrophic matrix of hematophagous insects
    • Marquardt W. (Ed), Elsevier Academic Press, New York
    • Devenport M., and Jacobs-Lorena M. The peritrophic matrix of hematophagous insects. In: Marquardt W. (Ed). Biology of Disease Vectors. second ed. (2005), Elsevier Academic Press, New York 297-310
    • (2005) Biology of Disease Vectors. second ed. , pp. 297-310
    • Devenport, M.1    Jacobs-Lorena, M.2
  • 4
    • 3943069803 scopus 로고    scopus 로고
    • Storage and secretion of the peritrophic matrix protein Ag-Aper1 and trypsin in the midgut of Anopheles gambiae
    • Devenport M., Fujioka H., and Jacobs-Lorena M. Storage and secretion of the peritrophic matrix protein Ag-Aper1 and trypsin in the midgut of Anopheles gambiae. Insect Mol. Biol. 13 (2004) 349-358
    • (2004) Insect Mol. Biol. , vol.13 , pp. 349-358
    • Devenport, M.1    Fujioka, H.2    Jacobs-Lorena, M.3
  • 5
    • 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-Doman M., Shen Z., and Jacobs-Lorena M. Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae. Cell Tissue Res. 320 (2005) 175-185
    • (2005) Cell Tissue Res. , vol.320 , pp. 175-185
    • Devenport, M.1    Fujioka, H.2    Donnelly-Doman, M.3    Shen, Z.4    Jacobs-Lorena, M.5
  • 7
    • 0029803741 scopus 로고    scopus 로고
    • Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae
    • Dimopoulos G., Richman A., della Torre A., Kafatos F.C., and Louis C. Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae. Proc. Natl. Acad. Sci. U.S.A. 23 (1996) 13066-13071
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.23 , pp. 13066-13071
    • Dimopoulos, G.1    Richman, A.2    della Torre, A.3    Kafatos, F.C.4    Louis, C.5
  • 8
    • 0032476592 scopus 로고    scopus 로고
    • Malaria infection of the mosquito Anopheles gambiae activates immune-responsive genes during critical transition stages of the parasite life cycle
    • Dimopoulos G., Seeley D., Wolf A., and Kafatos F.C. Malaria infection of the mosquito Anopheles gambiae activates immune-responsive genes during critical transition stages of the parasite life cycle. EMBO J 21 (1998) 6115-6123
    • (1998) EMBO J , vol.21 , pp. 6115-6123
    • Dimopoulos, G.1    Seeley, D.2    Wolf, A.3    Kafatos, F.C.4
  • 9
    • 28444479128 scopus 로고    scopus 로고
    • Insight into a conserved lifestyle: protein-carbohydrate adhesion strategies of vector-borne pathogens
    • Dinglasan R.R., and Jacobs-Lorena M. Insight into a conserved lifestyle: protein-carbohydrate adhesion strategies of vector-borne pathogens. Infect. Immun. 73 (2005) 7797-7807
    • (2005) Infect. Immun. , vol.73 , pp. 7797-7807
    • Dinglasan, R.R.1    Jacobs-Lorena, M.2
  • 11
    • 0031427314 scopus 로고    scopus 로고
    • Rapid induction by a blood meal of a carboxypeptidase gene in the gut of the mosquito Anopheles gambiae
    • Edwards M.J., Lemos F.J., Donnelly-Doman M., and Jacobs-Lorena M. Rapid induction by a blood meal of a carboxypeptidase gene in the gut of the mosquito Anopheles gambiae. Insect Biochem. Mol. Biol. 27 (1997) 1063-1072
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 1063-1072
    • Edwards, M.J.1    Lemos, F.J.2    Donnelly-Doman, M.3    Jacobs-Lorena, M.4
  • 12
    • 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.M., Vuocolo T., Pearson R.D., East I.J., Riding G.A., Eisemann C.H., and Tellam R.L. Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences. J. Biol. Chem. 271 (1996) 8925-8935
    • (1996) J. Biol. Chem. , vol.271 , pp. 8925-8935
    • Elvin, C.M.1    Vuocolo, T.2    Pearson, R.D.3    East, I.J.4    Riding, G.A.5    Eisemann, C.H.6    Tellam, R.L.7
  • 13
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., McCormack A.L., and Yates J.R.I. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5 (1994) 979
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 979
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.I.3
  • 14
    • 0036529479 scopus 로고    scopus 로고
    • An efficient algorithm for large-scale detection of protein families
    • Enright A.J., Van Dongen S., and Ouzounis C.A. An efficient algorithm for large-scale detection of protein families. Nucleic Acids Res. 7 (2002) 1575-1584
