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Volumn 423, Issue 2, 2012, Pages 169-181

Alpha-1 giardin is an annexin with highly unusual calcium-regulated mechanisms

Author keywords

giardiasis; host pathogen interaction; protein membrane interactions

Indexed keywords

ALPHA 1 GIARDIN; ANNEXIN; CALCIUM; CALCIUM BINDING PROTEIN; DIMER; GLYCOSAMINOGLYCAN; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 84866484049     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.041     Document Type: Article
Times cited : (19)

References (53)
  • 1
    • 33750984241 scopus 로고    scopus 로고
    • Field testing of a fenbendazole treatment combined with hygienic and management measures against a natural Giardia infection in calves
    • T. Geurden, J. Vercruysse, and E. Claerebout Field testing of a fenbendazole treatment combined with hygienic and management measures against a natural Giardia infection in calves Vet. Parasitol. 142 2006 367 371
    • (2006) Vet. Parasitol. , vol.142 , pp. 367-371
    • Geurden, T.1    Vercruysse, J.2    Claerebout, E.3
  • 2
    • 33646484063 scopus 로고    scopus 로고
    • Giardia and Cryptosporidium join the 'Neglected Diseases Initiative'
    • L. Savioli, H. Smith, and A. Thompson Giardia and Cryptosporidium join the 'Neglected Diseases Initiative' Trends Parasitol. 22 2006 203 208
    • (2006) Trends Parasitol. , vol.22 , pp. 203-208
    • Savioli, L.1    Smith, H.2    Thompson, A.3
  • 3
    • 77958526575 scopus 로고    scopus 로고
    • Giardiasis in the post genomic era: Treatment, drug resistance and novel therapeutic perspectives
    • M. Lalle Giardiasis in the post genomic era: treatment, drug resistance and novel therapeutic perspectives Infect. Disord. Drug Targets 10 2010 283 294
    • (2010) Infect. Disord. Drug Targets , vol.10 , pp. 283-294
    • Lalle, M.1
  • 5
    • 0029300651 scopus 로고
    • Annexin homologues in Giardia lamblia
    • K. Fiedler, and K. Simons Annexin homologues in Giardia lamblia Trends Biochem. Sci. 20 1995 177 178
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 177-178
    • Fiedler, K.1    Simons, K.2
  • 6
  • 7
    • 0027167511 scopus 로고
    • SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil
    • K. Weber, N. Geisler, U. Plessmann, A. Bremerich, K.F. Lechtreck, and M. Melkonian SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil J. Cell Biol. 121 1993 837 845
    • (1993) J. Cell Biol. , vol.121 , pp. 837-845
    • Weber, K.1    Geisler, N.2    Plessmann, U.3    Bremerich, A.4    Lechtreck, K.F.5    Melkonian, M.6
  • 8
    • 0026496442 scopus 로고
    • Identification and characterization of gamma-giardin and the gamma-giardin gene from Giardia lamblia
    • A. Nohria, R.A. Alonso, and D.A. Peattie Identification and characterization of gamma-giardin and the gamma-giardin gene from Giardia lamblia Mol. Biochem. Parasitol. 56 1992 27 37
    • (1992) Mol. Biochem. Parasitol. , vol.56 , pp. 27-37
    • Nohria, A.1    Alonso, R.A.2    Peattie, D.A.3
  • 9
    • 77958184452 scopus 로고    scopus 로고
    • Parasite annexins - New molecules with potential for drug and vaccine development
    • A. Hofmann, A. Osman, C.Y. Leow, P. Driguez, D.P. McManus, and M.K. Jones Parasite annexins - new molecules with potential for drug and vaccine development BioEssays 32 2010 967 976
    • (2010) BioEssays , vol.32 , pp. 967-976
    • Hofmann, A.1    Osman, A.2    Leow, C.Y.3    Driguez, P.4    McManus, D.P.5    Jones, M.K.6
  • 10
    • 34848894621 scopus 로고    scopus 로고
    • Genomic minimalism in the early diverging intestinal parasite Giardia lamblia
    • H.G. Morrison, A.G. McArthur, F.D. Gillin, S.B. Aley, R.D. Adam, and G.J. Olsen Genomic minimalism in the early diverging intestinal parasite Giardia lamblia Science 317 2007 1921 1926
