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Volumn 40, Issue 7, 2010, Pages 524-532

Disrupting the Amblyomma americanum (L.) CD147 receptor homolog prevents ticks from feeding to repletion and blocks spontaneous detachment of ticks from their host

Author keywords

Amblyomma americanum; Tick CD147 receptor homolog; Tick vaccine targets

Indexed keywords

CD147 ANTIGEN;

EID: 77953911766     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2010.04.012     Document Type: Article
Times cited : (14)

References (58)
  • 1
    • 0022668672 scopus 로고
    • Immunization of cattle against Boophilus microplus using extracts derived from adult female ticks: histopathology of ticks feeding on vaccinated cattle
    • Agbede R.I.S., Kemp D.H. Immunization of cattle against Boophilus microplus using extracts derived from adult female ticks: histopathology of ticks feeding on vaccinated cattle. Int. J. Parasitol. 1986, 16:35-41.
    • (1986) Int. J. Parasitol. , vol.16 , pp. 35-41
    • Agbede, R.I.S.1    Kemp, D.H.2
  • 2
    • 0024825053 scopus 로고
    • Cloning of cDNA for a novel mouse membrane glycoprotein (gp42): shared identity to histocompatibility antigens, immunoglobulins and neural-cell adhesion molecules
    • Altruda F., Cervella P., Gaeta M.L., Daniele A., Giancotti F., Tarone G., Stefanuto G., Silengo L. Cloning of cDNA for a novel mouse membrane glycoprotein (gp42): shared identity to histocompatibility antigens, immunoglobulins and neural-cell adhesion molecules. Gene 1989, 85:445-451.
    • (1989) Gene , vol.85 , pp. 445-451
    • Altruda, F.1    Cervella, P.2    Gaeta, M.L.3    Daniele, A.4    Giancotti, F.5    Tarone, G.6    Stefanuto, G.7    Silengo, L.8
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0031861480 scopus 로고    scopus 로고
    • Rickettsial pathogens and their arthropod vectors
    • Azad A.F., Beard C.B. Rickettsial pathogens and their arthropod vectors. Emerg. Infect. Dis. 1998, 4:179-186.
    • (1998) Emerg. Infect. Dis. , vol.4 , pp. 179-186
    • Azad, A.F.1    Beard, C.B.2
  • 5
    • 34249891614 scopus 로고    scopus 로고
    • The Ig cell adhesion molecule Basigin controls compartmentalization and vesicle release at Drosophila melanogaster synapses
    • Besse F., Mertel S., Kittel R.J., Wichmann C., Rasse T.M., Sigrist S.J., Ephrussi A. The Ig cell adhesion molecule Basigin controls compartmentalization and vesicle release at Drosophila melanogaster synapses. J. Cell Biol. 2007, 177:843-855.
    • (2007) J. Cell Biol. , vol.177 , pp. 843-855
    • Besse, F.1    Mertel, S.2    Kittel, R.J.3    Wichmann, C.4    Rasse, T.M.5    Sigrist, S.J.6    Ephrussi, A.7
  • 6
    • 0023444008 scopus 로고
    • Membrane association of collagenase stimulatory factor(s) from B-16 melanoma cells
    • Biswas C., Nugent M.A. Membrane association of collagenase stimulatory factor(s) from B-16 melanoma cells. J. Cell Biochem. 1987, 35:247-258.
    • (1987) J. Cell Biochem. , vol.35 , pp. 247-258
    • Biswas, C.1    Nugent, M.A.2
  • 7
    • 0028795147 scopus 로고
    • The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily
    • Biswas C., Zhang Y., DeCastro R., Guo H., Nakamura T., Kataoka H., Nabeshima K. The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res. 1995, 55:434-439.
