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Volumn 35, Issue 9, 2005, Pages 947-959

Identification and characterization of a novel peritrophic matrix protein, Ae-Aper50, and the microvillar membrane protein, AEG12, from the mosquito, Aedes aegypti

Author keywords

Aedes aegypti; Microvilli; Midgut; Mosquito; Peritrophic matrix

Indexed keywords

CHITIN; INSECT PROTEIN;

EID: 20544437456     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2005.03.012     Document Type: Article
Times cited : (65)

References (56)
  • 2
    • 20444429428 scopus 로고    scopus 로고
    • Driving midgut-specific expression and secretion of a foreign protein in transgenic mosquitoes with AgAper1 regulatory elements
    • in press.
    • Abraham, E.G., Donnelly-Doman, M., Fujioka, M., Ghosh, A.K., Moreira, L., Jacobs-Lorena, M., 2005. Driving midgut-specific expression and secretion of a foreign protein in transgenic mosquitoes with AgAper1 regulatory elements. Insect Mol. Biol., in press.
    • (2005) Insect Mol. Biol.
    • Abraham, E.G.1    Donnelly-Doman, M.2    Fujioka, M.3    Ghosh, A.K.4    Moreira, L.5    Jacobs-Lorena, M.6
  • 7
    • 0001915114 scopus 로고
    • Studies on mosquito-borne viruses in their vectors 1: The normal fine structure of the midgut epithelium of the adult female Aedes aegypti (L.) and the functional significance of its modifications following a blood meal
    • D.S. Bertram, and R.G. Bird Studies on mosquito-borne viruses in their vectors 1: the normal fine structure of the midgut epithelium of the adult female Aedes aegypti (L.) and the functional significance of its modifications following a blood meal Trans. R. Soc. Trop. Med. Hyg. 55 1961 404 423
    • (1961) Trans. R. Soc. Trop. Med. Hyg. , vol.55 , pp. 404-423
    • Bertram, D.S.1    Bird, R.G.2
  • 8
    • 0026742343 scopus 로고
    • The role of the mosquito peritrophic membrane in bloodmeal digestion and infectivity of Plasmodium species
    • P.F. Billingsley, and W. Rudin 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
  • 10
    • 20544450751 scopus 로고    scopus 로고
    • The peritrophic matrix of hematophagous insects
    • W.C. Marquardt second ed Elsevier Academic Press Amsterdam
    • M. Devenport, and M. Jacobs-Lorena The peritrophic matrix of hematophagous insects W.C. Marquardt Biology of Disease Vectors second ed 2005 Elsevier Academic Press Amsterdam 297 310
    • (2005) Biology of Disease Vectors , pp. 297-310
    • Devenport, M.1    Jacobs-Lorena, M.2
  • 11
    • 3943069803 scopus 로고    scopus 로고
    • Storage and secretion of the peritrophic matrix protein Ag-Aper1 and trypsin in the midgut of Anopheles gambiae
    • M. Devenport, H. Fujioka, and M. Jacobs-Lorena Storage and secretion of the peritrophic matrix protein Ag-Aper1 and trypsin in the midgut of Anopheles gambiae Insect Mol. Biol. 13 4 2004 349 358
    • (2004) Insect Mol. Biol. , vol.13 , Issue.4 , pp. 349-358
    • Devenport, M.1    Fujioka, H.2    Jacobs-Lorena, M.3
  • 13
    • 0033931463 scopus 로고    scopus 로고
    • Permeability and disruption of the peritrophic matrix and caecal membrane from Aedes aegypti and Anopheles gambiae mosquito larvae
    • M.J. Edwards, and M. Jacobs-Lorena Permeability and disruption of the peritrophic matrix and caecal membrane from Aedes aegypti and Anopheles gambiae mosquito larvae J. Insect Physiol. 46 9 2000 1313 1320
    • (2000) J. Insect Physiol. , vol.46 , Issue.9 , pp. 1313-1320
