메뉴 건너뛰기




Volumn 58, Issue 5, 2014, Pages 1144-1155

Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: A comprehensive allergenomic approach

Author keywords

Allergen dimers; Allergen fragments; Black tiger prawn; Heat processing; In vitro diagnostics

Indexed keywords

ALLERGEN; IMMUNOGLOBULIN E; RECOMBINANT PROTEIN; TROPOMYOSIN;

EID: 84896804037     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201300584     Document Type: Article
Times cited : (106)

References (32)
  • 2
    • 3442895900 scopus 로고    scopus 로고
    • Prevalence of seafood allergy in the United States determined by a random telephone survey
    • Sicherer, S. H., Munoz-Furlong, A., Sampson, H. A., Prevalence of seafood allergy in the United States determined by a random telephone survey. J. Allergy Clin. Immunol. 2004, 114, 159-165.
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 159-165
    • Sicherer, S.H.1    Munoz-Furlong, A.2    Sampson, H.A.3
  • 3
    • 34248380799 scopus 로고    scopus 로고
    • Bioinformatics applied to allergy: allergen databases, from collecting sequence information to data integration. The Allergome platform as a model
    • Mari, A., Scala, E., Palazzo, P., Ridolfi, S. et al., Bioinformatics applied to allergy: allergen databases, from collecting sequence information to data integration. The Allergome platform as a model. Cell. Immunol. 2006, 244, 97-100.
    • (2006) Cell. Immunol. , vol.244 , pp. 97-100
    • Mari, A.1    Scala, E.2    Palazzo, P.3    Ridolfi, S.4
  • 4
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • Radauer, C., Bublin, M., Wagner, S., Mari, A. et al., Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J. Allergy Clin. Immunol. 2008, 121, 847-852.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 847-852
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4
  • 5
    • 33645316499 scopus 로고    scopus 로고
    • Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, Penaeus aztecus
    • Reese, G., Schicktanz, S., Lauer, I., Randow, S. et al., Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, Penaeus aztecus. Clin. Exp. Allergy 2006, 36, 517-524.
    • (2006) Clin. Exp. Allergy , vol.36 , pp. 517-524
    • Reese, G.1    Schicktanz, S.2    Lauer, I.3    Randow, S.4
  • 7
    • 77955361387 scopus 로고    scopus 로고
    • Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry
    • Abdel Rahman, A. M., Kamath, S., Lopata, A. L., Helleur, R. J., Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry. Rapid Commun. Mass Spectrom. 2010, 24, 2462-2470.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 2462-2470
    • Abdel Rahman, A.M.1    Kamath, S.2    Lopata, A.L.3    Helleur, R.J.4
  • 8
    • 77950612737 scopus 로고    scopus 로고
    • Characterization and de novo sequencing of snow crab tropomyosin enzymatic peptides by both electrospray ionization and matrix-assisted laser desorption ionization QqToF tandem mass spectrometry
    • Abdel Rahman, A. M., Lopata, A. L., O'Hehir, R. E., Robinson, J. J. et al., Characterization and de novo sequencing of snow crab tropomyosin enzymatic peptides by both electrospray ionization and matrix-assisted laser desorption ionization QqToF tandem mass spectrometry. J. Mass Spectrom. 2010, 45, 372-381.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 372-381
    • Abdel Rahman, A.M.1    Lopata, A.L.2    O'Hehir, R.E.3    Robinson, J.J.4
  • 10
    • 80052657523 scopus 로고    scopus 로고
    • Tropomyosin IgE-positive results are a good predictor of shrimp allergy
    • Gámez, C., Sánchez-García, S., Ibáñez, M. D., López, R. et al., Tropomyosin IgE-positive results are a good predictor of shrimp allergy. Allergy 2011, 66, 1375-1383.
    • (2011) Allergy , vol.66 , pp. 1375-1383
    • Gámez, C.1    Sánchez-García, S.2    Ibáñez, M.D.3    López, R.4
  • 11
    • 77950299077 scopus 로고    scopus 로고
    • Measurement of IgE antibodies to shrimp tropomyosin is superior to skin prick testing with commercial extract and measurement of IgE to shrimp for predicting clinically relevant allergic reactions after shrimp ingestion
