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Dokl Biochem Biophys. 2018 Jan;478(1):34-36. doi: 10.1134/S160767291801009X. Epub 2018 Mar 14.
The Development and Inmmunochemical Properties of the Dimer of Immunoglobulin A Specific to the Influenza Virus A Hemagglutinin.
Aliev TK1, Dement'eva IG2, Toporova VA2, Argentova VV3, Pozdnyakova LP2, Bokov MN2, Dolgikh DA3,4, Sveshnikov PG2, Kirpichnikov MP3,4.
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Abstract
We obtained dimeric forms of IgA1- and IgA2m1-isotypes of FI6 antibody broadly specific to hemagglutinins of different subtypes of influenza A virus. It was shown that the dimers of IgA1 isotype are characterized by a higher antigen-binding activity compared to the IgA2m1 dimers. The affinity of IgA1 dimers to the strains of the H1N1 subtype is higher than that of the H3N2 subtype, which correlates with the properties of the parental human FI6 antibody.
PMID: 29536306 DOI: 10.1134/S160767291801009X
The Development and Inmmunochemical Properties of the Dimer of Immunoglobulin A Specific to the Influenza Virus A Hemagglutinin.
Aliev TK1, Dement'eva IG2, Toporova VA2, Argentova VV3, Pozdnyakova LP2, Bokov MN2, Dolgikh DA3,4, Sveshnikov PG2, Kirpichnikov MP3,4.
Author information
Abstract
We obtained dimeric forms of IgA1- and IgA2m1-isotypes of FI6 antibody broadly specific to hemagglutinins of different subtypes of influenza A virus. It was shown that the dimers of IgA1 isotype are characterized by a higher antigen-binding activity compared to the IgA2m1 dimers. The affinity of IgA1 dimers to the strains of the H1N1 subtype is higher than that of the H3N2 subtype, which correlates with the properties of the parental human FI6 antibody.
PMID: 29536306 DOI: 10.1134/S160767291801009X