    • (1995) Cancer Res. , vol.55 , pp. 434-439
    • Biswas, C.1    Zhang, Y.2    DeCastro, R.3    Guo, H.4    Nakamura, T.5    Kataoka, H.6    Nabeshima, K.7
  • 9
    • 21644447229 scopus 로고    scopus 로고
    • Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture
    • Curtin K.D., Meinertzhagen I.A., Wyman R.J. Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture. J. Cell Sci. 2005, 118:2649-2660.
    • (2005) J. Cell Sci. , vol.118 , pp. 2649-2660
    • Curtin, K.D.1    Meinertzhagen, I.A.2    Wyman, R.J.3
  • 10
    • 0030849487 scopus 로고    scopus 로고
    • Sustainable tick and tick-borne disease control in livestock improvement in developing countries
    • deCastro J.J. Sustainable tick and tick-borne disease control in livestock improvement in developing countries. Vet. Parasitol. 1997, 71:77-97.
    • (1997) Vet. Parasitol. , vol.71 , pp. 77-97
    • deCastro, J.J.1
  • 12
    • 0024386474 scopus 로고
    • Monoclonal antibody preparation and purification of a tumor cell collagenase-stimulatory factor
    • Ellis S.M., Nabeshima K., Biswas C. Monoclonal antibody preparation and purification of a tumor cell collagenase-stimulatory factor. Cancer Res. 1989, 49:3385-3391.
    • (1989) Cancer Res. , vol.49 , pp. 3385-3391
    • Ellis, S.M.1    Nabeshima, K.2    Biswas, C.3
  • 13
    • 0027478549 scopus 로고
    • Differential glycosylation of the 5A11/HT7 antigen by neural retina and epithelial tissues in the chicken
    • Fadool J.M., Linser P.J. Differential glycosylation of the 5A11/HT7 antigen by neural retina and epithelial tissues in the chicken. J. Neurochem. 1993, 60:1354-1364.
    • (1993) J. Neurochem. , vol.60 , pp. 1354-1364
    • Fadool, J.M.1    Linser, P.J.2
  • 14
    • 0025971638 scopus 로고
    • The MRC OX-47 antigen is a member of the immunoglobulin superfamily with an unusual transmembrane sequence
    • Fossum S., Mallett S., Barclay A.N. The MRC OX-47 antigen is a member of the immunoglobulin superfamily with an unusual transmembrane sequence. Eur. J. Immunol. 1991, 21:671-679.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 671-679
    • Fossum, S.1    Mallett, S.2    Barclay, A.N.3
  • 15
    • 3042582658 scopus 로고    scopus 로고
    • A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
    • Hanna S.M., Kirk P., Holt O.J., Puklavec M.J., Brown M.H., Barclay A.N. A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically. BMC Biochem. 2003, 4:17.
    • (2003) BMC Biochem. , vol.4 , pp. 17
    • Hanna, S.M.1    Kirk, P.2    Holt, O.J.3    Puklavec, M.J.4    Brown, M.H.5    Barclay, A.N.6
  • 17
    • 36048958229 scopus 로고    scopus 로고
    • CD147 immunoglobulin superfamily receptor function and role in pathology
    • Iacono K.T., Brown A.L., Greene M.I., Saouaf S.J. CD147 immunoglobulin superfamily receptor function and role in pathology. Exp. Mol. Pathol. 2007, 83:283-295.
    • (2007) Exp. Mol. Pathol. , vol.83 , pp. 283-295
    • Iacono, K.T.1    Brown, A.L.2    Greene, M.I.3    Saouaf, S.J.4
  • 19
    • 0036772337 scopus 로고    scopus 로고
    • Fold-recognition detects an error in the Protein Data Bank
    • Janusz B., Leszek R., Daniel F. Fold-recognition detects an error in the Protein Data Bank. Bioinformatics 2002, 18:1391-1395.
    • (2002) Bioinformatics , vol.18 , pp. 1391-1395
    • Janusz, B.1    Leszek, R.2    Daniel, F.3
  • 20
    • 16844371922 scopus 로고    scopus 로고
    • The global importance of ticks
    • Jonejan F., Uilenberg G. The global importance of ticks. Parasitology 2004, 129(Suppl):S3-S14.
