메뉴 건너뛰기




Volumn 41, Issue 10, 2014, Pages 6509-6517

New insights into the allergenicity of tropomyosin: a bioinformatics approach

Author keywords

Allergy; Anisakis simplex; Bioinformatics; Epitopes; Evolutionary Marker; Tropomyosin

Indexed keywords

TROPOMYOSIN; ALLERGEN;

EID: 84919399349     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-014-3534-6     Document Type: Article
Times cited : (14)

References (51)
  • 1
    • 39049167419 scopus 로고    scopus 로고
    • Molluscan shellfish allergy
    • PID: 18291306, COI: 1:CAS:528:DC%2BD1cXmtFSmtL0%3D
    • Taylor SL (2008) Molluscan shellfish allergy. Adv Food Nutr Res 54:139–177
    • (2008) Adv Food Nutr Res , vol.54 , pp. 139-177
    • Taylor, S.L.1
  • 2
    • 85006269364 scopus 로고    scopus 로고
    • Not all shellfish “allergy” is allergy!
    • PID: 22410209, COI: 1:CAS:528:DC%2BC38XltF2lu7Y%3D
    • Woo CK, Bahna SL (2011) Not all shellfish “allergy” is allergy! Clin Transl Allergy 1:3
    • (2011) Clin Transl Allergy , vol.1 , pp. 3
    • Woo, C.K.1    Bahna, S.L.2
  • 4
    • 0027991504 scopus 로고
    • Identification of the major brown shrimp (Penaeus aztecus) allergen (Pen a 1) as the muscle protein tropomyosin
    • PID: 7916224, COI: 1:CAS:528:DyaK2cXmsl2ht7s%3D
    • Daul CB, Slattery M, Reese G, Lehrer SB (1994) Identification of the major brown shrimp (Penaeus aztecus) allergen (Pen a 1) as the muscle protein tropomyosin. Int Arch Allergy Immunol 105:49–55
    • (1994) Int Arch Allergy Immunol , vol.105 , pp. 49-55
    • Daul, C.B.1    Slattery, M.2    Reese, G.3    Lehrer, S.B.4
  • 5
    • 0027386139 scopus 로고
    • Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes
    • PID: 7693809, COI: 1:CAS:528:DyaK2cXhtVGhtbw%3D
    • Shanti KN, Martin BM, Nagpal S, Metcalfe DD, Rao PV (1993) Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J Immunol 151:5354–5363
    • (1993) J Immunol , vol.151 , pp. 5354-5363
    • Shanti, K.N.1    Martin, B.M.2    Nagpal, S.3    Metcalfe, D.D.4    Rao, P.V.5
  • 7
    • 36749050495 scopus 로고    scopus 로고
    • Evolutionary distance from human homologs reflects allergenicity of animal food proteins
    • PID: 17935767, COI: 1:CAS:528:DC%2BD2sXhsVSmtb3L
    • Jenkins JA, Breiteneder H, Mills EN (2007) Evolutionary distance from human homologs reflects allergenicity of animal food proteins. J Allergy Clin Immunol 120:1399–1405
    • (2007) J Allergy Clin Immunol , vol.120 , pp. 1399-1405
    • Jenkins, J.A.1    Breiteneder, H.2    Mills, E.N.3
  • 8
    • 79551502921 scopus 로고    scopus 로고
    • Structural and immunologic cross-reactivity among filarial and mite tropomyosin: implications for the higiene hypothesis
    • PID: 21185070, COI: 1:CAS:528:DC%2BC3MXhtlSqurY%3D
    • Santiago HC, Bennuru S, Boyd A, Eberhard M, Nutman TB (2011) Structural and immunologic cross-reactivity among filarial and mite tropomyosin: implications for the higiene hypothesis. J Allergy Clin Immunol 127:479–486
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 479-486
    • Santiago, H.C.1    Bennuru, S.2    Boyd, A.3    Eberhard, M.4    Nutman, T.B.5
  • 9
    • 84873950636 scopus 로고    scopus 로고
    • Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen
    • PID: 23414545, COI: 1:CAS:528:DC%2BC3sXivFaktLo%3D
    • Liu R, Holck AL, Yang E, Liu C, Xue W (2013) Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen. Clin Exp Allergy 43:365–377
    • (2013) Clin Exp Allergy , vol.43 , pp. 365-377
    • Liu, R.1    Holck, A.L.2    Yang, E.3    Liu, C.4    Xue, W.5
  • 10
    • 70149124302 scopus 로고    scopus 로고
    • Survival of the fittest: allergology or parasitology?
    • PID: 19744885
    • Fitzsimmons CM, Dunne DW (2009) Survival of the fittest: allergology or parasitology? Trends Parasitol 25:447–451
    • (2009) Trends Parasitol , vol.25 , pp. 447-451
    • Fitzsimmons, C.M.1    Dunne, D.W.2
  • 11
    • 0033883492 scopus 로고    scopus 로고
    • Is tropomyosin an allergen in Anisakis?
