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Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure

We have discovered an Aleuria Aurantia Lectin (AAL)-reactive immunoglobulin G (IgG) that naturally occurs in the circulation of rabbits and mice, following immune responses induced by various foreign antigens. AAL can specifically bind to fucose moieties on glycoproteins. However, most serum IgGs ar...

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Autores principales: Chen, Songming, Lu, Chen, Gu, Hongbo, Mehta, Anand, Li, Jianwei, Romano, Patrick B., Horn, David, Hooper, D. Craig, Bazemore-Walker, Carthene R., Block, Timothy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3443102/
https://www.ncbi.nlm.nih.gov/pubmed/23024749
http://dx.doi.org/10.1371/journal.pone.0044422
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author Chen, Songming
Lu, Chen
Gu, Hongbo
Mehta, Anand
Li, Jianwei
Romano, Patrick B.
Horn, David
Hooper, D. Craig
Bazemore-Walker, Carthene R.
Block, Timothy
author_facet Chen, Songming
Lu, Chen
Gu, Hongbo
Mehta, Anand
Li, Jianwei
Romano, Patrick B.
Horn, David
Hooper, D. Craig
Bazemore-Walker, Carthene R.
Block, Timothy
author_sort Chen, Songming
collection PubMed
description We have discovered an Aleuria Aurantia Lectin (AAL)-reactive immunoglobulin G (IgG) that naturally occurs in the circulation of rabbits and mice, following immune responses induced by various foreign antigens. AAL can specifically bind to fucose moieties on glycoproteins. However, most serum IgGs are poorly bound by AAL unless they are denatured or treated with glycosidase. In this study, using an immunogen-independent AAL-antibody microarray assay that we developed, we detected AAL-reactive IgG in the sera of all animals that had been immunized 1–2 weeks previously with various immunogens with and without adjuvants and developed immunogen-specific responses. All of these animals subsequently developed immunogen-specific immune responses. The kinetics of the production of AAL-reactive IgG in mice and rabbits were distinct from those of the immunogen-specific IgGs elicited in the same animals: they rose and fell within one to two weeks, and peaked between four to seven days after exposure, while immunogen-specific IgGs continued to rise during the same period. Mass spectrometric profiling of the Fc glycoforms of purified AAL-reactive IgGs indicates that these are mainly comprised of IgGs with core-fucosylated and either mono-or non-galactosylated Fc N-glycan structures. Our results suggest that AAL-reactive IgG could be a previously unrecognized IgG subset that is selectively produced at the onset of a humoral response.
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spelling pubmed-34431022012-09-28 Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure Chen, Songming Lu, Chen Gu, Hongbo Mehta, Anand Li, Jianwei Romano, Patrick B. Horn, David Hooper, D. Craig Bazemore-Walker, Carthene R. Block, Timothy PLoS One Research Article We have discovered an Aleuria Aurantia Lectin (AAL)-reactive immunoglobulin G (IgG) that naturally occurs in the circulation of rabbits and mice, following immune responses induced by various foreign antigens. AAL can specifically bind to fucose moieties on glycoproteins. However, most serum IgGs are poorly bound by AAL unless they are denatured or treated with glycosidase. In this study, using an immunogen-independent AAL-antibody microarray assay that we developed, we detected AAL-reactive IgG in the sera of all animals that had been immunized 1–2 weeks previously with various immunogens with and without adjuvants and developed immunogen-specific responses. All of these animals subsequently developed immunogen-specific immune responses. The kinetics of the production of AAL-reactive IgG in mice and rabbits were distinct from those of the immunogen-specific IgGs elicited in the same animals: they rose and fell within one to two weeks, and peaked between four to seven days after exposure, while immunogen-specific IgGs continued to rise during the same period. Mass spectrometric profiling of the Fc glycoforms of purified AAL-reactive IgGs indicates that these are mainly comprised of IgGs with core-fucosylated and either mono-or non-galactosylated Fc N-glycan structures. Our results suggest that AAL-reactive IgG could be a previously unrecognized IgG subset that is selectively produced at the onset of a humoral response. Public Library of Science 2012-09-14 /pmc/articles/PMC3443102/ /pubmed/23024749 http://dx.doi.org/10.1371/journal.pone.0044422 Text en © 2012 Chen et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Chen, Songming
Lu, Chen
Gu, Hongbo
Mehta, Anand
Li, Jianwei
Romano, Patrick B.
Horn, David
Hooper, D. Craig
Bazemore-Walker, Carthene R.
Block, Timothy
Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure
title Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure
title_full Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure
title_fullStr Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure
title_full_unstemmed Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure
title_short Aleuria Aurantia Lectin (AAL)-Reactive Immunoglobulin G Rapidly Appears in Sera of Animals following Antigen Exposure
title_sort aleuria aurantia lectin (aal)-reactive immunoglobulin g rapidly appears in sera of animals following antigen exposure
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3443102/
https://www.ncbi.nlm.nih.gov/pubmed/23024749
http://dx.doi.org/10.1371/journal.pone.0044422
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