    • Yang, A. C., Arruda, L. K., Santos, A. B. R., Barbosa, M. C. R. et al., Measurement of IgE antibodies to shrimp tropomyosin is superior to skin prick testing with commercial extract and measurement of IgE to shrimp for predicting clinically relevant allergic reactions after shrimp ingestion. J. Allergy Clin. Immunol. 2010, 125, 872-878.
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 872-878
    • Yang, A.C.1    Arruda, L.K.2    Santos, A.B.R.3    Barbosa, M.C.R.4
  • 12
    • 84879218827 scopus 로고    scopus 로고
    • IgE reactivity of blue swimmer crab Portunus pelagicus tropomyosin, por p 1, and other allergens; cross-reactivity with black tiger prawn and effects of heating
    • Abramovitch, J. B., Kamath, S., Varese, N., Zubrinich, C. et al., IgE reactivity of blue swimmer crab Portunus pelagicus tropomyosin, por p 1, and other allergens; cross-reactivity with black tiger prawn and effects of heating. PLoS ONE 2013, 8, e67487.
    • (2013) PLoS ONE , vol.8
    • Abramovitch, J.B.1    Kamath, S.2    Varese, N.3    Zubrinich, C.4
  • 13
    • 78650305492 scopus 로고    scopus 로고
    • Biomolecular characterization of allergenic proteins in snow crab (Chionoecetes opilio) and de novo sequencing of the second allergen arginine kinase using tandem mass spectrometry
    • Abdel Rahman, A. M., Kamath, S. D., Lopata, A. L., Robinson, J. J. et al., Biomolecular characterization of allergenic proteins in snow crab (Chionoecetes opilio) and de novo sequencing of the second allergen arginine kinase using tandem mass spectrometry. J. Proteomics 2011, 74, 231-241.
    • (2011) J. Proteomics , vol.74 , pp. 231-241
    • Abdel Rahman, A.M.1    Kamath, S.D.2    Lopata, A.L.3    Robinson, J.J.4
  • 14
    • 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
  • 15
    • 4444221565 scopus 로고    scopus 로고
    • UCSF chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S. et al., UCSF chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 2004, 25, 1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3    Couch, G.S.4
  • 16
    • 6344225313 scopus 로고    scopus 로고
    • Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity
    • Drew, A. C., Eusebius, N. P., Kenins, L., de Silva, H. D. et al., Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity. J. Immunol. 2004, 173, 5872-5879.
    • (2004) J. Immunol. , vol.173 , pp. 5872-5879
    • Drew, A.C.1    Eusebius, N.P.2    Kenins, L.3    de Silva, H.D.4
  • 17
    • 78049378681 scopus 로고    scopus 로고
    • Proteome mining for novel IgE-binding proteins from the German cockroach (Blattella germanica) and allergen profiling of patients
    • Chuang, J. G., Su, S. N., Chiang, B. L., Lee, H. J. et al., Proteome mining for novel IgE-binding proteins from the German cockroach (Blattella germanica) and allergen profiling of patients. Proteomics 2010, 10, 3854-3867.
    • (2010) Proteomics , vol.10 , pp. 3854-3867
    • Chuang, J.G.1    Su, S.N.2    Chiang, B.L.3    Lee, H.J.4
  • 18
    • 80051938257 scopus 로고    scopus 로고
    • Generation of a comprehensive panel of crustacean allergens from the North Sea shrimp Crangon crangon
    • Bauermeister, K., Wangorsch, A., Garoffo, L. P., Reuter, A. et al., Generation of a comprehensive panel of crustacean allergens from the North Sea shrimp Crangon crangon. Mol. Immunol. 2011, 48, 1983-1992.
    • (2011) Mol. Immunol. , vol.48 , pp. 1983-1992
    • Bauermeister, K.1    Wangorsch, A.2    Garoffo, L.P.3    Reuter, A.4
  • 19
    • 84856484030 scopus 로고    scopus 로고
    • Is epitope recognition of shrimp allergens useful to predict clinical reactivity
    • Ayuso, R., Sanchez-Garcia, S., Pascal, M., Lin, J. et al., Is epitope recognition of shrimp allergens useful to predict clinical reactivity? Clin. Exp. Allergy 2012, 42, 293-304.
    • (2012) Clin. Exp. Allergy , vol.42 , pp. 293-304
    • Ayuso, R.1    Sanchez-Garcia, S.2    Pascal, M.3    Lin, J.4
  • 20
    • 67651213741 scopus 로고    scopus 로고
    • Relevance of IgE binding to short peptides for the allergenic activity of food allergens
    • Albrecht, M., Kuhne, Y., Ballmer-Weber, B. K., Becker, W. M. et al., Relevance of IgE binding to short peptides for the allergenic activity of food allergens. J. Allergy Clin. Immunol. 2009, 124, 328-336.