    • PID: 11003461, COI: 1:STN:280:DC%2BD3cvkvFCkuw%3D%3D
    • Asturias JA, Eraso E, Moneo I, Martínez A (2000) Is tropomyosin an allergen in Anisakis? Allergy 55:898–899
    • (2000) Allergy , vol.55 , pp. 898-899
    • Asturias, J.A.1    Eraso, E.2    Moneo, I.3    Martínez, A.4
  • 12
    • 0018762433 scopus 로고
    • Structure and functions of tropomyosins from muscle and non-muscle sources
    • COI: 1:CAS:528:DyaE1MXltVersbY%3D
    • Smillie LB (1979) Structure and functions of tropomyosins from muscle and non-muscle sources. Trends Biochem Sci 4:151–155
    • (1979) Trends Biochem Sci , vol.4 , pp. 151-155
    • Smillie, L.B.1
  • 14
    • 0034070331 scopus 로고    scopus 로고
    • Cloning and high level expression in Escherichia coli of an Anisakis simplex tropomyosin isoform
    • PID: 10838230, COI: 1:CAS:528:DC%2BD3cXjs1ChtbY%3D
    • Asturias JA, Eraso E, Martínez A (2000) Cloning and high level expression in Escherichia coli of an Anisakis simplex tropomyosin isoform. Mol Biochem Parasitol 108:263–267
    • (2000) Mol Biochem Parasitol , vol.108 , pp. 263-267
    • Asturias, J.A.1    Eraso, E.2    Martínez, A.3
  • 15
    • 33746601347 scopus 로고    scopus 로고
    • Allergenic tropomyosins and their cross-reactivities
    • PID: 17073731, COI: 1:CAS:528:DC%2BD28Xotlygurg%3D
    • Jeong KY, Hong CS, Yong TS (2006) Allergenic tropomyosins and their cross-reactivities. Protein Pept Lett 13:835–845
    • (2006) Protein Pept Lett , vol.13 , pp. 835-845
    • Jeong, K.Y.1    Hong, C.S.2    Yong, T.S.3
  • 16
    • 0027386139 scopus 로고
    • Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes
    • PID: 7693809, COI: 1:CAS:528:DyaK2cXhtVGhtbw%3D
    • Shanti KN, Martin BM, Nagpal S, Metcalfe DD, Rao PV (1993) Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J Immunol 151:5354–5363
    • (1993) J Immunol , vol.151 , pp. 5354-5363
    • Shanti, K.N.1    Martin, B.M.2    Nagpal, S.3    Metcalfe, D.D.4    Rao, P.V.5
  • 17
    • 0032913749 scopus 로고    scopus 로고
    • IgE-binding epitopes of shrimp tropomyosin, the major allergen Pen a 1
    • PID: 10224419, COI: 1:CAS:528:DyaK1MXjsV2qtrk%3D
    • Reese G, Ayuso R, Carle T, Lehrer SB (1999) IgE-binding epitopes of shrimp tropomyosin, the major allergen Pen a 1. Int Arch Allergy Immunol 118:300–301
    • (1999) Int Arch Allergy Immunol , vol.118 , pp. 300-301
    • Reese, G.1    Ayuso, R.2    Carle, T.3    Lehrer, S.B.4
  • 18
    • 0032802882 scopus 로고    scopus 로고
    • Tropomyosin: an invertebrate pan-allergen
    • PID: 10474029, COI: 1:CAS:528:DyaK1MXmt1OltLo%3D
    • Reese G, Ayuso R, Lehrer SB (1999) Tropomyosin: an invertebrate pan-allergen. Int Arch Allergy Immunol 119:247–258
    • (1999) Int Arch Allergy Immunol , vol.119 , pp. 247-258
    • Reese, G.1    Ayuso, R.2    Lehrer, S.B.3
  • 22
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: a tool for editing and annotating multiple sequence alignments
    • Nicholas KB, Nicholas HB (1997) GeneDoc: a tool for editing and annotating multiple sequence alignments. Distributed by the author, http://www.nrbsc.org/downloads/
    • (1997) Distributed by the author
    • Nicholas, K.B.1    Nicholas, H.B.2
  • 23
    • 48449095267 scopus 로고    scopus 로고
    • PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery
    • García-Boronat M, Diez-Rivero CM, Reinherz EL, Reche PA (2008) PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery. Nucleic Acids Res 36:35–41
    • (2008) Nucleic Acids Res , vol.36 , pp. 35-41
    • García-Boronat, M.1    Diez-Rivero, C.M.2    Reinherz, E.L.3    Reche, P.A.4
  • 24
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods
    • PID: 21546353, COI: 1:CAS:528:DC%2BC3MXht1eiu73K
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods. Mol Biol Evol 28:2731–2739
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 25
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • COI: 1:CAS:528:DC%2BC3cXks1Kms7s%3D
