메뉴 건너뛰기




Volumn 40, Issue 6, 2010, Pages 721-729

Longistatin, a novel EF-hand protein from the ixodid tick Haemaphysalis longicornis, is required for acquisition of host blood-meals

Author keywords

Arthropods; Blood feeding; EF hand domain; Haemaphysalis longicornis; Ixodid ticks; Longistatin

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; LONGISTATIN; RUTHENIUM RED; UNCLASSIFIED DRUG;

EID: 77951299257     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2009.11.004     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 34547532754 scopus 로고    scopus 로고
    • Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis
    • Alim M.A., Tsuji N., Miyoshi T., Islam M.K., Huang X., Motobu M., Fujisaki K. Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 2007, 37:911-922.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 911-922
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3    Islam, M.K.4    Huang, X.5    Motobu, M.6    Fujisaki, K.7
  • 4
    • 0032531818 scopus 로고    scopus 로고
    • Calcium - a life and death signal
    • Berridge M.J., Bootman M.D., Lipp P. Calcium - a life and death signal. Nature 1998, 395:645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 5
    • 0019246828 scopus 로고
    • Role of tick salivary glands in feeding and disease transmission
    • Binnington K.C., Kemp D.H. Role of tick salivary glands in feeding and disease transmission. Adv. Parasitol. 1980, 18:315-339.
    • (1980) Adv. Parasitol. , vol.18 , pp. 315-339
    • Binnington, K.C.1    Kemp, D.H.2
  • 6
    • 29144503154 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis
    • Boldbaatar D., Sikasunge C.S., Battsetseg B., Xuan X., Fujisaki K. Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis. Insect. Biochem. Mol. Biol. 2006, 36:25-36.
    • (2006) Insect. Biochem. Mol. Biol. , vol.36 , pp. 25-36
    • Boldbaatar, D.1    Sikasunge, C.S.2    Battsetseg, B.3    Xuan, X.4    Fujisaki, K.5
  • 7
    • 11844284452 scopus 로고    scopus 로고
    • Tick immunobiology
    • Brossard M., Wikel S.K. Tick immunobiology. Parasitology 2004, 129(Suppl):S161-S176.
    • (2004) Parasitology , vol.129 , Issue.SUPPL.
    • Brossard, M.1    Wikel, S.K.2
  • 9
    • 22144494698 scopus 로고    scopus 로고
    • Tick saliva is a potent inhibitor of endothelial cell proliferation and angiogenesis
    • Francischetti I.M., Mather T.N., Ribeiro J.M. Tick saliva is a potent inhibitor of endothelial cell proliferation and angiogenesis. Thromb. Haemost. 2005, 94:167-174.
    • (2005) Thromb. Haemost. , vol.94 , pp. 167-174
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 10
  • 11
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 1998, 141:1539-1550.
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 12
    • 0020572087 scopus 로고
    • Primary sequence analysis and folding behavior of EF hands in relation to the mechanism of action of troponon C and calmodulin
    • Gariépy J., Hodges R.S. Primary sequence analysis and folding behavior of EF hands in relation to the mechanism of action of troponon C and calmodulin. FEBS Lett. 1983, 160:1-6.
    • (1983) FEBS Lett. , vol.160 , pp. 1-6
    • Gariépy, J.1    Hodges, R.S.2
  • 13
    • 0021101593 scopus 로고
    • Lanthanide-induced peptide folding: variations in lanthanide affinity and induced peptide conformation
    • Gariépy J., Sykes B.D., Hodges R.S. Lanthanide-induced peptide folding: variations in lanthanide affinity and induced peptide conformation. Biochemistry 1983, 22:1765-1772.
    • (1983) Biochemistry , vol.22 , pp. 1765-1772
    • Gariépy, J.1    Sykes, B.D.2    Hodges, R.S.3
  • 14
    • 33646761687 scopus 로고    scopus 로고
    • Structural basis for diversity of the EF-hand calcium-binding proteins
    • Grabarek Z. Structural basis for diversity of the EF-hand calcium-binding proteins. J. Mol. Biol. 2006, 359:509-525.
    • (2006) J. Mol. Biol. , vol.359 , pp. 509-525