    • (2007) Science , vol.317 , pp. 1921-1926
    • Morrison, H.G.1    McArthur, A.G.2    Gillin, F.D.3    Aley, S.B.4    Adam, R.D.5    Olsen, G.J.6
  • 11
    • 0024447603 scopus 로고
    • Ultrastructural localization of giardins to the edges of disk microribbons of Giardia lamblia and the nucleotide and deduced protein sequence of alpha giardin
    • D.A. Peattie, R.A. Alonso, A. Hein, and J.P. Caulfield Ultrastructural localization of giardins to the edges of disk microribbons of Giardia lamblia and the nucleotide and deduced protein sequence of alpha giardin J. Cell Biol. 109 1989 2323 2335
    • (1989) J. Cell Biol. , vol.109 , pp. 2323-2335
    • Peattie, D.A.1    Alonso, R.A.2    Hein, A.3    Caulfield, J.P.4
  • 12
    • 18044380882 scopus 로고    scopus 로고
    • Annexin-like alpha giardins: A new cytoskeletal gene family in Giardia lamblia
    • M. Weiland, A. McArthur, H. Morrison, M. Sogin, and S. Svärd Annexin-like alpha giardins: a new cytoskeletal gene family in Giardia lamblia Int. J. Parasitol. 35 2005 617 626
    • (2005) Int. J. Parasitol. , vol.35 , pp. 617-626
    • Weiland, M.1    McArthur, A.2    Morrison, H.3    Sogin, M.4    Svärd, S.5
  • 15
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu. Rev. Biochem. 69 2000 531 569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 16
    • 0033609079 scopus 로고    scopus 로고
    • The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1
    • J.C. Reeder, A.F. Cowman, K.M. Davern, J.G. Beeson, J.K. Thompson, S.J. Rogerson, and G.V. Brown The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1 Proc. Natl Acad. Sci. USA 96 1999 5198 5202
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 5198-5202
    • Reeder, J.C.1    Cowman, A.F.2    Davern, K.M.3    Beeson, J.G.4    Thompson, J.K.5    Rogerson, S.J.6    Brown, G.V.7
  • 17
    • 3242752562 scopus 로고    scopus 로고
    • Proteins that recognise glycans. Microbial carbohydrate-binding proteins
    • A. Varki, R. Cummings, J.D. Esko, H. Freeze, G. Hart, J. Marth, Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • J.D. Esko Proteins that recognise glycans. Microbial carbohydrate-binding proteins A. Varki, R. Cummings, J.D. Esko, H. Freeze, G. Hart, J. Marth, Essentials of Glycobiology 1999 Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • (1999) Essentials of Glycobiology
    • Esko, J.D.1
  • 18
    • 0037033081 scopus 로고    scopus 로고
    • A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes
    • Y. Tsujii-Hayashi, M. Kitahara, T. Yamagaki, K. Kojima-Aikawa, and I. Matsumoto A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes J. Biol. Chem. 277 2002 47493 47499
    • (2002) J. Biol. Chem. , vol.277 , pp. 47493-47499
    • Tsujii-Hayashi, Y.1    Kitahara, M.2    Yamagaki, T.3    Kojima-Aikawa, K.4    Matsumoto, I.5
  • 19
    • 0035148547 scopus 로고    scopus 로고
    • Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surface
    • I. Capila, M. Hernaiz, Y. Mo, T. Mealy, B. Campos, and J. Dedman Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surface Structure 9 2001 57 64
    • (2001) Structure , vol.9 , pp. 57-64
    • Capila, I.1    Hernaiz, M.2    Mo, Y.3    Mealy, T.4    Campos, B.5    Dedman, J.6
  • 20
    • 0037101954 scopus 로고    scopus 로고
    • Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains
    • H. Takagi, Y. Asano, N. Yamakawa, I. Matsumoto, and K. Kimata Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains J. Cell Sci. 115 2002 3309 3318
    • (2002) J. Cell Sci. , vol.115 , pp. 3309-3318
    • Takagi, H.1    Asano, Y.2    Yamakawa, N.3    Matsumoto, I.4    Kimata, K.5
  • 21
    • 0141867659 scopus 로고    scopus 로고
    • Characterisation of alpha-1 giardin: An immunodominant Giardia lamblia annexin with glycosaminoglycan-binding activity