    • (2002) Nucleic Acids Res. , vol.7 , pp. 1575-1584
    • Enright, A.J.1    Van Dongen, S.2    Ouzounis, C.A.3
  • 15
    • 33746500659 scopus 로고    scopus 로고
    • Proteomic analysis by multidimensional protein identification technology
    • Florens L., and Washburn M.P. Proteomic analysis by multidimensional protein identification technology. Methods Mol. Biol (2006) 159-175
    • (2006) Methods Mol. Biol , pp. 159-175
    • Florens, L.1    Washburn, M.P.2
  • 16
    • 0007493585 scopus 로고
    • Feeding response in Aedes aegypti: stimulation by adenosine triphosphate
    • Galun R., Avi-Dor Y., and Bar-Zeev M. Feeding response in Aedes aegypti: stimulation by adenosine triphosphate. Science 3600 (1963) 1674-1675
    • (1963) Science , vol.3600 , pp. 1674-1675
    • Galun, R.1    Avi-Dor, Y.2    Bar-Zeev, M.3
  • 17
    • 0034643804 scopus 로고    scopus 로고
    • Sp22D: a multidomain serine protease with a putative role in insect immunity
    • Gorman M.J., Andreeva O.V., and Paskewitz S.M. Sp22D: a multidomain serine protease with a putative role in insect immunity. Gene 251 (2000) 9-17
    • (2000) Gene , vol.251 , pp. 9-17
    • Gorman, M.J.1    Andreeva, O.V.2    Paskewitz, S.M.3
  • 18
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: high-performance signaling in networked arrays
    • Hazelbauer G.L., Falke J.J., and Parkinson J.S. Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem. Sci. 33 (2008) 9-19
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 9-19
    • Hazelbauer, G.L.1    Falke, J.J.2    Parkinson, J.S.3
  • 20
    • 0025857170 scopus 로고
    • Malaria parasite chitinase and penetration of the mosquito peritrophic membrane
    • Huber M., Cabib E., and Miller L.H. Malaria parasite chitinase and penetration of the mosquito peritrophic membrane. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 2807-2810
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2807-2810
    • Huber, M.1    Cabib, E.2    Miller, L.H.3
  • 21
    • 0018341656 scopus 로고
    • Identification of a methyl-accepting chemotaxis protein for the ribose and galactose chemoreceptors of Escherichia coli
    • Kondoh H., Ball C.B., and Adler J. Identification of a methyl-accepting chemotaxis protein for the ribose and galactose chemoreceptors of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 260-264
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 260-264
    • Kondoh, H.1    Ball, C.B.2    Adler, J.3
  • 22
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., and Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54 (1985) 631-664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 23
    • 0036139267 scopus 로고    scopus 로고
    • Identification of novel Plasmodium gallinaceum zygote- and ookinete-expressed proteins as targets for blocking malaria transmission
    • Langer R.C., Li F., and Vinetz J.M. Identification of novel Plasmodium gallinaceum zygote- and ookinete-expressed proteins as targets for blocking malaria transmission. Infect. Immun. 70 (2002) 102-106
    • (2002) Infect. Immun. , vol.70 , pp. 102-106
    • Langer, R.C.1    Li, F.2    Vinetz, J.M.3
  • 24
    • 0036179634 scopus 로고    scopus 로고
    • Monoclonal antibody against the Plasmodium falciparum chitinase, PfCHT1, recognizes a malaria transmission-blocking epitope in Plasmodium gallinaceum ookinetes unrelated to the chitinase PgCHT1
    • Langer R.C., Li F., Popov V., Kurosky A., and Vinetz J.M. Monoclonal antibody against the Plasmodium falciparum chitinase, PfCHT1, recognizes a malaria transmission-blocking epitope in Plasmodium gallinaceum ookinetes unrelated to the chitinase PgCHT1. Infect. Immun. 70 (2002) 1581-1590
    • (2002) Infect. Immun. , vol.70 , pp. 1581-1590
    • Langer, R.C.1    Li, F.2    Popov, V.3    Kurosky, A.4    Vinetz, J.M.5
  • 25
    • 0030186191 scopus 로고    scopus 로고
    • Trypsin and aminopeptidase gene expression is affected by age and food composition in Anopheles gambiae
    • Lemos F.J., Cornel A.J., and Jacobs-Lorena M. Trypsin and aminopeptidase gene expression is affected by age and food composition in Anopheles gambiae. Insect Biochem. Mol. Biol. 26 (1996) 651-658
