Phl p 2: Difference between revisions

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In this experiment it was determined that IgE antibodies bound to <scene name='Phl_p_2/Phl_p_2/5'>Phl p 2</scene>, a grass pollen allergen, in allergic patients rather than IgG antibodies. This was strange because both antibodies are capable of specifically binding Phl p 2 however IgE antibodies are the least abundant in mammalian immune systems whereas IgG antibodies are one of the most abundant. Researchers predicted that the epitope specific heavy chain of the IgE antibody bound to a different epitope on the pollen than did the IgG antibody and that the IgE epitope had a much higher affinity for the antigen than the IgG antibody. To test this hypothesis, researchers took the constant region of an IgG antibody (Fc receptor) and paired it when the variable region of the allergen specific IgE epitope (Fab region). Researchers then termed this new antibody huMab2 which had the IgE Fab region and the IgG Fc region. The huMab2 antibody had a new <scene name='Phl_p_2/Heavy_chain/3'>heavy chain</scene> and a new <scene name='Phl_p_2/Light_chain/2'>light chain</scene>. It was important for researchers to keep the Fc region of the IgG antibody because the Fc region does not bind mast cells to cause degranulation and allergic reaction when exposed to Phlp2 antigen.

In this experiment it was determined that IgE antibodies bound to <scene name='Phl_p_2/Phl_p_2/5'>Phl p 2</scene>, a grass pollen allergen, in allergic patients rather than IgG antibodies.<ref>PMID:19201867</ref> This was strange because both antibodies are capable of specifically binding Phl p 2 however IgE antibodies are the least abundant in mammalian immune systems whereas IgG antibodies are one of the most abundant. Researchers predicted that the epitope specific heavy chain of the IgE antibody bound to a different epitope on the pollen than did the IgG antibody and that the IgE epitope had a much higher affinity for the antigen than the IgG antibody. To test this hypothesis, researchers took the constant region of an IgG antibody (Fc receptor) and paired it when the variable region of the allergen specific IgE epitope (Fab region). Researchers then termed this new antibody huMab2 which had the IgE Fab region and the IgG Fc region. The huMab2 antibody had a new <scene name='Phl_p_2/Heavy_chain/3'>heavy chain</scene> and a new <scene name='Phl_p_2/Light_chain/2'>light chain</scene>. It was important for researchers to keep the Fc region of the IgG antibody because the Fc region does not bind mast cells to cause degranulation and allergic reaction when exposed to Phlp2 antigen.

When huMab2 was mixed in solution with mast cell bound IgE antibodies it actually prevented the binding of Phl p 2 with IgE as the IgG like antibody was more abundant and free floating in solution. This was a significant discovery because this research information can be used and applied to further develop the treatment of type I hypersensitivity patients.

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 <Structure load='2vxq' size='400' frame='true' align='right' caption='Insert caption here' scene='Phl_p_2/Phl_p_2/4' />
-In this experiment it was determined that IgE antibodies bound to <scene name='Phl_p_2/Phl_p_2/5'>Phl p 2</scene>, a grass pollen allergen, in allergic patients rather than IgG antibodies. This was strange because both antibodies are capable of specifically binding Phl p 2 however IgE antibodies are the least abundant in mammalian immune systems whereas IgG antibodies are one of the most abundant. Researchers predicted that the epitope specific heavy chain of the IgE antibody bound to a different epitope on the pollen than did the IgG antibody and that the IgE epitope had a much higher affinity for the antigen than the IgG antibody. To test this hypothesis, researchers took the constant region of an IgG antibody (Fc receptor) and paired it when the variable region of the allergen specific IgE epitope (Fab region). Researchers then termed this new antibody huMab2 which had the IgE Fab region and the IgG Fc region. The huMab2 antibody had a new <scene name='Phl_p_2/Heavy_chain/3'>heavy chain</scene> and a new <scene name='Phl_p_2/Light_chain/2'>light chain</scene>. It was important for researchers to keep the Fc region of the IgG antibody because the Fc region does not bind mast cells to cause degranulation and allergic reaction when exposed to Phlp2 antigen.
+In this experiment it was determined that IgE antibodies bound to <scene name='Phl_p_2/Phl_p_2/5'>Phl p 2</scene>, a grass pollen allergen, in allergic patients rather than IgG antibodies.<ref>PMID:19201867</ref> This was strange because both antibodies are capable of specifically binding Phl p 2 however IgE antibodies are the least abundant in mammalian immune systems whereas IgG antibodies are one of the most abundant. Researchers predicted that the epitope specific heavy chain of the IgE antibody bound to a different epitope on the pollen than did the IgG antibody and that the IgE epitope had a much higher affinity for the antigen than the IgG antibody. To test this hypothesis, researchers took the constant region of an IgG antibody (Fc receptor) and paired it when the variable region of the allergen specific IgE epitope (Fab region). Researchers then termed this new antibody huMab2 which had the IgE Fab region and the IgG Fc region. The huMab2 antibody had a new <scene name='Phl_p_2/Heavy_chain/3'>heavy chain</scene> and a new <scene name='Phl_p_2/Light_chain/2'>light chain</scene>. It was important for researchers to keep the Fc region of the IgG antibody because the Fc region does not bind mast cells to cause degranulation and allergic reaction when exposed to Phlp2 antigen.
 When huMab2 was mixed in solution with mast cell bound IgE antibodies it actually prevented the binding of Phl p 2 with IgE as the IgG like antibody was more abundant and free floating in solution. This was a significant discovery because this research information can be used and applied to further develop the treatment of type I hypersensitivity patients.