    • (2004) Parasitology , vol.129 , Issue.SUPPL
    • Jonejan, F.1    Uilenberg, G.2
  • 21
    • 0031946850 scopus 로고    scopus 로고
    • Duration of tick attachment required for transmission of granulocytic ehrlichiosis
    • Katavolos P., Armstrong P.M., Dawson J.E., Telford S.R. Duration of tick attachment required for transmission of granulocytic ehrlichiosis. J. Infect. Dis. 1998, 177:1422-1425.
    • (1998) J. Infect. Dis. , vol.177 , pp. 1422-1425
    • Katavolos, P.1    Armstrong, P.M.2    Dawson, J.E.3    Telford, S.R.4
  • 23
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 1992, 356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 24
    • 0025718981 scopus 로고
    • The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen
    • Miyauchi T., Masuzawa Y., Muramatsu T. The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen. J Biochem (Tokyo) 1991, 110:770-774.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 770-774
    • Miyauchi, T.1    Masuzawa, Y.2    Muramatsu, T.3
  • 25
    • 34248144915 scopus 로고    scopus 로고
    • The molecular basis of the Amblyomma americanum tick attachment phase
    • Mulenga A., Blandon M., Khumthong R. The molecular basis of the Amblyomma americanum tick attachment phase. Exp. Appl. Acarol. 2007, 41:267-287.
    • (2007) Exp. Appl. Acarol. , vol.41 , pp. 267-287
    • Mulenga, A.1    Blandon, M.2    Khumthong, R.3
  • 26
    • 77951451908 scopus 로고    scopus 로고
    • Silencing of three Amblyomma americanum (L.) insulin-like growth factor binding protein-related proteins prevents ticks from feeding to repletion
    • Mulenga A., Khumthong R. Silencing of three Amblyomma americanum (L.) insulin-like growth factor binding protein-related proteins prevents ticks from feeding to repletion. J. Exp. Biol. 2010, 213(Pt 7):1153-1161.
    • (2010) J. Exp. Biol. , vol.213 , Issue.PART 7 , pp. 1153-1161
    • Mulenga, A.1    Khumthong, R.2
  • 27
    • 66749177735 scopus 로고    scopus 로고
    • Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis
    • Mulenga A., Khumthong R., Chalaire K.C. Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis. BMC Genomics 2009, 10:217.
    • (2009) BMC Genomics , vol.10 , pp. 217
    • Mulenga, A.1    Khumthong, R.2    Chalaire, K.C.3
  • 28
    • 55549128950 scopus 로고    scopus 로고
    • Molecular and biological characterization of the Amblyomma americanum organic anion transporter polypeptide
    • Mulenga A., Khumthong R., Chalaire K.C., Strey O., Teel P. Molecular and biological characterization of the Amblyomma americanum organic anion transporter polypeptide. J. Exp. Biol. 2008, 211:3401-3408.
    • (2008) J. Exp. Biol. , vol.211 , pp. 3401-3408
    • Mulenga, A.1    Khumthong, R.2    Chalaire, K.C.3    Strey, O.4    Teel, P.5
  • 29
    • 1542647244 scopus 로고    scopus 로고
    • Three serine proteinases from midguts of the hard tick Rhipicephalus microplus; cDNA cloning and preliminary characterization
    • Mulenga A., Misao O., Sugimoto C. Three serine proteinases from midguts of the hard tick Rhipicephalus microplus; cDNA cloning and preliminary characterization. Exp. Appl. Acarol. 2003, 29:151-164.