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 651-658
    • Lemos, F.J.1    Cornel, A.J.2    Jacobs-Lorena, M.3
  • 26
    • 2942705911 scopus 로고    scopus 로고
    • Plasmodium ookinete-secreted proteins secreted through a common micronemal pathway are targets of blocking malaria transmission
    • Li F., Templeton T.J., Popov V., Comer J.E., Tsuboi T., Torii M., and Vinetz J.M. Plasmodium ookinete-secreted proteins secreted through a common micronemal pathway are targets of blocking malaria transmission. J. Biol. Chem. 279 (2004) 26635-26644
    • (2004) J. Biol. Chem. , vol.279 , pp. 26635-26644
    • Li, F.1    Templeton, T.J.2    Popov, V.3    Comer, J.E.4    Tsuboi, T.5    Torii, M.6    Vinetz, J.M.7
  • 27
    • 0030293932 scopus 로고    scopus 로고
    • Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti
    • Moskalyk L.A., Oo M.M., and Jacobs-Lorena M. Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti. Insect Mol. Biol. 5 (1996) 261-268
    • (1996) Insect Mol. Biol. , vol.5 , pp. 261-268
    • Moskalyk, L.A.1    Oo, M.M.2    Jacobs-Lorena, M.3
  • 28
    • 0027296176 scopus 로고
    • Members of a trypsin gene family in Anopheles gambiae are induced in the gut by blood meal
    • Muller H.M., Crampton J.M., della Torre A., Sinden R., and Crisanti A. Members of a trypsin gene family in Anopheles gambiae are induced in the gut by blood meal. EMBO J 7 (1993) 2891-2900
    • (1993) EMBO J , vol.7 , pp. 2891-2900
    • Muller, H.M.1    Crampton, J.M.2    della Torre, A.3    Sinden, R.4    Crisanti, A.5
  • 29
    • 0027638384 scopus 로고
    • Temporal and spatial expression of serine protease genes in Anopheles gambiae
    • Muller H.M., Vizioli I., della Torre A., and Crisanti A. Temporal and spatial expression of serine protease genes in Anopheles gambiae. Parassitologia (1993) 73-76
    • (1993) Parassitologia , pp. 73-76
    • Muller, H.M.1    Vizioli, I.2    della Torre, A.3    Crisanti, A.4
  • 32
    • 0037244415 scopus 로고    scopus 로고
    • The heterogeneity of mast cell tryptase from human lung and skin
    • Peng Q., McEuen A.R., Benyon R.C., and Walls A.F. The heterogeneity of mast cell tryptase from human lung and skin. Eur. J. Biochem. 270 (2003) 270-283
    • (2003) Eur. J. Biochem. , vol.270 , pp. 270-283
    • Peng, Q.1    McEuen, A.R.2    Benyon, R.C.3    Walls, A.F.4
  • 34
    • 0028773123 scopus 로고
    • Peritrophic matrix of the black fly Simulium vittatum: formation, structure, and analysis of its protein components
    • Ramos A., Mahowald A., and Jacobs-Lorena M. Peritrophic matrix of the black fly Simulium vittatum: formation, structure, and analysis of its protein components. J. Exp. Zool. 268 (1994) 269-281
    • (1994) J. Exp. Zool. , vol.268 , pp. 269-281
    • Ramos, A.1    Mahowald, A.2    Jacobs-Lorena, M.3
  • 35
    • 0043166470 scopus 로고    scopus 로고
    • Characterization of an intestinal mucin from the peritrophic matrix of the diamondback moth, Plutella xylostella
    • Sarauer B.L., Gillott C., and Hegedus D. Characterization of an intestinal mucin from the peritrophic matrix of the diamondback moth, Plutella xylostella. Insect Mol. Biol. 12 (2003) 333-343
    • (2003) Insect Mol. Biol. , vol.12 , pp. 333-343
    • Sarauer, B.L.1    Gillott, C.2    Hegedus, D.3
  • 36
    • 0027308860 scopus 로고
    • Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease
    • Shahabuddin M., Toyoshima T., Aikawa M., and Kaslow D.C. Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 4266-4270
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 4266-4270
    • Shahabuddin, M.1    Toyoshima, T.2    Aikawa, M.3    Kaslow, D.C.4
  • 37
    • 0030044285 scopus 로고    scopus 로고
    • Antibody-mediated inhibition of Aedes Aegypti midgut trypsins blocks sporogonic development of Plasmodium gallinaceum
    • Shahabuddin M., Lemos F.J., Kaslow D.C., and Jacobs-Lorena M. Antibody-mediated inhibition of Aedes Aegypti midgut trypsins blocks sporogonic development of Plasmodium gallinaceum. Infect. Immun. 64 (1996) 739-743
    • (1996) Infect. Immun. , vol.64 , pp. 739-743
