Lol p XI, a new major grass pollen allergen, is a member of a family of soybean trypsin inhibitor-related proteins Ronald van Ree, PhDa, Donald R. Hoffman,

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Lol p XI, a new major grass pollen allergen, is a member of a family of soybean trypsin inhibitor-related proteins Ronald van Ree, PhDa, Donald R. Hoffman, PhDb, Willem van Dijk, PhDc, Virginie Brodard, MScd, Karin Mahieu, MSca, Carolien A.M. Koeleman, BScc, Marjolein Grande, MSca, W.Astrid van Leeuwen, BSca, Rob C. Aalberse, PhDa Journal of Allergy and Clinical Immunology Volume 95, Issue 5, Pages 970-978 (May 1995) DOI: 10.1016/S0091-6749(95)70097-8 Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 1 Two-dimensional analysis of Lol p XI (silver stained). Left, Two-dimensional separation of 10 μg of Lol p XI; right, two-dimensional separation of 36 μg of total Lol p extract. Lanes at far left and far right contain molecular weight markers (14.4, 20.1, 30.0, 43.0, 67.0, and 94.0 kd). Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 2 A and B Amino acid sequence analysis of Lol p XI. A, Complete amino acid sequence of Lol p XI (shaded area) contains 134 amino acids. Position 24 is N-linked glycosylation site, position 103 (X) represents atypical residue. Amino acid at this position is not a hydroxyproline, phosphoserine, phosphotyrosine, or a carbohydrate-modified asparagine. Under the complete sequence all separate peptides obtained with four different enzymes are shown. Some peptides were longer than could be sequenced (indicated by +). Some residues could not be identified in some peptides (indicated by U). Peptide starting with amino acid 61 obtained after chymotrypsin digestion continues in second half of figure (arrows). B, Complete sequence of Lol p XI was aligned for maximum homology with Ole e I.24 In the latter one insertion (–) was made to obtain maximum homology. Boxes were drawn around identical and similar residues. The following groups of amino acids were regarded similar: (V,I,L), (T,S), (D,E), (K,R), (N,Q), and (F,Y). Conserved positions of six cysteines are in shaded regions. C, Alignment for maximum homology of Lol p XI and amino acids 30 to 162 of maize pollen protein Zmc1325 and 22 to 154 of tomato pollen protein LAT52.26 One insertion (-) was made in sequences of Zmc13 and LAT52. D, Figure shows 108–amino-acid overlap of Lol p XI (1 to 108) with SBTI (72 to 181). For maximum homology, insertions were made in both sequences. Active site of SBTI is not included in overlap (63 and 64) and is not present in Lol p XI. (Sequence was submitted to Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, 3900 Reservoir Rd., N.W., Washington, DC 20007; accession No. A54002.) Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 2 A and B Amino acid sequence analysis of Lol p XI. A, Complete amino acid sequence of Lol p XI (shaded area) contains 134 amino acids. Position 24 is N-linked glycosylation site, position 103 (X) represents atypical residue. Amino acid at this position is not a hydroxyproline, phosphoserine, phosphotyrosine, or a carbohydrate-modified asparagine. Under the complete sequence all separate peptides obtained with four different enzymes are shown. Some peptides were longer than could be sequenced (indicated by +). Some residues could not be identified in some peptides (indicated by U). Peptide starting with amino acid 61 obtained after chymotrypsin digestion continues in second half of figure (arrows). B, Complete sequence of Lol p XI was aligned for maximum homology with Ole e I.24 In the latter one insertion (–) was made to obtain maximum homology. Boxes were drawn around identical and similar residues. The following groups of amino acids were regarded similar: (V,I,L), (T,S), (D,E), (K,R), (N,Q), and (F,Y). Conserved positions of six cysteines are in shaded regions. C, Alignment for maximum homology of Lol p XI and amino acids 30 to 162 of maize pollen protein Zmc1325 and 22 to 154 of tomato pollen protein LAT52.26 One insertion (-) was made in sequences of Zmc13 and LAT52. D, Figure shows 108–amino-acid overlap of Lol p XI (1 to 108) with SBTI (72 to 181). For maximum homology, insertions were made in both sequences. Active site of SBTI is not included in overlap (63 and 64) and is not present in Lol p XI. (Sequence was submitted to Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, 3900 Reservoir Rd., N.W., Washington, DC 20007; accession No. A54002.) Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 2 A and B Amino acid sequence analysis of Lol p XI. A, Complete amino acid sequence of Lol p XI (shaded area) contains 134 amino acids. Position 24 is N-linked glycosylation site, position 103 (X) represents atypical residue. Amino acid at this position is not a hydroxyproline, phosphoserine, phosphotyrosine, or a carbohydrate-modified asparagine. Under the complete sequence all separate peptides obtained with four different enzymes are shown. Some peptides were longer than could be sequenced (indicated by +). Some residues could not be identified in some peptides (indicated by U). Peptide starting with amino acid 61 obtained after chymotrypsin digestion continues in second half of figure (arrows). B, Complete sequence of Lol p XI was aligned for maximum homology with Ole e I.24 In the latter one insertion (–) was made to obtain maximum homology. Boxes were drawn around identical and similar residues. The following groups of amino acids were regarded similar: (V,I,L), (T,S), (D,E), (K,R), (N,Q), and (F,Y). Conserved positions of six cysteines are in shaded regions. C, Alignment for maximum homology of Lol p XI and amino acids 30 to 162 of maize pollen protein Zmc1325 and 22 to 154 of tomato pollen protein LAT52.26 One insertion (-) was made in sequences of Zmc13 and LAT52. D, Figure shows 108–amino-acid overlap of Lol p XI (1 to 108) with SBTI (72 to 181). For maximum homology, insertions were made in both sequences. Active site of SBTI is not included in overlap (63 and 64) and is not present in Lol p XI. (Sequence was submitted to Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, 3900 Reservoir Rd., N.W., Washington, DC 20007; accession No. A54002.) Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 2 A and B Amino acid sequence analysis of Lol p XI. A, Complete amino acid sequence of Lol p XI (shaded area) contains 134 amino acids. Position 24 is N-linked glycosylation site, position 103 (X) represents atypical residue. Amino acid at this position is not a hydroxyproline, phosphoserine, phosphotyrosine, or a carbohydrate-modified asparagine. Under the complete sequence all separate peptides obtained with four different enzymes are shown. Some peptides were longer than could be sequenced (indicated by +). Some residues could not be identified in some peptides (indicated by U). Peptide starting with amino acid 61 obtained after chymotrypsin digestion continues in second half of figure (arrows). B, Complete sequence of Lol p XI was aligned for maximum homology with Ole e I.24 In the latter one insertion (–) was made to obtain maximum homology. Boxes were drawn around identical and similar residues. The following groups of amino acids were regarded similar: (V,I,L), (T,S), (D,E), (K,R), (N,Q), and (F,Y). Conserved positions of six cysteines are in shaded regions. C, Alignment for maximum homology of Lol p XI and amino acids 30 to 162 of maize pollen protein Zmc1325 and 22 to 154 of tomato pollen protein LAT52.26 One insertion (-) was made in sequences of Zmc13 and LAT52. D, Figure shows 108–amino-acid overlap of Lol p XI (1 to 108) with SBTI (72 to 181). For maximum homology, insertions were made in both sequences. Active site of SBTI is not included in overlap (63 and 64) and is not present in Lol p XI. (Sequence was submitted to Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, 3900 Reservoir Rd., N.W., Washington, DC 20007; accession No. A54002.) Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 3 Proteinase K and TFMS treatment. A, Influence of proteinase K treatment on binding of mAbs 2H4 (antipeptide) and Dp6 (anticarbohydrate) to Lol p XI. Results are expressed as percentage of uninhibited value. B, Influence of TFMS treatment on binding of mAbs 2H4 and Dp6 to Lol p XI. C and D, Influence of proteinase K (C) and of TFMS (D) treatment on binding of IgE from serum with predominantly anticarbohydrate IgE activity (pf138) and from serum with predominantly antipeptide activity (pf126). Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 3 Proteinase K and TFMS treatment. A, Influence of proteinase K treatment on binding of mAbs 2H4 (antipeptide) and Dp6 (anticarbohydrate) to Lol p XI. Results are expressed as percentage of uninhibited value. B, Influence of TFMS treatment on binding of mAbs 2H4 and Dp6 to Lol p XI. C and D, Influence of proteinase K (C) and of TFMS (D) treatment on binding of IgE from serum with predominantly anticarbohydrate IgE activity (pf138) and from serum with predominantly antipeptide activity (pf126). Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 3 Proteinase K and TFMS treatment. A, Influence of proteinase K treatment on binding of mAbs 2H4 (antipeptide) and Dp6 (anticarbohydrate) to Lol p XI. Results are expressed as percentage of uninhibited value. B, Influence of TFMS treatment on binding of mAbs 2H4 and Dp6 to Lol p XI. C and D, Influence of proteinase K (C) and of TFMS (D) treatment on binding of IgE from serum with predominantly anticarbohydrate IgE activity (pf138) and from serum with predominantly antipeptide activity (pf126). Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 3 Proteinase K and TFMS treatment. A, Influence of proteinase K treatment on binding of mAbs 2H4 (antipeptide) and Dp6 (anticarbohydrate) to Lol p XI. Results are expressed as percentage of uninhibited value. B, Influence of TFMS treatment on binding of mAbs 2H4 and Dp6 to Lol p XI. C and D, Influence of proteinase K (C) and of TFMS (D) treatment on binding of IgE from serum with predominantly anticarbohydrate IgE activity (pf138) and from serum with predominantly antipeptide activity (pf126). Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions

FIG. 4 Anticarbohydrate IgE in Lol p XI–positive sera. RAST results are expressed as percentage binding of total [125I] anti-IgE added. Journal of Allergy and Clinical Immunology 1995 95, 970-978DOI: (10.1016/S0091-6749(95)70097-8) Copyright © 1995 Mosby, Inc. Terms and Conditions