    • Grabarek, Z.1
  • 15
    • 48449089504 scopus 로고    scopus 로고
    • New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2
    • Guy J.E., Wigren E., Svärd M., Härd T., Lindqvist Y. New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. J. Mol. Biol. 2008, 381:941-955.
    • (2008) J. Mol. Biol. , vol.381 , pp. 941-955
    • Guy, J.E.1    Wigren, E.2    Svärd, M.3    Härd, T.4    Lindqvist, Y.5
  • 17
    • 0014399463 scopus 로고
    • Review of Haemaphysalis (Kaiseriana) longicornis Neumann (resurrected) of Australia, New Zealand, New Caledonia, Fiji, Japan, Korea, and northeastern China and USSR, and its parthogenetic and bisexual populations (Ixodoidea, Ixodidae)
    • Hoogstraal H., Roberts F.H., Kohls G.M., Tipton V.J. Review of Haemaphysalis (Kaiseriana) longicornis Neumann (resurrected) of Australia, New Zealand, New Caledonia, Fiji, Japan, Korea, and northeastern China and USSR, and its parthogenetic and bisexual populations (Ixodoidea, Ixodidae). J. Parasitol. 1968, 54:1197-1213.
    • (1968) J. Parasitol. , vol.54 , pp. 1197-1213
    • Hoogstraal, H.1    Roberts, F.H.2    Kohls, G.M.3    Tipton, V.J.4
  • 19
    • 0347949547 scopus 로고    scopus 로고
    • Regulation of cell cycle progression by calcium/calmodulin-dependent pathways
    • Kahl C.R., Means A.R. Regulation of cell cycle progression by calcium/calmodulin-dependent pathways. Endocr. Rev. 2003, 24:719-736.
    • (2003) Endocr. Rev. , vol.24 , pp. 719-736
    • Kahl, C.R.1    Means, A.R.2
  • 20
    • 0032454584 scopus 로고    scopus 로고
    • Classification and evolution of EF-hand proteins
    • Kawasaki H., Nakayama S., Kretsinger R.H. Classification and evolution of EF-hand proteins. BioMetals 1998, 11:277-295.
    • (1998) BioMetals , vol.11 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 21
    • 0001897462 scopus 로고
    • Tick attachment and feeding: role of the mouthparts, feeding apparatus, salivary gland secretions, and the host response
    • Pergamon Press Inc., New York, F.D. Obenchain, R. Galun (Eds.)
    • Kemp D.H., Stone B.F., Binnington K.C. Tick attachment and feeding: role of the mouthparts, feeding apparatus, salivary gland secretions, and the host response. Physiology of Ticks 1982, 119-168. Pergamon Press Inc., New York. F.D. Obenchain, R. Galun (Eds.).
    • (1982) Physiology of Ticks , pp. 119-168
    • Kemp, D.H.1    Stone, B.F.2    Binnington, K.C.3
  • 22
    • 0001018554 scopus 로고
    • Calcineurin: a calcium- and calmodulin-binding protein of the nervous system
    • Klee C.B., Crouch T.H., Krinks M.H. Calcineurin: a calcium- and calmodulin-binding protein of the nervous system. Proc. Natl. Acad. Sci. USA 1979, 76:6270-6273.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6270-6273
    • Klee, C.B.1    Crouch, T.H.2    Krinks, M.H.3
  • 23
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger R.H., Nockolds C.E. Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem. 1973, 248:3313-3326.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 26
    • 33846839167 scopus 로고    scopus 로고
    • Molecular and reverse genetic characterization of serine proteinase-induced hemolysis in the midgut of the ixodid tick Haemaphysalis longicornis
    • Miyoshi T., Tsuji N., Islam M.K., Huang X., Motobu M., Alim M.A., Fujisaki K. Molecular and reverse genetic characterization of serine proteinase-induced hemolysis in the midgut of the ixodid tick Haemaphysalis longicornis. J. Insect Physiol. 2007, 53:195-203.
    • (2007) J. Insect Physiol. , vol.53 , pp. 195-203
    • Miyoshi, T.1    Tsuji, N.2    Islam, M.K.3    Huang, X.4    Motobu, M.5    Alim, M.A.6    Fujisaki, K.7
  • 28
    • 0025982850 scopus 로고
    • Off-host physiological ecology of ixodid ticks
    • Needham G.R., Teel P.D. Off-host physiological ecology of ixodid ticks. Annu. Rev. Entomol. 1991, 36:659-681.
