Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study
One of the purposes of specific immunotherapy (SIT) is to modulate humoral immune response against allergens with significant increases in allergen-specific IgG levels, commonly associated with blocking activity. The present study investigated in vitro blocking activity of allergen-specific IgG anti...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2013-01-01
|
| Series: | Clinical and Developmental Immunology |
| Online Access: | http://dx.doi.org/10.1155/2013/657424 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849473471871975424 |
|---|---|
| author | Isabella Lima Siman Lais Martins de Aquino Leandro Hideki Ynoue Juliana Silva Miranda Ana Claudia Arantes Marquez Pajuaba Jair Pereira Cunha-Júnior Deise Aparecida Oliveira Silva Ernesto Akio Taketomi |
| author_facet | Isabella Lima Siman Lais Martins de Aquino Leandro Hideki Ynoue Juliana Silva Miranda Ana Claudia Arantes Marquez Pajuaba Jair Pereira Cunha-Júnior Deise Aparecida Oliveira Silva Ernesto Akio Taketomi |
| author_sort | Isabella Lima Siman |
| collection | DOAJ |
| description | One of the purposes of specific immunotherapy (SIT) is to modulate humoral immune response against allergens with significant increases in allergen-specific IgG levels, commonly associated with blocking activity. The present study investigated in vitro blocking activity of allergen-specific IgG antibodies on IgE reactivity to Dermatophagoides pteronyssinus (Dpt) in sera from atopic patients. Dpt-specific IgG antibodies were purified by ammonium sulfate precipitation followed by protein-G affinity chromatography. Purity was checked by SDS-PAGE and immunoreactivity by slot-blot and immunoblot assays. The blocking activity was evaluated by inhibition ELISA. The electrophoretic profile of the ammonium sulfate precipitated fraction showed strongly stained bands in ligand fraction after chromatography, compatible with molecular weight of human whole IgG molecule. The purity degree was confirmed by detecting strong immunoreactivity to IgG, negligible to IgA, and no reactivity to IgE and IgM. Dpt-specific IgG fraction was capable of significantly reducing levels of IgE anti-Dpt, resulting in 35%–51% inhibition of IgE reactivity to Dpt in atopic patients sera. This study showed that allergen-specific IgG antibodies purified from mite-allergic patients sera block the IgE recognition of Dermatophagoides pteronyssinus antigens. This approach reinforces that intermittent measurement of serum allergen-specific IgG antibodies will be an important objective laboratorial parameter that will help specialists to follow their patients under SIT. |
| format | Article |
| id | doaj-art-d2bc69c9889b4c3b8cd947cd550a1add |
| institution | Kabale University |
| issn | 1740-2522 1740-2530 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Clinical and Developmental Immunology |
| spelling | doaj-art-d2bc69c9889b4c3b8cd947cd550a1add2025-08-20T03:24:07ZengWileyClinical and Developmental Immunology1740-25221740-25302013-01-01201310.1155/2013/657424657424Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro StudyIsabella Lima Siman0Lais Martins de Aquino1Leandro Hideki Ynoue2Juliana Silva Miranda3Ana Claudia Arantes Marquez Pajuaba4Jair Pereira Cunha-Júnior5Deise Aparecida Oliveira Silva6Ernesto Akio Taketomi7Laboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilLaboratory of Allergy and Clinical Immunology, Institute of Biomedical Sciences, Federal University of Uberlândia, Avenida Pará 1720, Bloco 4 C, Campus Umuarama, 38400-902 Uberlândia, MG, BrazilOne of the purposes of specific immunotherapy (SIT) is to modulate humoral immune response against allergens with significant increases in allergen-specific IgG levels, commonly associated with blocking activity. The present study investigated in vitro blocking activity of allergen-specific IgG antibodies on IgE reactivity to Dermatophagoides pteronyssinus (Dpt) in sera from atopic patients. Dpt-specific IgG antibodies were purified by ammonium sulfate precipitation followed by protein-G affinity chromatography. Purity was checked by SDS-PAGE and immunoreactivity by slot-blot and immunoblot assays. The blocking activity was evaluated by inhibition ELISA. The electrophoretic profile of the ammonium sulfate precipitated fraction showed strongly stained bands in ligand fraction after chromatography, compatible with molecular weight of human whole IgG molecule. The purity degree was confirmed by detecting strong immunoreactivity to IgG, negligible to IgA, and no reactivity to IgE and IgM. Dpt-specific IgG fraction was capable of significantly reducing levels of IgE anti-Dpt, resulting in 35%–51% inhibition of IgE reactivity to Dpt in atopic patients sera. This study showed that allergen-specific IgG antibodies purified from mite-allergic patients sera block the IgE recognition of Dermatophagoides pteronyssinus antigens. This approach reinforces that intermittent measurement of serum allergen-specific IgG antibodies will be an important objective laboratorial parameter that will help specialists to follow their patients under SIT.http://dx.doi.org/10.1155/2013/657424 |
| spellingShingle | Isabella Lima Siman Lais Martins de Aquino Leandro Hideki Ynoue Juliana Silva Miranda Ana Claudia Arantes Marquez Pajuaba Jair Pereira Cunha-Júnior Deise Aparecida Oliveira Silva Ernesto Akio Taketomi Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study Clinical and Developmental Immunology |
| title | Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study |
| title_full | Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study |
| title_fullStr | Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study |
| title_full_unstemmed | Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study |
| title_short | Allergen-Specific IgG Antibodies Purified from Mite-Allergic Patients Sera Block the IgE Recognition of Dermatophagoides pteronyssinus Antigens: An In Vitro Study |
| title_sort | allergen specific igg antibodies purified from mite allergic patients sera block the ige recognition of dermatophagoides pteronyssinus antigens an in vitro study |
| url | http://dx.doi.org/10.1155/2013/657424 |
| work_keys_str_mv | AT isabellalimasiman allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT laismartinsdeaquino allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT leandrohidekiynoue allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT julianasilvamiranda allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT anaclaudiaarantesmarquezpajuaba allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT jairpereiracunhajunior allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT deiseaparecidaoliveirasilva allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy AT ernestoakiotaketomi allergenspecificiggantibodiespurifiedfrommiteallergicpatientsserablocktheigerecognitionofdermatophagoidespteronyssinusantigensaninvitrostudy |