    • (2003) Exp. Appl. Acarol. , vol.29 , pp. 151-164
    • Mulenga, A.1    Misao, O.2    Sugimoto, C.3
  • 30
    • 0035933451 scopus 로고    scopus 로고
    • Characterization of two cDNAs encoding serine proteinases from the hard tick Haemaphysalis longicornis
    • Mulenga A., Sugimoto C., Ingram G., Ohashi K., Misao O. Characterization of two cDNAs encoding serine proteinases from the hard tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 2001, 31:817-825.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 817-825
    • Mulenga, A.1    Sugimoto, C.2    Ingram, G.3    Ohashi, K.4    Misao, O.5
  • 31
    • 33745075529 scopus 로고    scopus 로고
    • Matrix metalloproteinase modulator and multifunctional cell recognition molecule that plays a critical role in cancer progression
    • Nabeshima K., Iwasaki H., Koga K., Hojo H., Suzumiya J., Kikuchi M. Matrix metalloproteinase modulator and multifunctional cell recognition molecule that plays a critical role in cancer progression. Pathol. Int. 2006, 56:359-367.
    • (2006) Pathol. Int. , vol.56 , pp. 359-367
    • Nabeshima, K.1    Iwasaki, H.2    Koga, K.3    Hojo, H.4    Suzumiya, J.5    Kikuchi, M.6
  • 32
    • 0029079786 scopus 로고
    • Distribution of the integral plasma membrane glycoprotein CE9 (MRC OX-47) among rat tissues and its induction by diverse stimuli of metabolic activation
    • Nehme C.L., Fayos B.E., Bartles J.R. Distribution of the integral plasma membrane glycoprotein CE9 (MRC OX-47) among rat tissues and its induction by diverse stimuli of metabolic activation. Biochem. J. 1995, 310(Pt 2):693-698.
    • (1995) Biochem. J. , vol.310 , Issue.PART 2 , pp. 693-698
    • Nehme, C.L.1    Fayos, B.E.2    Bartles, J.R.3
  • 34
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: a tool for multiple sequence and structure alignment
    • Pei J., Kim B.H., Grishin N.V. PROMALS3D: a tool for multiple sequence and structure alignment. Nucleic Acids Res. 2008, 36:2295-2300.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 35
    • 15444381280 scopus 로고
    • Protein modeling by E-mail Bio/Technology 13
    • Peitsch, M.C., 1995. Protein modeling by E-mail Bio/Technology 13, 658-660.
    • (1995) , pp. 658-660
    • Peitsch, M.C.1
  • 37
  • 38
    • 0019204423 scopus 로고
    • Human babesiosis on Nantucket Island: prevalence of Babesia microti in ticks
    • Piesman J., Spielman A. Human babesiosis on Nantucket Island: prevalence of Babesia microti in ticks. Am. J. Trop. Med. Hyg. 1980, 29:742-746.
    • (1980) Am. J. Trop. Med. Hyg. , vol.29 , pp. 742-746
    • Piesman, J.1    Spielman, A.2
  • 42
    • 0036119370 scopus 로고    scopus 로고
    • Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice
    • Saxena D.K., Oh-Oka T., Kadomatsu K., Muramatsu T., Toshimori K. Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice. Reproduction 2002, 123:435-444.
    • (2002) Reproduction , vol.123 , pp. 435-444
    • Saxena, D.K.1    Oh-Oka, T.2    Kadomatsu, K.3    Muramatsu, T.4    Toshimori, K.5
  • 44
    • 0028818328 scopus 로고
    • Neurothelin: amino acid sequence, cell surface dynamics and actin co-localization
    • Schlosshauer B., Bauch H., Frank R. Neurothelin: amino acid sequence, cell surface dynamics and actin co-localization. Eur. J. Cell Biol. 1995, 68:159-166.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 159-166
    • Schlosshauer, B.1    Bauch, H.2    Frank, R.3
  • 45
    • 0025296074 scopus 로고
    • The inducible blood-brain barrier specific molecule HT7 is a novel immunoglobulin-like cell surface glycoprotein
    • Seulberger H., Lottspeich F., Risau W. The inducible blood-brain barrier specific molecule HT7 is a novel immunoglobulin-like cell surface glycoprotein. EMBO J 1990, 9:2151-2158.