    • Shahabuddin, M.1    Lemos, F.J.2    Kaslow, D.C.3    Jacobs-Lorena, M.4
  • 39
    • 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., Ghosh A., and Jacobs-Lorena M. 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. 35 (2005) 947-959
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 947-959
    • Shao, L.1    Devenport, M.2    Fujioka, H.3    Ghosh, A.4    Jacobs-Lorena, M.5
  • 40
    • 0030665155 scopus 로고    scopus 로고
    • Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae
    • Shen Z., and Jacobs-Lorena M. Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae. J. Biol. Chem. 272 (1997) 28895-28900
    • (1997) J. Biol. Chem. , vol.272 , pp. 28895-28900
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 41
    • 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., and 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. 273 (1998) 17665-17670
    • (1998) J. Biol. Chem. , vol.273 , pp. 17665-17670
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 42
    • 0033007284 scopus 로고    scopus 로고
    • Evolution of chitin-binding proteins in invertebrates
    • Shen Z., and Jacobs-Lorena M. Evolution of chitin-binding proteins in invertebrates. J. Mol. Evol. 48 (1999) 341-347
    • (1999) J. Mol. Evol. , vol.48 , pp. 341-347
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 43
    • 0033545975 scopus 로고    scopus 로고
    • A cell surface mucin specifically expressed in the midgut of the malaria mosquito Anopheles gambiae
    • Shen Z., Dimopoulos G., Kafatos F.C., and Jacobs-Lorena M. A cell surface mucin specifically expressed in the midgut of the malaria mosquito Anopheles gambiae. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 5610-5615
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 5610-5615
    • Shen, Z.1    Dimopoulos, G.2    Kafatos, F.C.3    Jacobs-Lorena, M.4
  • 44
    • 3943084209 scopus 로고    scopus 로고
    • Identification and molecular characterization of two immune-responsive chitinase-like proteins from Anopheles gambiae
    • Shi L., and Paskewitz S.M. Identification and molecular characterization of two immune-responsive chitinase-like proteins from Anopheles gambiae. Insect Mol. Biol. 13 (2004) 387-398
    • (2004) Insect Mol. Biol. , vol.13 , pp. 387-398
    • Shi, L.1    Paskewitz, S.M.2
  • 45
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb D.L., McDonald W.H., and Yates III J.R. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1 (2002) 21-26
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 47
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson M.P. The structure and function of proline-rich regions in proteins. Biochem. J. 297 Pt 2 (1994) 249-260
    • (1994) Biochem. J. , vol.297 , Issue.PART 2 , pp. 249-260
    • Williamson, M.P.1
  • 48
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D.A., Washburn M.P., and Yates III J.R. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 23 (2001) 5683-5690
    • (2001) Anal. Chem. , vol.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 49
    • 0034788314 scopus 로고    scopus 로고
    • Hydroxyproline-rich glycoproteins in plant reproductive tissues: structure, functions and regulation
    • Wu H., de Graaf B., Mariani C., and Cheung A.Y. Hydroxyproline-rich glycoproteins in plant reproductive tissues: structure, functions and regulation. Cell Mol. Life Sci. 58 (2001) 1418-1429
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1418-1429
    • Wu, H.1    de Graaf, B.2    Mariani, C.3    Cheung, A.Y.4
  • 50
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu C.C., MacCoss M.J., Howell K.E., and Yates III J.R. A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 5 (2003) 532-538
    • (2003) Nat. Biotechnol. , vol.5 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 51
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov B., Coleman M.K., Florens L., and Washburn M.P. Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal. Chem. 19 (2005) 6218-6224
    • (2005) Anal. Chem. , vol.19 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4


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