    • Edwards, M.J.1    Jacobs-Lorena, M.2
  • 14
    • 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
    • C.M. Elvin, T. Vuocolo, R.D. Pearson, I.J. East, G.A. Riding, C.H. Eisemann, and R.L. Tellam 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
  • 16
    • 0013533431 scopus 로고
    • The prerequisites for the formation of a peritrophic membrane in culicidae females
    • T.A. Freyvogel, and C. Jaquet The prerequisites for the formation of a peritrophic membrane in culicidae females Acta. Trop. 22 1965 148 154
    • (1965) Acta. Trop. , vol.22 , pp. 148-154
    • Freyvogel, T.A.1    Jaquet, C.2
  • 17
    • 0001119092 scopus 로고
    • The formation of the peritrophic membrane in culicidae
    • T.A. Freyvogel, and W. Staubli The formation of the peritrophic membrane in culicidae Acta. Trop. 22 1965 118 147
    • (1965) Acta. Trop. , vol.22 , pp. 118-147
    • Freyvogel, T.A.1    Staubli, W.2
  • 19
    • 0031809552 scopus 로고    scopus 로고
    • NetOglyc: Prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility
    • J.E. Hansen, O. Lund, N. Tolstrup, A.A. Gooley, K.L. Williams, and S. Brunak NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility Glycoconjugate J. 15 1998 115 130
    • (1998) Glycoconjugate J. , vol.15 , pp. 115-130
    • Hansen, J.E.1    Lund, O.2    Tolstrup, N.3    Gooley, A.A.4    Williams, K.L.5    Brunak, S.6
  • 20
    • 0025857170 scopus 로고
    • Malaria parasite chitinase and penetration of the mosquito peritrophic membrane
    • M. Huber, E. Cabib, and L.H. Miller Malaria parasite chitinase and penetration of the mosquito peritrophic membrane Proc. Natl. Acad. Sci. USA 88 1991 2807 2810
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2807-2810
    • Huber, M.1    Cabib, E.2    Miller, L.H.3
  • 21
    • 0036000565 scopus 로고    scopus 로고
    • Glucosamine: Fructose-6-phosphate aminotransferase: Gene characterization, chitin biosynthesis and peritrophic matrix formation in Aedes aegypti
    • N. Kato, R. Dasgupta, C. Smartt, and B.M. Christensen Glucosamine: fructose-6-phosphate aminotransferase: gene characterization, chitin biosynthesis and peritrophic matrix formation in Aedes aegypti Insect Mol. Biol. 11 3 2002 207 216
    • (2002) Insect Mol. Biol. , vol.11 , Issue.3 , pp. 207-216
    • Kato, N.1    Dasgupta, R.2    Smartt, C.3    Christensen, B.M.4
  • 23
    • 0030891189 scopus 로고    scopus 로고
    • Peritrophic matrix structure and function
    • M.J. Lehane Peritrophic matrix structure and function Annu. Rev. Entomol. 42 1997 525 550
    • (1997) Annu. Rev. Entomol. , vol.42 , pp. 525-550
    • Lehane, M.J.1
  • 24
    • 0034922594 scopus 로고    scopus 로고
    • Identification of a polymorphic mucin-like gene expressed in the midgut of the mosquito Aedes aegypti, using an integrated bulked segregant and differential display analysis
    • I. Morlais, and D.W. Severson Identification of a polymorphic mucin-like gene expressed in the midgut of the mosquito Aedes aegypti, using an integrated bulked segregant and differential display analysis Genetics 158 2001 1125 1136
    • (2001) Genetics , vol.158 , pp. 1125-1136
    • Morlais, I.1    Severson, D.W.2
  • 25
    • 0345094936 scopus 로고    scopus 로고
    • Intraspecific DNA variation in nuclear genes of the mosquito Aedes aegypti
    • I. Morlais, and D.W. Severson Intraspecific DNA variation in nuclear genes of the mosquito Aedes aegypti Insect Mol. Biol. 12 6 2003 631 639