    • (1990) EMBO J , vol.9 , pp. 2151-2158
    • Seulberger, H.1    Lottspeich, F.2    Risau, W.3
  • 46
    • 0026653792 scopus 로고
    • HT7, Neurothelin, Basigin, gp42 and OX-47 - many names for one developmentally regulated immuno-globulin-like surface glycoprotein on blood-brain barrier endothelium, epithelial tissue barriers and neurons
    • Seulberger H., Unger C.M., Risau W. HT7, Neurothelin, Basigin, gp42 and OX-47 - many names for one developmentally regulated immuno-globulin-like surface glycoprotein on blood-brain barrier endothelium, epithelial tissue barriers and neurons. Neurosci. Lett. 1992, 140:93-97.
    • (1992) Neurosci. Lett. , vol.140 , pp. 93-97
    • Seulberger, H.1    Unger, C.M.2    Risau, W.3
  • 49
    • 4344668062 scopus 로고    scopus 로고
    • Links between CD147 function, glycosylation, and caveolin-1
    • Tang W., Chang S.B., Hemler M.E. Links between CD147 function, glycosylation, and caveolin-1. Mol. Biol. Cell. 2004, 15:4043-4050.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 4043-4050
    • Tang, W.1    Chang, S.B.2    Hemler, M.E.3
  • 50
    • 1642483595 scopus 로고    scopus 로고
    • Caveolin-1 regulates matrix metalloproteinases-1 induction and CD147/EMMPRIN cell surface clustering
    • Tang W., Hemler M.E. Caveolin-1 regulates matrix metalloproteinases-1 induction and CD147/EMMPRIN cell surface clustering. J. Biol. Chem. 2004, 279:11112-11118.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11112-11118
    • Tang, W.1    Hemler, M.E.2
  • 51
    • 17144422889 scopus 로고    scopus 로고
    • Extracellular matrix metalloproteinase inducer stimulates tumor angiogenesis by elevating vascular endothelial cell growth factor and matrix metalloproteinases
    • Tang Y., Nakada M.T., Kesavan P., McCabe F., Millar H., Rafferty P., Bugelski P., Yan L. Extracellular matrix metalloproteinase inducer stimulates tumor angiogenesis by elevating vascular endothelial cell growth factor and matrix metalloproteinases. Cancer Res. 2005, 65:3193-3199.
    • (2005) Cancer Res. , vol.65 , pp. 3193-3199
    • Tang, Y.1    Nakada, M.T.2    Kesavan, P.3    McCabe, F.4    Millar, H.5    Rafferty, P.6    Bugelski, P.7    Yan, L.8
  • 52
    • 0035919563 scopus 로고    scopus 로고
    • cDNA cloning, characterization and vaccine effect analysis of Haemaphysalis longicornis tick saliva proteins.Vaccine. 19:
    • Tsuda, A., Mulenga, A., Sugimoto, C., Nakajima, M., Ohashi, K., Onuma, M., 2001. cDNA cloning, characterization and vaccine effect analysis of Haemaphysalis longicornis tick saliva proteins.Vaccine. 19: 4287-4296.
    • (2001) , pp. 4287-4296
    • Tsuda A1    Mulenga A2    Sugimoto C3    Nakajima M4    Ohashi K5    Onuma, M.6
  • 57
    • 33645072764 scopus 로고    scopus 로고
    • Expression of CD147 on monocytes/macrophages in rheumatoid arthritis: its potential role in monocyte accumulation and matrix metalloproteinase production
    • Zhu P., Ding J., Zhou J., Dong W.J., Fan C.M., Chen Z.N. Expression of CD147 on monocytes/macrophages in rheumatoid arthritis: its potential role in monocyte accumulation and matrix metalloproteinase production. Arthritis Res. Ther. 2005, 7:R1023-R1033.
    • (2005) Arthritis Res. Ther. , vol.7
    • Zhu, P.1    Ding, J.2    Zhou, J.3    Dong, W.J.4    Fan, C.M.5    Chen, Z.N.6


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