    • (1991) Annu. Rev. Entomol. , vol.36 , pp. 659-681
    • Needham, G.R.1    Teel, P.D.2
  • 29
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage site
    • Nielsen H., Engelbrecht J., Brunak S., Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage site. Protein Eng. Des. Sel. 1997, 10:1-6.
    • (1997) Protein Eng. Des. Sel. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Heijne, G.4
  • 30
    • 0031837745 scopus 로고    scopus 로고
    • Displaced tick-parasite interactions at the host interface
    • Nuttall P.A. Displaced tick-parasite interactions at the host interface. Parasitology 1998, 116:65-72.
    • (1998) Parasitology , vol.116 , pp. 65-72
    • Nuttall, P.A.1
  • 31
    • 33645109969 scopus 로고    scopus 로고
    • Exposed and concealed antigens as vaccine targets for controlling ticks and tick-borne diseases
    • Nuttall P.A., Trimnell A.R., Kazimirova M., Labuda M. Exposed and concealed antigens as vaccine targets for controlling ticks and tick-borne diseases. Parasite Immunol. 2006, 28:155-163.
    • (2006) Parasite Immunol. , vol.28 , pp. 155-163
    • Nuttall, P.A.1    Trimnell, A.R.2    Kazimirova, M.3    Labuda, M.4
  • 32
    • 0028286760 scopus 로고
    • Changes in calcium and collagen IV binding caused by mutations in the EF hand and other domains of extracellular matrix protein BM-40 (SPARC, osteonectin)
    • Pottgiesser J., Maurer P., Mayer U., Nischt R., Mann K., Timpl R., Krieg T., Engel J. Changes in calcium and collagen IV binding caused by mutations in the EF hand and other domains of extracellular matrix protein BM-40 (SPARC, osteonectin). J. Mol. Biol. 1994, 238:563-574.
    • (1994) J. Mol. Biol. , vol.238 , pp. 563-574
    • Pottgiesser, J.1    Maurer, P.2    Mayer, U.3    Nischt, R.4    Mann, K.5    Timpl, R.6    Krieg, T.7    Engel, J.8
  • 33
    • 84970058643 scopus 로고
    • Signal transduction versus buffering activity in Ca2+-binding proteins. Nat. Struct. Biol. 1,
    • Skelton, N.J., Kördel, J., Akke, M., Forsén, S. Chazin, W.J., 1994. Signal transduction versus buffering activity in Ca2+-binding proteins. Nat. Struct. Biol. 1, 239-245.
    • (1994) , pp. 239-245
    • Skelton, N.J.1    Kördel, J.2    Akke, M.3    Forsén, S.4    Chazin, W.J.5
  • 35
    • 0035047815 scopus 로고    scopus 로고
    • Molecular characterization of a peroxiredoxin from the hard tick Haemaphysalis longicornis
    • Tsuji N., Kamio T., Isobe T., Fujisaki K. Molecular characterization of a peroxiredoxin from the hard tick Haemaphysalis longicornis. Insect. Mol. Biol. 2001, 10:121-129.
    • (2001) Insect. Mol. Biol. , vol.10 , pp. 121-129
    • Tsuji, N.1    Kamio, T.2    Isobe, T.3    Fujisaki, K.4
  • 40
    • 0036542901 scopus 로고    scopus 로고
    • Alternative insecticides: an urgent need
    • Zaim M., Guillet P. Alternative insecticides: an urgent need. Trends Parasitol. 2002, 18:161-163.
    • (2002) Trends Parasitol. , vol.18 , pp. 161-163
    • Zaim, M.1    Guillet, P.2
  • 41
    • 0036489173 scopus 로고    scopus 로고
    • Thrombostasin: purification, molecular cloning and expression of a novel anti-thrombin protein from horn fly saliva
    • Zhang D., Cupp M.S., Cupp E.W. Thrombostasin: purification, molecular cloning and expression of a novel anti-thrombin protein from horn fly saliva. Insect. Biochem. Mol. Biol. 2002, 32:321-330.
    • (2002) Insect. Biochem. Mol. Biol. , vol.32 , pp. 321-330
    • Zhang, D.1    Cupp, M.S.2    Cupp, E.W.3
  • 42
    • 0016757164 scopus 로고
    • The amino acid sequence of bovine cardiac tamponin-C. Comparison with rabbit skeletal troponin-C
    • van Eerd J.P., Takahashi K. The amino acid sequence of bovine cardiac tamponin-C. Comparison with rabbit skeletal troponin-C. Biochem. Biophys. Res. Commun. 1975, 64:122-127.
    • (1975) Biochem. Biophys. Res. Commun. , vol.64 , pp. 122-127
    • van Eerd, J.P.1    Takahashi, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.