메뉴 건너뛰기




Volumn 365, Issue 4, 2008, Pages 685-690

Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity

Author keywords

Allergen; Epitope mapping; IgE binding epitopes; Lipid transfer proteins; Rosaceae fruit allergy

Indexed keywords

ALLERGEN; EPITOPE; IMMUNOGLOBULIN E; LIPID TRANSFER PROTEIN;

EID: 37049037250     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.11.046     Document Type: Article
Times cited : (51)

References (27)
  • 4
    • 0036864152 scopus 로고    scopus 로고
    • Clinical importance of non-specific lipid transfer proteins as food allergens
    • van Ree R. Clinical importance of non-specific lipid transfer proteins as food allergens. Biochem. Soc. Trans. 30 (2002) 910-913
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 910-913
    • van Ree, R.1
  • 5
    • 18844438359 scopus 로고    scopus 로고
    • Nonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class
    • Breiteneder H., and Mills C. Nonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class. Curr. Opin. Allergy Clin. Immunol. 5 (2005) 275-279
    • (2005) Curr. Opin. Allergy Clin. Immunol. , vol.5 , pp. 275-279
    • Breiteneder, H.1    Mills, C.2
  • 6
    • 0036864268 scopus 로고    scopus 로고
    • Pathogenesis-related (PR)-proteins identified as allergens
    • Hoffmann-Sommergruber K. Pathogenesis-related (PR)-proteins identified as allergens. Biochem. Soc. Trans. 30 (2002) 930-935
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 930-935
    • Hoffmann-Sommergruber, K.1
  • 8
    • 31344451312 scopus 로고    scopus 로고
    • Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
    • Pasquato N., Berni R., Folli C., Cianci M., Pantano S., Helliwell J.R., and Zanotti G. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J. Mol. Biol. 356 (2006) 684-694
    • (2006) J. Mol. Biol. , vol.356 , pp. 684-694
    • Pasquato, N.1    Berni, R.2    Folli, C.3    Cianci, M.4    Pantano, S.5    Helliwell, J.R.6    Zanotti, G.7
  • 12
    • 33750961047 scopus 로고    scopus 로고
    • The lipid transfer protein (LTP) essentially concentrate in the skin of Rosaceae fruits as a cell-surface exposed allergen
    • Borges J.P., Jauneau A., Brulé C., Culerrier R., Barre A., Didier A., and Rougé P. The lipid transfer protein (LTP) essentially concentrate in the skin of Rosaceae fruits as a cell-surface exposed allergen. Plant Physiol. Biochem. 44 (2006) 535-542
    • (2006) Plant Physiol. Biochem. , vol.44 , pp. 535-542
    • Borges, J.P.1    Jauneau, A.2    Brulé, C.3    Culerrier, R.4    Barre, A.5    Didier, A.6    Rougé, P.7
  • 14
    • 8744295783 scopus 로고    scopus 로고
    • Clinical role of lipid transfer proteins in food allergy
    • Pastorello E.A., and Robino A.M. Clinical role of lipid transfer proteins in food allergy. Mol. Nutr. Food Res. 48 (2004) 356-362
    • (2004) Mol. Nutr. Food Res. , vol.48 , pp. 356-362
    • Pastorello, E.A.1    Robino, A.M.2
  • 15
    • 34248138941 scopus 로고    scopus 로고
    • Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases
    • Zuidmeer L., and van Ree R. Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases. Curr. Opin. Allergy Clin. Immunol. 7 (2007) 269-273
    • (2007) Curr. Opin. Allergy Clin. Immunol. , vol.7 , pp. 269-273
    • Zuidmeer, L.1    van Ree, R.2
  • 17
    • 33845790480 scopus 로고    scopus 로고
    • How reliable is the structural prediction of IgE-binding epitopes of allergens: the case study of plant lipid transfer proteins
    • Borges J.-P., Barre A., Culerrier R., Archimbaud N., Didier A., and Rougé P. How reliable is the structural prediction of IgE-binding epitopes of allergens: the case study of plant lipid transfer proteins. Biochimie 89 (2007) 83-91
    • (2007) Biochimie , vol.89 , pp. 83-91
    • Borges, J.-P.1    Barre, A.2    Culerrier, R.3    Archimbaud, N.4    Didier, A.5    Rougé, P.6
  • 18
    • 0026656122 scopus 로고
    • Spot-synthesis: an easy technique for the positionally addressable parallel chemical synthesis on a membrane support
    • Frank R. Spot-synthesis: an easy technique for the positionally addressable parallel chemical synthesis on a membrane support. Tetrahedron 48 (1992) 9217-9232
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 19
    • 0036721676 scopus 로고    scopus 로고
    • Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding
    • Laune D., Molina F., Ferrieres G., Villard S., Bes C., Rieunier F., Chardes T., and Granier C. Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding. J. Immunol. Methods 267 (2002) 53-70
    • (2002) J. Immunol. Methods , vol.267 , pp. 53-70
    • Laune, D.1    Molina, F.2    Ferrieres, G.3    Villard, S.4    Bes, C.5    Rieunier, F.6    Chardes, T.7    Granier, C.8
  • 20
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., and Suh S.W. High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure 3 (1995) 189-199
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 21
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder J.W., and Richards F.M. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193 (1987) 775-791
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemistry of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemistry of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struc. Func. Genet. 11 (1991) 281-296
    • (1991) Proteins Struc. Func. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
  • 27
    • 20144386252 scopus 로고    scopus 로고
    • Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity
    • Barre A., Borges J.-P., and Rougé P. Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity. Biochimie 87 (2005) 499-506
    • (2005) Biochimie , vol.87 , pp. 499-506
    • Barre, A.1    Borges, J.-P.2    Rougé, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.