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O (2010) New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biology 59:307–321
    • (2010) Syst Biology , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 26
    • 0029884694 scopus 로고    scopus 로고
    • GOR secondary structure prediction method version IV
    • PID: 8743705, COI: 1:CAS:528:DyaK28Xltl2ntb4%3D
    • Garnier J, Gibrat JF, Robson B (1996) GOR secondary structure prediction method version IV. Meth Enzymol 266:540–553
    • (1996) Meth Enzymol , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 27
    • 0034161321 scopus 로고    scopus 로고
    • NPS@: Network Protein Sequence Analysis
    • PID: 10694887, COI: 1:CAS:528:DC%2BD3cXhsleiu7Y%3D
    • Combet C, Blanchet C, Geourjon C, Deléage G (2000) NPS@: Network Protein Sequence Analysis. TIBS 25:147–150
    • (2000) TIBS , vol.25 , pp. 147-150
    • Combet, C.1    Blanchet, C.2    Geourjon, C.3    Deléage, G.4
  • 28
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: an approach using the bootstrap
    • Felsenstein J (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783–791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 29
    • 0001895697 scopus 로고
    • Evolutionary divergence and convergence in proteins
    • Bryson V, Vogel HJ, (eds), Academic Press, New York:
    • Zuckerkandl E, Pauling L (1965) Evolutionary divergence and convergence in proteins. In: Bryson V, Vogel HJ (eds) Evolving Genes and Proteins. Academic Press, New York, pp 97–166
    • (1965) Evolving Genes and Proteins , pp. 97-166
    • Zuckerkandl, E.1    Pauling, L.2
  • 31
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • PID: 3447015, COI: 1:STN:280:DyaL1c7ovFSjsA%3D%3D
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406–425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 32
    • 0026660413 scopus 로고
    • A simple method for estimating and testing minimum evolution trees
    • COI: 1:CAS:528:DyaK38Xls1KhsL0%3D
    • Rzhetsky A, Nei M (1992) A simple method for estimating and testing minimum evolution trees. Mol Biol Evol 9:945–967
    • (1992) Mol Biol Evol , vol.9 , pp. 945-967
    • Rzhetsky, A.1    Nei, M.2
  • 34
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • PID: 18367465, COI: 1:CAS:528:DC%2BD1cXotlKgsbg%3D
    • Le SQ, Gascuel O (2008) An improved general amino acid replacement matrix. Mol Biol Evol 25:1307–1320
    • (2008) Mol Biol Evol , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 35
    • 0030807655 scopus 로고    scopus 로고
    • BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data
    • PID: 9254330, COI: 1:CAS:528:DyaK2sXksVahs7o%3D
    • Gascuel O (1997) BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol Biol Evol 14:685–695
    • (1997) Mol Biol Evol , vol.14 , pp. 685-695
    • Gascuel, O.1
  • 36
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: selection of best-fit models of protein evolution
    • PID: 15647292, COI: 1:CAS:528:DC%2BD2MXjsl2ns7Y%3D
    • Abascal F, Zardoya R, Posada D (2005) ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21:2104–2105
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 37
    • 80052479352 scopus 로고    scopus 로고
    • Tropomyosin is a nice marker gene for phylogenetic analysis of molluscs
    • PID: 21132380, COI: 1:CAS:528:DC%2BC3MXhtV2htLnO
    • Wang X, Li L, Xu F, Zhang G (2011) Tropomyosin is a nice marker gene for phylogenetic analysis of molluscs. Mol Biol Rep 38:4589–4593
    • (2011) Mol Biol Rep , vol.38 , pp. 4589-4593
    • Wang, X.1    Li, L.2    Xu, F.3    Zhang, G.4
  • 38
    • 84907148233 scopus 로고    scopus 로고
    • Métodos de inferencia filogenética
    • Peña C (2011) Métodos de inferencia filogenética. Rev Peru Biol 18:265–267
    • (2011) Rev Peru Biol , vol.18 , pp. 265-267
    • Peña, C.1
  • 39
    • 84919358885 scopus 로고    scopus 로고
    • Evaluation of Allergenicity of Genetically Modified Foods. Report of a Joint FAO/WHO Expert Consultation on Allergenicity of Foods Derived from Biotechnology. FAO
