Induction of IgE antibodies in mice with recombinant grass pollen antigens

In this study, recombinant Poa pratensis (Poa p) IX allergens were examined for their in vivo allergenicity and antigenicity. Immunization of mice with a fusion protein (FP) comprising beta-galactosidase and recombinant KBG8.3 (rKBG8.3) allergen induced high titres of both IgG and IgE antibodies. By...

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Veröffentlicht in:Immunology 1992-05, Vol.76 (1), p.158-163
Hauptverfasser: ZHANG, L, SEHON, A. H, MOHAPATRA, S. S
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SEHON, A. H
MOHAPATRA, S. S
description In this study, recombinant Poa pratensis (Poa p) IX allergens were examined for their in vivo allergenicity and antigenicity. Immunization of mice with a fusion protein (FP) comprising beta-galactosidase and recombinant KBG8.3 (rKBG8.3) allergen induced high titres of both IgG and IgE antibodies. By contrast, immunization with rKBG60.2, which represents the N-terminal fragment of rKBG8.3, induced only IgG antibodies. The IgE antibody titre specific to Kentucky Bluegrass (KBG) was significantly higher than that to beta-galactosidase. Moreover, KBG-specific IgE antibodies showed no apparent decrease in their titres until 60 days after immunization, whereas the beta-galactosidase-specific IgE antibodies disappeared after 40 days. The antibodies induced with rKBG8.3 in mice were capable of inhibiting the binding of human IgE antibodies to KBG pollen allergens, which indicated that rKBG8.3-specific murine antibodies recognized epitopes similar to those recognized by human IgE antibodies. Analysis of allergenic cross-reactivities of rKBG8.3 with components from five other species of grass pollens revealed that IgE antibodies induced by this allergen are capable of binding in vivo to components from other grass pollens. These results suggest that the mouse may serve as a model for the manipulation of IgE responses to recombinant allergens or their chemically modified derivatives.
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H ; MOHAPATRA, S. S</creator><creatorcontrib>ZHANG, L ; SEHON, A. H ; MOHAPATRA, S. S</creatorcontrib><description>In this study, recombinant Poa pratensis (Poa p) IX allergens were examined for their in vivo allergenicity and antigenicity. Immunization of mice with a fusion protein (FP) comprising beta-galactosidase and recombinant KBG8.3 (rKBG8.3) allergen induced high titres of both IgG and IgE antibodies. By contrast, immunization with rKBG60.2, which represents the N-terminal fragment of rKBG8.3, induced only IgG antibodies. The IgE antibody titre specific to Kentucky Bluegrass (KBG) was significantly higher than that to beta-galactosidase. Moreover, KBG-specific IgE antibodies showed no apparent decrease in their titres until 60 days after immunization, whereas the beta-galactosidase-specific IgE antibodies disappeared after 40 days. The antibodies induced with rKBG8.3 in mice were capable of inhibiting the binding of human IgE antibodies to KBG pollen allergens, which indicated that rKBG8.3-specific murine antibodies recognized epitopes similar to those recognized by human IgE antibodies. Analysis of allergenic cross-reactivities of rKBG8.3 with components from five other species of grass pollens revealed that IgE antibodies induced by this allergen are capable of binding in vivo to components from other grass pollens. 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H</creatorcontrib><creatorcontrib>MOHAPATRA, S. S</creatorcontrib><title>Induction of IgE antibodies in mice with recombinant grass pollen antigens</title><title>Immunology</title><addtitle>Immunology</addtitle><description>In this study, recombinant Poa pratensis (Poa p) IX allergens were examined for their in vivo allergenicity and antigenicity. Immunization of mice with a fusion protein (FP) comprising beta-galactosidase and recombinant KBG8.3 (rKBG8.3) allergen induced high titres of both IgG and IgE antibodies. By contrast, immunization with rKBG60.2, which represents the N-terminal fragment of rKBG8.3, induced only IgG antibodies. The IgE antibody titre specific to Kentucky Bluegrass (KBG) was significantly higher than that to beta-galactosidase. Moreover, KBG-specific IgE antibodies showed no apparent decrease in their titres until 60 days after immunization, whereas the beta-galactosidase-specific IgE antibodies disappeared after 40 days. The antibodies induced with rKBG8.3 in mice were capable of inhibiting the binding of human IgE antibodies to KBG pollen allergens, which indicated that rKBG8.3-specific murine antibodies recognized epitopes similar to those recognized by human IgE antibodies. Analysis of allergenic cross-reactivities of rKBG8.3 with components from five other species of grass pollens revealed that IgE antibodies induced by this allergen are capable of binding in vivo to components from other grass pollens. 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Anaphylaxis, etc</topic><topic>Immunobiology</topic><topic>Immunoglobulin E - biosynthesis</topic><topic>Immunoglobulin G - biosynthesis</topic><topic>Mice</topic><topic>Mice, Inbred Strains</topic><topic>Poa pratensis</topic><topic>Pollen - immunology</topic><topic>Recombinant Proteins - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ZHANG, L</creatorcontrib><creatorcontrib>SEHON, A. H</creatorcontrib><creatorcontrib>MOHAPATRA, S. 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S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Induction of IgE antibodies in mice with recombinant grass pollen antigens</atitle><jtitle>Immunology</jtitle><addtitle>Immunology</addtitle><date>1992-05-01</date><risdate>1992</risdate><volume>76</volume><issue>1</issue><spage>158</spage><epage>163</epage><pages>158-163</pages><issn>0019-2805</issn><eissn>1365-2567</eissn><coden>IMMUAM</coden><abstract>In this study, recombinant Poa pratensis (Poa p) IX allergens were examined for their in vivo allergenicity and antigenicity. Immunization of mice with a fusion protein (FP) comprising beta-galactosidase and recombinant KBG8.3 (rKBG8.3) allergen induced high titres of both IgG and IgE antibodies. By contrast, immunization with rKBG60.2, which represents the N-terminal fragment of rKBG8.3, induced only IgG antibodies. The IgE antibody titre specific to Kentucky Bluegrass (KBG) was significantly higher than that to beta-galactosidase. Moreover, KBG-specific IgE antibodies showed no apparent decrease in their titres until 60 days after immunization, whereas the beta-galactosidase-specific IgE antibodies disappeared after 40 days. The antibodies induced with rKBG8.3 in mice were capable of inhibiting the binding of human IgE antibodies to KBG pollen allergens, which indicated that rKBG8.3-specific murine antibodies recognized epitopes similar to those recognized by human IgE antibodies. Analysis of allergenic cross-reactivities of rKBG8.3 with components from five other species of grass pollens revealed that IgE antibodies induced by this allergen are capable of binding in vivo to components from other grass pollens. These results suggest that the mouse may serve as a model for the manipulation of IgE responses to recombinant allergens or their chemically modified derivatives.</abstract><cop>Oxford</cop><pub>Blackwell</pub><pmid>1628894</pmid><tpages>6</tpages></addata></record>
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subjects Allergens - immunology
Animals
beta-Galactosidase - immunology
Binding, Competitive - immunology
Biological and medical sciences
Blotting, Western
Cross Reactions - immunology
Female
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Immediate hypersensitivity. Allergy. Anaphylaxis, etc
Immunobiology
Immunoglobulin E - biosynthesis
Immunoglobulin G - biosynthesis
Mice
Mice, Inbred Strains
Poa pratensis
Pollen - immunology
Recombinant Proteins - immunology
title Induction of IgE antibodies in mice with recombinant grass pollen antigens
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