    • M. Weiland, J. Palm, W. Griffiths, J. McCaffery, and S. Svärd Characterisation of alpha-1 giardin: an immunodominant Giardia lamblia annexin with glycosaminoglycan-binding activity Int. J. Parasitol. 33 2003 1341 1351
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1341-1351
    • Weiland, M.1    Palm, J.2    Griffiths, W.3    McCaffery, J.4    Svärd, S.5
  • 22
    • 33745619239 scopus 로고    scopus 로고
    • Biochemical characterization of annexin B1 from Cysticercus cellulosae
    • A. Winter, A.M. Yusof, E. Gao, H.L. Yan, and A. Hofmann Biochemical characterization of annexin B1 from Cysticercus cellulosae FEBS J. 273 2006 3238 3247
    • (2006) FEBS J. , vol.273 , pp. 3238-3247
    • Winter, A.1    Yusof, A.M.2    Gao, E.3    Yan, H.L.4    Hofmann, A.5
  • 23
    • 33947595016 scopus 로고    scopus 로고
    • Apo and calcium-bound crystal structures of alpha-11 giardin, an unusual annexin from Giardia lamblia
    • P. Pathuri, E.T. Nguyen, S.G. Svard, and H. Luecke Apo and calcium-bound crystal structures of alpha-11 giardin, an unusual annexin from Giardia lamblia J. Mol. Biol. 368 2007 493 508
    • (2007) J. Mol. Biol. , vol.368 , pp. 493-508
    • Pathuri, P.1    Nguyen, E.T.2    Svard, S.G.3    Luecke, H.4
  • 24
    • 58149333150 scopus 로고    scopus 로고
    • Apo and calcium-bound crystal structures of cytoskeletal protein alpha-14 giardin (annexin E1) from the intestinal protozoan parasite Giardia lamblia
    • P. Pathuri, E.T. Nguyen, G. Ozorowski, S.G. Svärd, and H. Luecke Apo and calcium-bound crystal structures of cytoskeletal protein alpha-14 giardin (annexin E1) from the intestinal protozoan parasite Giardia lamblia J. Mol. Biol. 385 2009 1098 1112
    • (2009) J. Mol. Biol. , vol.385 , pp. 1098-1112
    • Pathuri, P.1    Nguyen, E.T.2    Ozorowski, G.3    Svärd, S.G.4    Luecke, H.5
  • 25
    • 81955164754 scopus 로고    scopus 로고
    • A1-giardin based live heterologous vaccine protects against Giardia lamblia infection in a murine model
    • G. Jenikova, P. Hruz, M.K. Andersson, N. Tejman-Yarden, P.C.D. Ferreira, and Y.S. Andersen A1-giardin based live heterologous vaccine protects against Giardia lamblia infection in a murine model Vaccine 29 2011 9529 9537
    • (2011) Vaccine , vol.29 , pp. 9529-9537
    • Jenikova, G.1    Hruz, P.2    Andersson, M.K.3    Tejman-Yarden, N.4    Ferreira, P.C.D.5    Andersen, Y.S.6
  • 26
    • 0022507173 scopus 로고
    • A consensus amino acid sequence repeat in Torpedo and mammalian calcium-dependent membrane binding proteins
    • M. Geisow, U. Fritsche, J. Hexham, B. Dash, and T. Johnson A consensus amino acid sequence repeat in Torpedo and mammalian calcium-dependent membrane binding proteins Nature 320 1986 636 638
    • (1986) Nature , vol.320 , pp. 636-638
    • Geisow, M.1    Fritsche, U.2    Hexham, J.3    Dash, B.4    Johnson, T.5
  • 27
    • 0030966570 scopus 로고    scopus 로고
    • Annexins - From structure to function
    • J. Benz, and A. Hofmann Annexins - from structure to function Biol. Chem. 378 1997 177 183
    • (1997) Biol. Chem. , vol.378 , pp. 177-183
    • Benz, J.1    Hofmann, A.2
  • 30
    • 80052323135 scopus 로고    scopus 로고
    • Giardia flagellar motility is not directly required to maintain attachment to surfaces
    • S.A. House, D.J. Richter, J.K. Pham, and S.C. Dawson Giardia flagellar motility is not directly required to maintain attachment to surfaces PLoS Pathog. 7 2011 e1002167
    • (2011) PLoS Pathog. , vol.7 , pp. 1002167
    • House, S.A.1    Richter, D.J.2    Pham, J.K.3    Dawson, S.C.4
  • 32
    • 0027410046 scopus 로고
    • The pRSET family of T7 promoter expression vectors for Escherichia coli
    • R. Schoepfer The pRSET family of T7 promoter expression vectors for Escherichia coli Gene 124 1993 83 85