    • FAO/WHO (2001) Evaluation of Allergenicity of Genetically Modified Foods. Report of a Joint FAO/WHO Expert Consultation on Allergenicity of Foods Derived from Biotechnology. FAO, Rome
    • (2001) Rome
  • 40
    • 84919358884 scopus 로고    scopus 로고
    • Guideline for the conduct of food safety assessment of foods derived from recombinant DNA plants. In WHO/FAO (ed) Codex Alimentarius Guidelines. Foods derived from modern biotechnology, 2nd edn. FAO
    • FAO/WHO (2009) Guideline for the conduct of food safety assessment of foods derived from recombinant DNA plants. In WHO/FAO (ed) Codex Alimentarius Guidelines. Foods derived from modern biotechnology, 2nd edn. FAO, Rome pp 52–55
    • (2009) Rome pp 52–55
  • 42
    • 28444477329 scopus 로고    scopus 로고
    • Allergy to fish parvalbumins: studies on the cross-reactivity of allergens from 9 commonly consumed fish
    • PID: 16337465
    • Van Do T, Elsayed S, Florvaag E, Hordvik I, Endresen C (2005) Allergy to fish parvalbumins: studies on the cross-reactivity of allergens from 9 commonly consumed fish. J Allergy Clin Immunol 116:1314–1320
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 1314-1320
    • Van Do, T.1    Elsayed, S.2    Florvaag, E.3    Hordvik, I.4    Endresen, C.5
  • 44
    • 0037824392 scopus 로고    scopus 로고
    • Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews
    • PID: 12859453, COI: 1:CAS:528:DC%2BD3sXmt1Wnt7o%3D
    • Fernandes J, Reshef A, Patton L, Ayuso R, Reese G, Lehrer SB (2003) Immunoglobulin E antibody reactivity to the major shrimp allergen, tropomyosin, in unexposed Orthodox Jews. Clin Exp Allergy 33:956–961
    • (2003) Clin Exp Allergy , vol.33 , pp. 956-961
    • Fernandes, J.1    Reshef, A.2    Patton, L.3    Ayuso, R.4    Reese, G.5    Lehrer, S.B.6
  • 45
    • 34548207604 scopus 로고    scopus 로고
    • Structural insight into protein T1, the non-allergenic member of the Bet v 1 allergen family-An in silico analysis
    • PID: 17658604, COI: 1:CAS:528:DC%2BD2sXpslOluro%3D
    • Ghosh D, Gupta-Bhattacharya S (2008) Structural insight into protein T1, the non-allergenic member of the Bet v 1 allergen family-An in silico analysis. Mol Immunol 45:456–462
    • (2008) Mol Immunol , vol.45 , pp. 456-462
    • Ghosh, D.1    Gupta-Bhattacharya, S.2
  • 46
    • 77953806572 scopus 로고    scopus 로고
    • Animals (Metazoa)
    • Hedges SB, Kumar S, (eds), Oxford University Press, Oxford:
    • Blair JE (2009) Animals (Metazoa). In: Hedges SB, Kumar S (eds) The Timetree of Life. Oxford University Press, Oxford, pp 223–230
    • (2009) The Timetree of Life , pp. 223-230
    • Blair, J.E.1
  • 47
    • 0014211361 scopus 로고
    • Construction of phylogenetic trees
    • PID: 5334057, COI: 1:CAS:528:DyaF2sXnt1Gnsw%3D%3D
    • Fitch WM, Margoliash E (1967) Construction of phylogenetic trees. Science 155:279–284
    • (1967) Science , vol.155 , pp. 279-284
    • Fitch, W.M.1    Margoliash, E.2
  • 50
    • 0029591294 scopus 로고
    • The stability of tropomyosin, a two stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface
    • PID: 8527455, COI: 1:CAS:528:DyaK2MXpslChsbY%3D
    • Greenfield NJ, Hitchcock-DeGregori SE (1995) The stability of tropomyosin, a two stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface. Biochemistry 34:16797–16805
    • (1995) Biochemistry , vol.34 , pp. 16797-16805
    • Greenfield, N.J.1    Hitchcock-DeGregori, S.E.2
  • 51
    • 43749096824 scopus 로고    scopus 로고
    • Conserved Asp-137 imparts flexibility to tropomyosin and affects function
    • PID: 18165684, COI: 1:CAS:528:DC%2BD1cXivFyjsbo%3D
    • Sumida JP, Wu E, Lehrer SS (2008) Conserved Asp-137 imparts flexibility to tropomyosin and affects function. J Biol Chem 283:6728–6734
    • (2008) J Biol Chem , vol.283 , pp. 6728-6734
    • Sumida, J.P.1    Wu, E.2    Lehrer, S.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.