Identification of carboxymethyl (CM)-binding proteins derived from Lolium multiflorum pollen extract and antibody reactivity in Brazilian allergic patients
Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim of this study was to investigate antibody reactivity to L. multiflorum crude and carboxymethylligand extracts in allergic patients and healthy...
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Published in | Brazilian journal of medical and biological research Vol. 56; no. 1; p. e12957 |
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Language | English Portuguese |
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Associacao Brasileira de Divulgacao Cientifica (ABDC)
01.01.2023
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Abstract | Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim of this study was to investigate antibody reactivity to L. multiflorum crude and carboxymethylligand extracts in allergic patients and healthy individuals. Ion exchange carboxymethyl (CM) chromatography (CM-Sepharose) was used to isolate proteins (S2) from L. multiflorum crude extract (S1), which were assessed by SDS-PAGE. S1- and S2specific IgE and IgG4 levels were measured by ELISA using sera from 55 atopic and 16 non- atopic subjects. Reactive polypeptide bands in S1 and S2 were detected by immunoblotting, and the most prominent bands in S2 were analyzed by mass spectrometry (MS-MS). Similar IgE and IgG4 levels were observed to both S1 (IgE median absorbance: 1.22; IgG4 median absorbance: 0.68) and S2 (IgE median absorbance: 1.26; IgG4 median absorbance: 0.85) in atopic subjects. S1 and S2 had positive correlations for IgE and IgG4 (IgE: r=0.9567; IgG4: r=0.9229; P<0.0001) levels. Homology between S1 and S2 was confirmed by IgE (84%) and IgG4 (83%) inhibition. Immunoblotting revealed that the 29-32 kDa band was recognized by 100% of atopic subjects in both S1 and S2. MS-MS analysis identified similarity profile to groups 1 and 5 grass allergens. This study revealed thatcarboxymethyl-ligand fraction played an important role for pollen allergy diagnosis by containing clinically relevant allergens and constituted a promising candidate for allergen-specific immunotherapy. Key words: Allergen; Ion-exchange chromatography; Beta-expansin; Lolium multiflorum; IgE; IgG4 |
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AbstractList | Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim of this study was to investigate antibody reactivity to L. multiflorum crude and carboxymethyl-ligand extracts in allergic patients and healthy individuals. Ion exchange carboxymethyl (CM) chromatography (CM-Sepharose) was used to isolate proteins (S2) from L. multiflorum crude extract (S1), which were assessed by SDS-PAGE. S1- and S2-specific IgE and IgG4 levels were measured by ELISA using sera from 55 atopic and 16 non-atopic subjects. Reactive polypeptide bands in S1 and S2 were detected by immunoblotting, and the most prominent bands in S2 were analyzed by mass spectrometry (MS-MS). Similar IgE and IgG4 levels were observed to both S1 (IgE median absorbance: 1.22; IgG4 median absorbance: 0.68) and S2 (IgE median absorbance: 1.26; IgG4 median absorbance: 0.85) in atopic subjects. S1 and S2 had positive correlations for IgE and IgG4 (IgE: r=0.9567; IgG4: r=0.9229; P<0.0001) levels. Homology between S1 and S2 was confirmed by IgE (84%) and IgG4 (83%) inhibition. Immunoblotting revealed that the 29-32 kDa band was recognized by 100% of atopic subjects in both S1 and S2. MS-MS analysis identified similarity profile to groups 1 and 5 grass allergens. This study revealed that carboxymethyl-ligand fraction played an important role for pollen allergy diagnosis by containing clinically relevant allergens and constituted a promising candidate for allergen-specific immunotherapy. Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim of this study was to investigate antibody reactivity to L. multiflorum crude and carboxymethyl-ligand extracts in allergic patients and healthy individuals. Ion exchange carboxymethyl (CM) chromatography (CM-Sepharose) was used to isolate proteins (S2) from L. multiflorum crude extract (S1), which were assessed by SDS-PAGE. S1- and S2-specific IgE and IgG4 levels were measured by ELISA using sera from 55 atopic and 16 non-atopic subjects. Reactive polypeptide bands in S1 and S2 were detected by immunoblotting, and the most prominent bands in S2 were analyzed by mass spectrometry (MS-MS). Similar IgE and IgG4 levels were observed to both S1 (IgE median absorbance: 1.22; IgG4 median absorbance: 0.68) and S2 (IgE median absorbance: 1.26; IgG4 median absorbance: 0.85) in atopic subjects. S1 and S2 had positive correlations for IgE and IgG4 (IgE: r=0.9567; IgG4: r=0.9229; P<0.0001) levels. Homology between S1 and S2 was confirmed by IgE (84%) and IgG4 (83%) inhibition. Immunoblotting revealed that the 29-32 kDa band was recognized by 100% of atopic subjects in both S1 and S2. MS-MS analysis identified similarity profile to groups 1 and 5 grass allergens. This study revealed that carboxymethyl-ligand fraction played an important role for pollen allergy diagnosis by containing clinically relevant allergens and constituted a promising candidate for allergen-specific immunotherapy. Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim of this study was to investigate antibody reactivity to L. multiflorum crude and carboxymethylligand extracts in allergic patients and healthy individuals. Ion exchange carboxymethyl (CM) chromatography (CM-Sepharose) was used to isolate proteins (S2) from L. multiflorum crude extract (S1), which were assessed by SDS-PAGE. S1- and S2specific IgE and IgG4 levels were measured by ELISA using sera from 55 atopic and 16 non- atopic subjects. Reactive polypeptide bands in S1 and S2 were detected by immunoblotting, and the most prominent bands in S2 were analyzed by mass spectrometry (MS-MS). Similar IgE and IgG4 levels were observed to both S1 (IgE median absorbance: 1.22; IgG4 median absorbance: 0.68) and S2 (IgE median absorbance: 1.26; IgG4 median absorbance: 0.85) in atopic subjects. S1 and S2 had positive correlations for IgE and IgG4 (IgE: r=0.9567; IgG4: r=0.9229; P<0.0001) levels. Homology between S1 and S2 was confirmed by IgE (84%) and IgG4 (83%) inhibition. Immunoblotting revealed that the 29-32 kDa band was recognized by 100% of atopic subjects in both S1 and S2. MS-MS analysis identified similarity profile to groups 1 and 5 grass allergens. This study revealed thatcarboxymethyl-ligand fraction played an important role for pollen allergy diagnosis by containing clinically relevant allergens and constituted a promising candidate for allergen-specific immunotherapy. Key words: Allergen; Ion-exchange chromatography; Beta-expansin; Lolium multiflorum; IgE; IgG4 Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim of this study was to investigate antibody reactivity to L. multiflorum crude and carboxymethylligand extracts in allergic patients and healthy individuals. Ion exchange carboxymethyl (CM) chromatography (CM-Sepharose) was used to isolate proteins (S2) from L. multiflorum crude extract (S1), which were assessed by SDS-PAGE. S1- and S2specific IgE and IgG4 levels were measured by ELISA using sera from 55 atopic and 16 non- atopic subjects. Reactive polypeptide bands in S1 and S2 were detected by immunoblotting, and the most prominent bands in S2 were analyzed by mass spectrometry (MS-MS). Similar IgE and IgG4 levels were observed to both S1 (IgE median absorbance: 1.22; IgG4 median absorbance: 0.68) and S2 (IgE median absorbance: 1.26; IgG4 median absorbance: 0.85) in atopic subjects. S1 and S2 had positive correlations for IgE and IgG4 (IgE: r=0.9567; IgG4: r=0.9229; P<0.0001) levels. Homology between S1 and S2 was confirmed by IgE (84%) and IgG4 (83%) inhibition. Immunoblotting revealed that the 29-32 kDa band was recognized by 100% of atopic subjects in both S1 and S2. MS-MS analysis identified similarity profile to groups 1 and 5 grass allergens. This study revealed thatcarboxymethyl-ligand fraction played an important role for pollen allergy diagnosis by containing clinically relevant allergens and constituted a promising candidate for allergen-specific immunotherapy. |
Audience | Academic |
Author | Resende, R.O Correa, A.S Taketomi, E.A Moreira, P.F.S Cunha, J.P., Jr Miranda, J.S Oliveira, L.A.R Vieira, F.A.M |
AuthorAffiliation | Universidade de Caxias do Sul Instituto Oswaldo Cruz, Fiocruz Universidade Federal de Uberlândia |
AuthorAffiliation_xml | – name: Universidade de Caxias do Sul – name: Instituto Oswaldo Cruz, Fiocruz – name: Universidade Federal de Uberlândia |
Author_xml | – sequence: 1 fullname: Correa, A.S – sequence: 2 fullname: Miranda, J.S – sequence: 3 fullname: Oliveira, L.A.R – sequence: 4 fullname: Moreira, P.F.S – sequence: 5 fullname: Vieira, F.A.M – sequence: 6 fullname: Cunha, J.P., Jr – sequence: 7 fullname: Resende, R.O – sequence: 8 fullname: Taketomi, E.A |
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Cites_doi | 10.1016/0003-2697(76)90527-3 10.1111/j.1467-7652.2011.00654.x 10.1016/j.jaci.2018.09.039 10.1016/S1808-8694(15)31005-3 10.1016/j.ebiom.2019.11.006 10.1111/cea.12317 10.1007/s12016-018-8712-1 10.1172/JCI119330 10.1016/j.aller.2015.03.001 10.1590/S0100-879X2010005000004 10.1007/s00709-006-0176-0 10.1159/000464104 10.1016/S0031-3955(16)36544-0 10.1016/S1808-8694(15)31262-3 10.1371/journal.pone.0128402 10.1016/0021-8707(62)90067-9 10.7748/ns.2016.e9220 10.1073/pnas.76.9.4350 10.1002/pmic.200401038 10.1038/227680a0 10.1111/all.13210 10.1046/j.1432-1327.1999.00462.x 10.1104/pp.103.020024 10.1155/2019/9840890 10.1159/000092531 10.1016/j.imlet.2017.04.015 10.1016/j.pop.2016.04.009 10.1111/all.12696 10.1016/j.arbr.2018.12.020 10.1186/s12948-019-0110-6 10.1016/j.homp.2015.12.063 10.29328/journal.aaai.1001024 10.1159/000321821 10.1016/j.molimm.2018.03.012 10.1016/j.molimm.2008.08.267 10.1001/archopht.1990.01070030090035 |
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Keywords | IgG4 Beta-expansin Ion-exchange chromatography Lolium multiflorum IgE Allergen |
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Snippet | Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim... Lolium multiflorum grass is the major pollen allergen source in the southern region of Brazil, but most of its allergens remain poorly characterized. The aim... |
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SubjectTerms | Allergen Antigen-antibody reactions Beta-expansin Binding proteins BIOLOGY Care and treatment Grasses Hay-fever Health aspects IgE IgG4 Immunological research Immunotherapy Ion-exchange chromatography Lolium multiflorum Materia medica, Vegetable MEDICINE, RESEARCH & EXPERIMENTAL Methods Plant extracts Pollen |
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Title | Identification of carboxymethyl (CM)-binding proteins derived from Lolium multiflorum pollen extract and antibody reactivity in Brazilian allergic patients |
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