    • (1993) Gene , vol.124 , pp. 83-85
    • Schoepfer, R.1
  • 33
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.1
  • 34
    • 0035870953 scopus 로고    scopus 로고
    • Polyacrylamide gel electrophoresis without a stacking gel: Use of amino acids as electrolytes
    • T. Ahn, S. Yim, H. Choi, and C. Yun Polyacrylamide gel electrophoresis without a stacking gel: use of amino acids as electrolytes Anal. Biochem. 291 2001 300 303
    • (2001) Anal. Biochem. , vol.291 , pp. 300-303
    • Ahn, T.1    Yim, S.2    Choi, H.3    Yun, C.4
  • 35
    • 33847803989 scopus 로고
    • Metal cluster halide complexes. I. Efficient synthesis of hydrated hexanuclear niobium and tantalum cluster halides M6X14*8H2O
    • F. Koknat, J. Parsons, and A. Vongvusharintra Metal cluster halide complexes. I. Efficient synthesis of hydrated hexanuclear niobium and tantalum cluster halides M6X14*8H2O Inorg. Chem. 13 1974 1699 1702
    • (1974) Inorg. Chem. , vol.13 , pp. 1699-1702
    • Koknat, F.1    Parsons, J.2    Vongvusharintra, A.3
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D , vol.50 , pp. 760-763
  • 40
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • T.A. Jones, J.Y. Zou, S. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and location of errors in these models Acta Crystallogr., Sect. A 47 1991 110 119
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 43
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R. Laskowski, M. MacArthur, D. Moss, and J. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26 1993 283 291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 44
    • 0036173404 scopus 로고    scopus 로고
    • PCSB - A program collection for structural biology and biophysical chemistry
    • A. Hofmann, and A. Wlodawer PCSB - a program collection for structural biology and biophysical chemistry Bioinformatics 18 2002 209 210
    • (2002) Bioinformatics , vol.18 , pp. 209-210
    • Hofmann, A.1    Wlodawer, A.2
  • 45
    • 0041935939 scopus 로고    scopus 로고
    • version 1.30 National Institutes of Health, Bethesda, MD
    • Rasband, W. (2005). ImageJ, version 1.30. National Institutes of Health, Bethesda, MD, http://rsb.info.nih.gov/ij/.
    • (2005) ImageJ
    • Rasband, W.1
  • 46
    • 0014468553 scopus 로고
    • Formation and properties of thin-walled phospholipid vesicles
    • J. Reeves, and R. Dowben Formation and properties of thin-walled phospholipid vesicles J. Cell. Physiol. 73 1969 49 60
    • (1969) J. Cell. Physiol. , vol.73 , pp. 49-60
    • Reeves, J.1    Dowben, R.2
  • 47
    • 0242317911 scopus 로고    scopus 로고
    • Liposomes in assessment of annexin-membrane interactions
    • A. Hofmann, and R. Huber Liposomes in assessment of annexin-membrane interactions Methods Enzymol. 372 2003 186 216
    • (2003) Methods Enzymol. , vol.372 , pp. 186-216
    • Hofmann, A.1    Huber, R.2
  • 49
    • 0026244044 scopus 로고
    • GNOM: A program package for small-angle scattering data processing
    • A. Semenyuk, and D. Svergun GNOM: a program package for small-angle scattering data processing J. Appl. Crystallogr. 24 1991 537 540
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.1    Svergun, D.2
  • 51
    • 80052470762 scopus 로고    scopus 로고
    • Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models
    • A. Ortega, D. Amoros, and J.G. de la Torre Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models Biophys. J. 101 2011 892 898
    • (2011) Biophys. J. , vol.101 , pp. 892-898
    • Ortega, A.1    Amoros, D.2    De La Torre, J.G.3
  • 52
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A. Brünger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.1


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