TY - JOUR
T1 - Major linear IgE epitopes of mountain cedar pollen allergen Jun a 1 map to the pectate lyase catalytic site
AU - Midoro-Horiuti, Terumi
AU - Mathura, Venkatarajan
AU - Schein, Catherine H.
AU - Braun, Werner
AU - Yu, Shaoning
AU - Watanabe, Masanao
AU - Lee, J. Ching
AU - Brooks, Edward G.
AU - Goldblum, Randall M.
N1 - Funding Information:
We wish to thank Dr. Julius van Bavel for providing sera from patient with mountain cedar pollinosis. The study was supported by a NICHD-sponsored Child Health Research Center (P30 HD27841, New Project Award, T.M.H.), NIEHS Center for Environmental Science (ES06676, T.M.H.), the John Sealy Memorial Endowment for Biomedical Research (R.M.G., T.M.H. and W.B.) from UTMB, Advanced Technology Program from Texas Higher Education Coordinating Board (R.M.G.) and Parker B. Francis Fellowship in Pulmonary Research from Francis Families Foundation (T.M.H.), grant support FDA (FD-U-002249-1, W.B.).
PY - 2003/12
Y1 - 2003/12
N2 - Resolution of the 3D structures and IgE epitopes of allergens may identify common or conserved features of allergens. Jun a 1, the predominant allergen in mountain cedar pollen, was chosen as a model for identifying common structural and functional features among a group of plant allergens. In this study, synthetic, overlapping peptides of Jun a 1 and sera from patients allergic to mountain cedar pollen were used to identify linear epitopes. A 3D model of Jun a 1 was produced using the Bacillus subtiles pectate lyase (PL) as a template and validated with biophysical measurements. This allowed mappings of four IgE binding sites on Jun a 1. Two of the epitopes mapped to turns or loops on the surface of the model structure. The other two epitopes mapped to the β-sheet region, homologous to the catalytic site of PL. This region of Jun a 1 is highly conserved in the group 1 allergens from other cedar trees as well as microbial PLs. The finding that two out of three major IgE epitopes map to highly conserved catalytic regions of group 1 cedar allergens may help to explain the high degree of cross-reactivity between cedar pollen allergens and might represent a pattern of reactivity common to other allergens with catalytic activity.
AB - Resolution of the 3D structures and IgE epitopes of allergens may identify common or conserved features of allergens. Jun a 1, the predominant allergen in mountain cedar pollen, was chosen as a model for identifying common structural and functional features among a group of plant allergens. In this study, synthetic, overlapping peptides of Jun a 1 and sera from patients allergic to mountain cedar pollen were used to identify linear epitopes. A 3D model of Jun a 1 was produced using the Bacillus subtiles pectate lyase (PL) as a template and validated with biophysical measurements. This allowed mappings of four IgE binding sites on Jun a 1. Two of the epitopes mapped to turns or loops on the surface of the model structure. The other two epitopes mapped to the β-sheet region, homologous to the catalytic site of PL. This region of Jun a 1 is highly conserved in the group 1 allergens from other cedar trees as well as microbial PLs. The finding that two out of three major IgE epitopes map to highly conserved catalytic regions of group 1 cedar allergens may help to explain the high degree of cross-reactivity between cedar pollen allergens and might represent a pattern of reactivity common to other allergens with catalytic activity.
KW - Allergen structure
KW - Cedar pollen hypersensitivity
KW - Cry j 1
KW - IgE epitope
KW - Jun a 1
KW - Juniperus ashei
KW - Mountain cedar
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U2 - 10.1016/S0161-5890(03)00168-8
DO - 10.1016/S0161-5890(03)00168-8
M3 - Article
C2 - 14563374
AN - SCOPUS:0141953202
SN - 0161-5890
VL - 40
SP - 555
EP - 562
JO - Molecular Immunology
JF - Molecular Immunology
IS - 8
ER -