    • (2003) Insect Mol. Biol. , vol.12 , Issue.6 , pp. 631-639
    • Morlais, I.1    Severson, D.W.2
  • 26
    • 0141619387 scopus 로고    scopus 로고
    • A targeted approach to the identification of candidate genes determining susceptibility to Plasmodium gallinaceum in Aedes aegypti
    • I. Morlais, A. Mori, J.R. Schneider, and D.W. Severson A targeted approach to the identification of candidate genes determining susceptibility to Plasmodium gallinaceum in Aedes aegypti Mol. Genet. Genom. 269 6 2003 753 764
    • (2003) Mol. Genet. Genom. , vol.269 , Issue.6 , pp. 753-764
    • Morlais, I.1    Mori, A.2    Schneider, J.R.3    Severson, D.W.4
  • 27
    • 0030293932 scopus 로고    scopus 로고
    • Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti
    • L.A. Moskalyk, M.-M. Oo, and M. Jacobs-Lorena 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
  • 29
    • 0035213081 scopus 로고    scopus 로고
    • Molecular biocomuting suite: A word processor add-in for the analysis and manipulation of nucleic acid and protein sequence data
    • P.Y. Muller, E. Studer, and A.R. Miserez Molecular biocomuting suite: a word processor add-in for the analysis and manipulation of nucleic acid and protein sequence data Biotechniques 31 2001 1306 1313
    • (2001) Biotechniques , vol.31 , pp. 1306-1313
    • Muller, P.Y.1    Studer, E.2    Miserez, A.R.3
  • 30
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. von Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng. 10 1997 1 6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 31
    • 0033015768 scopus 로고    scopus 로고
    • A molecular view of trypsin synthesis in the midgut of Aedes aegypti
    • F.G. Noriega, and M.A. Wells A molecular view of trypsin synthesis in the midgut of Aedes aegypti J. Insect Physiol. 45 1999 613 620
    • (1999) J. Insect Physiol. , vol.45 , pp. 613-620
    • Noriega, F.G.1    Wells, M.A.2
  • 33
    • 0023947408 scopus 로고
    • Time and site of assembly of the peritrophic membrane of the mosquito Aedes aegypti
    • J.B. Perrone, and A. Spielman Time and site of assembly of the peritrophic membrane of the mosquito Aedes aegypti Cell Tissue Res. 252 1988 473 478
    • (1988) Cell Tissue Res. , vol.252 , pp. 473-478
    • Perrone, J.B.1    Spielman, A.2
  • 34
    • 0001806279 scopus 로고
    • Peritrophic membranes
    • D. Bradshaw W. Burggren H.C. Heller S. Ishii H. Langer G. Neuweiler D.J. Randall Springer Berlin
    • W. Peters Peritrophic membranes D. Bradshaw W. Burggren H.C. Heller S. Ishii H. Langer G. Neuweiler D.J. Randall Zoophysiology vol. 130 1992 Springer Berlin
    • (1992) Zoophysiology , vol.130
    • Peters, W.1
  • 35
    • 0032515169 scopus 로고    scopus 로고
    • Novel allergen structures with tandem amino acid repeats derived from German and American cockroach
    • A. Pomes, E. Melen, L.D. Vailes, J.D. Retief, L.K. Arruda, and M.D. Chapman Novel allergen structures with tandem amino acid repeats derived from German and American cockroach J. Biol. Chem. 273 46 1998 30801 30807
    • (1998) J. Biol. Chem. , vol.273 , Issue.46 , pp. 30801-30807
    • Pomes, A.1    Melen, E.2    Vailes, L.D.3    Retief, J.D.4    Arruda, L.K.5    Chapman, M.D.6
  • 36
    • 0033821708 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a metal responsive Aedes aegypti intestinal mucin cDNA