    • (2009) J. Allergy Clin. Immunol. , vol.124 , pp. 328-336
    • Albrecht, M.1    Kuhne, Y.2    Ballmer-Weber, B.K.3    Becker, W.M.4
  • 21
    • 84884634149 scopus 로고    scopus 로고
    • Impact of heat processing on the detection of the major shellfish allergen tropomyosin in crustaceans and molluscs using specific monoclonal antibodies
    • Kamath, S. D., Abdel Rahman, A. M., Komoda, T., Lopata, A. L., Impact of heat processing on the detection of the major shellfish allergen tropomyosin in crustaceans and molluscs using specific monoclonal antibodies. Food Chem. 2013, 141, 4031-4039.
    • (2013) Food Chem. , vol.141 , pp. 4031-4039
    • Kamath, S.D.1    Abdel Rahman, A.M.2    Komoda, T.3    Lopata, A.L.4
  • 22
    • 84873403931 scopus 로고    scopus 로고
    • Comprehensive proteomics approach in characterizing and quantifying allergenic proteins from northern shrimp: toward better occupational asthma prevention
    • Abdel Rahman, A. M., Kamath, S. D., Gagne, S., Lopata, A. L. et al., Comprehensive proteomics approach in characterizing and quantifying allergenic proteins from northern shrimp: toward better occupational asthma prevention. J. Proteome Res. 2013, 12, 647-656.
    • (2013) J. Proteome Res. , vol.12 , pp. 647-656
    • Abdel Rahman, A.M.1    Kamath, S.D.2    Gagne, S.3    Lopata, A.L.4
  • 24
    • 67649233033 scopus 로고    scopus 로고
    • Sarcoplasmic calcium-binding protein is an EF-hand-type protein identified as a new shrimp allergen
    • Ayuso, R., Grishina, G., Ibanez, M. D., Blanco, C. et al., Sarcoplasmic calcium-binding protein is an EF-hand-type protein identified as a new shrimp allergen. J. Allergy Clin. Immunol. 2009, 124, 114-120.
    • (2009) J. Allergy Clin. Immunol. , vol.124 , pp. 114-120
    • Ayuso, R.1    Grishina, G.2    Ibanez, M.D.3    Blanco, C.4
  • 26
    • 84898929039 scopus 로고
    • Titin is an extraordinarily long and flexible myofibrillar protein
    • Wang, K., Ramirezmitchell, R., Titin is an extraordinarily long and flexible myofibrillar protein. J. Cell Biol. 1982, 95, A372-A372.
    • (1982) J. Cell Biol. , vol.95
    • Wang, K.1    Ramirezmitchell, R.2
  • 27
    • 0344394432 scopus 로고    scopus 로고
    • The entire cDNA sequences of projectin isoforms of crayfish claw closer and flexor muscles and their localization
    • Oshino, T., Shimamura, J., Fukuzawa, A., Maruyama, K. et al., The entire cDNA sequences of projectin isoforms of crayfish claw closer and flexor muscles and their localization. J. Muscle Res. Cell Motil. 2003, 24, 431-438.
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 431-438
    • Oshino, T.1    Shimamura, J.2    Fukuzawa, A.3    Maruyama, K.4
  • 28
    • 0028030181 scopus 로고
    • Titin-related protein in invertebrate muscles
    • Ziegler, C., Titin-related protein in invertebrate muscles. Comp. Biochem. Physiol. A-Physiol. 1994, 109, 823-833.
    • (1994) Comp. Biochem. Physiol. A-Physiol. , vol.109 , pp. 823-833
    • Ziegler, C.1
  • 29
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: an immunologic perspective
    • Rosenberg, A. S., Effects of protein aggregates: an immunologic perspective. AAPS J. 2006, 8, E501-E507.
    • (2006) AAPS J. , vol.8
    • Rosenberg, A.S.1
  • 31
    • 79955554029 scopus 로고    scopus 로고
    • The effect of simulated gastrointestinal digestion on shrimp Penaeus vannamei allergenicity
    • Guo, Y. C., Li, Z. X., Lin, H., The effect of simulated gastrointestinal digestion on shrimp Penaeus vannamei allergenicity. Chinese J. Oceanol. Limnol. 2009, 27, 703-707.
    • (2009) Chinese J. Oceanol. Limnol. , vol.27 , pp. 703-707
    • Guo, Y.C.1    Li, Z.X.2    Lin, H.3
  • 32
    • 29144449172 scopus 로고    scopus 로고
    • Reduced allergenic potency of VR9-1, a mutant of the major shrimp allergen Pen a 1 (tropomyosin)
    • Reese, G., Viebranz, J., Leong-Kee, S. M., Plante, M. et al., Reduced allergenic potency of VR9-1, a mutant of the major shrimp allergen Pen a 1 (tropomyosin). J. Immunol. 2005, 175, 8354-8364.
    • (2005) J. Immunol. , vol.175 , pp. 8354-8364
    • Reese, G.1    Viebranz, J.2    Leong-Kee, S.M.3    Plante, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.