    • A. Rayms-Keller, M. McGaw, C. Oray, J.O. Carlson, and B.J. Beaty Molecular cloning and characterization of a metal responsive Aedes aegypti intestinal mucin cDNA Insect Mol. Biol. 9 2000 419 426
    • (2000) Insect Mol. Biol. , vol.9 , pp. 419-426
    • Rayms-Keller, A.1    McGaw, M.2    Oray, C.3    Carlson, J.O.4    Beaty, B.J.5
  • 38
    • 0032004767 scopus 로고    scopus 로고
    • CDNA and deduced amino acid sequences of a peritrophic membrane glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina
    • S. Schorderet, R.D. Pearson, T. Vuocolo, C. Eisemann, G.A. Riding, and R.L. Tellam cDNA and deduced amino acid sequences of a peritrophic membrane glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina Insect Biochem. Mol. Biol. 28 1998 99 111
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 99-111
    • Schorderet, S.1    Pearson, R.D.2    Vuocolo, T.3    Eisemann, C.4    Riding, G.A.5    Tellam, R.L.6
  • 39
    • 0027308860 scopus 로고
    • Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease
    • M. Shahabuddin, T. Toyoshima, M. Aikawa, and D.C. Kaslow Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease Proc. Natl. Acad. Sci. USA 90 1993 4266 4270
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4266-4270
    • Shahabuddin, M.1    Toyoshima, T.2    Aikawa, M.3    Kaslow, D.C.4
  • 40
    • 0029559634 scopus 로고
    • Plasmodium gallinaceum: Mosquito peritrophic matrix and the parasite-vector compatibility
    • M. Shahabuddin, T. Kaidoh, M. Aikawa, and D.C. Kaslow Plasmodium gallinaceum: mosquito peritrophic matrix and the parasite-vector compatibility Exp. Parasitol. 81 3 1995 386 393
    • (1995) Exp. Parasitol. , vol.81 , Issue.3 , pp. 386-393
    • Shahabuddin, M.1    Kaidoh, T.2    Aikawa, M.3    Kaslow, D.C.4
  • 41
    • 0033007284 scopus 로고    scopus 로고
    • Evolution of chitin-binding proteins in invertebrates
    • Z. Shen, and M. Jacobs-Lorena Evolution of chitin-binding proteins in invertebrates Mol. Evol. 48 3 1999 341 347
    • (1999) Mol. Evol. , vol.48 , Issue.3 , pp. 341-347
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 43
    • 0042724130 scopus 로고
    • Structural modifications of the endoplasmatic reticulum of midgut epithelial cells of mosquitoes in relation to blood intake
    • W. Staubli, T.A. Freyvogel, and J. Suter Structural modifications of the endoplasmatic reticulum of midgut epithelial cells of mosquitoes in relation to blood intake J. Microsc. 5 1966 189 204
    • (1966) J. Microsc. , vol.5 , pp. 189-204
    • Staubli, W.1    Freyvogel, T.A.2    Suter, J.3
  • 44
    • 0002548913 scopus 로고    scopus 로고
    • The peritrophic matrix
    • M.J. Lehane P.F. Billingsley Chapman & Hall London
    • R.L. Tellam The peritrophic matrix M.J. Lehane P.F. Billingsley The Insect Midgut 1996 Chapman & Hall London
    • (1996) The Insect Midgut
    • Tellam, R.L.1
  • 46
    • 0035378362 scopus 로고    scopus 로고
    • The origins and functions of the insect peritrophic membrane and peritrophic gel
    • W.R. Terra The origins and functions of the insect peritrophic membrane and peritrophic gel Arch. Insect Biochem. Physiol. 47 2 2001 47 61
    • (2001) Arch. Insect Biochem. Physiol. , vol.47 , Issue.2 , pp. 47-61
    • Terra, W.R.1
  • 49
    • 0034616295 scopus 로고    scopus 로고
    • Chitinases of the avian malaria parasite Plasmodium gallinaceum, a class of enzymes necessary for parasite invasion of the mosquito midgut
    • J.M. Vinetz, J.G. Valenzuela, C.A. Specht, L. Aravind, R.C. Langer, J.M. Ribeiro, and D.C. Kaslow Chitinases of the avian malaria parasite Plasmodium gallinaceum, a class of enzymes necessary for parasite invasion of the mosquito midgut J. Biol. Chem. 275 2000 10331 10341
    • (2000) J. Biol. Chem. , vol.275 , pp. 10331-10341
    • Vinetz, J.M.1    Valenzuela, J.G.2    Specht, C.A.3    Aravind, L.4    Langer, R.C.5    Ribeiro, J.M.6    Kaslow, D.C.7
  • 50
    • 0030990106 scopus 로고    scopus 로고
    • An intestinal mucin is the target substrate for a baculovirus enhancing
    • P. Wang, and R.R. Granados An intestinal mucin is the target substrate for a baculovirus enhancing Proc. Natl. Acad. Sci. USA 94 1997 6977 6982
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6977-6982
    • Wang, P.1    Granados, R.R.2
  • 51
    • 0030985902 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of a novel invertebrate intestinal mucin cDNA
    • P. Wang, and R.R. Granados Molecular cloning and sequencing of a novel invertebrate intestinal mucin cDNA J. Biol. Chem. 272 26 1997 16663 16669
    • (1997) J. Biol. Chem. , vol.272 , Issue.26 , pp. 16663-16669
    • Wang, P.1    Granados, R.R.2
  • 52
    • 0035377371 scopus 로고    scopus 로고
    • Molecular structure of the peritrophic membrane (PM): Identification of potential PM target sites for insect control
    • P. Wang, and R.R. Granados Molecular structure of the peritrophic membrane (PM): identification of potential PM target sites for insect control Arch. Insect Biochem. Physiol. 47 2 2001 110 118
    • (2001) Arch. Insect Biochem. Physiol. , vol.47 , Issue.2 , pp. 110-118
    • Wang, P.1    Granados, R.R.2
  • 53
    • 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
    • P. Wang, G. Li, and R.R. Granados 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. 34 2004 215 227
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 215-227
    • Wang, P.1    Li, G.2    Granados, R.R.3
  • 54
    • 0002274284 scopus 로고
    • The formation of the peritrophic membrane in insects, with special reference to the larvae of mosquitoes
    • V.B. Wigglesworth The formation of the peritrophic membrane in insects, with special reference to the larvae of mosquitoes Q. J. Microsc. Sci. 73 1930 593 616
    • (1930) Q. J. Microsc. Sci. , vol.73 , pp. 593-616
    • Wigglesworth, V.B.1
  • 55
    • 0034877127 scopus 로고    scopus 로고
    • Partial characterization of oligosaccharides expressed on midgut microvillar glycoproteins of the mosquito, Anopheles stephensi Liston
    • S. Wilkins, and P.F. Billingsley Partial characterization of oligosaccharides expressed on midgut microvillar glycoproteins of the mosquito, Anopheles stephensi Liston Insect Biochem. Mol. Biol. 31 2001 937 948
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 937-948
    • Wilkins, S.1    Billingsley, P.F.2
  • 56
    • 0031841770 scopus 로고    scopus 로고
    • Cloning of the American cockroach Cr-PII allergens: Evidence for the existence of cross-reactive allergens between species
    • C.H. Wu, N.M. Wang, M.F. Lee, C.Y. Kao, and S.F. Luo Cloning of the American cockroach Cr-PII allergens: evidence for the existence of cross-reactive allergens between species J. Allergy Clin. Immunol. 101 1998 832 840
    • (1998) J. Allergy Clin. Immunol. , vol.101 , pp. 832-840
    • Wu, C.H.1    Wang, N.M.2    Lee, M.F.3    Kao, C.Y.4    Luo, S.F.5


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