Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity
Abstract The bat immune system features multiple unique properties such as dampened inflammatory responses and increased tissue protection, explaining their long lifespan and tolerance to viral infections. Here, we demonstrated that body temperature fluctuations corresponding to different physiologi...
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ftdoajarticles:oai:doaj.org/article:13f32342da5a482e90b688394328e434 2024-09-15T18:27:24+00:00 Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity Nia Toshkova Violeta Zhelyzkova Alejandra Reyes-Ruiz Eline Haerens Marina de Castro Deus Robin V. Lacombe Maxime Lecerf Gaelle Gonzalez Nolwenn Jouvenet Cyril Planchais Jordan D. Dimitrov 2024-07-01T00:00:00Z https://doi.org/10.1038/s41467-024-50316-x https://doaj.org/article/13f32342da5a482e90b688394328e434 EN eng Nature Portfolio https://doi.org/10.1038/s41467-024-50316-x https://doaj.org/toc/2041-1723 doi:10.1038/s41467-024-50316-x 2041-1723 https://doaj.org/article/13f32342da5a482e90b688394328e434 Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024) Science Q article 2024 ftdoajarticles https://doi.org/10.1038/s41467-024-50316-x 2024-08-05T17:48:55Z Abstract The bat immune system features multiple unique properties such as dampened inflammatory responses and increased tissue protection, explaining their long lifespan and tolerance to viral infections. Here, we demonstrated that body temperature fluctuations corresponding to different physiological states in bats exert a large impact on their antibody repertoires. At elevated temperatures typical for flight, IgG from the bat species Myotis myotis and Nyctalus noctula show elevated antigen binding strength and diversity, recognizing both pathogen-derived antigens and autoantigens. The opposite is observed at temperatures reflecting inactive physiological states. IgG antibodies of human and other mammals, or antibodies of birds do not appear to behave in a similar way. Importantly, diversification of bat antibody specificities results in preferential recognition of damaged endothelial and epithelial cells, indicating an anti-inflammatory function. The temperature-sensitivity of bat antibodies is mediated by the variable regions of immunoglobulin molecules. Additionally, we uncover specific molecular features of bat IgG, such as low thermodynamic stability and implication of hydrophobic interactions in antigen binding as well as high prevalence of polyreactivity. Overall, our results extend the understanding of bat tolerance to disease and inflammation and highlight the link between metabolism and immunity. Article in Journal/Newspaper Nyctalus noctula Directory of Open Access Journals: DOAJ Articles Nature Communications 15 1 |
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Science Q Nia Toshkova Violeta Zhelyzkova Alejandra Reyes-Ruiz Eline Haerens Marina de Castro Deus Robin V. Lacombe Maxime Lecerf Gaelle Gonzalez Nolwenn Jouvenet Cyril Planchais Jordan D. Dimitrov Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
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Science Q |
description |
Abstract The bat immune system features multiple unique properties such as dampened inflammatory responses and increased tissue protection, explaining their long lifespan and tolerance to viral infections. Here, we demonstrated that body temperature fluctuations corresponding to different physiological states in bats exert a large impact on their antibody repertoires. At elevated temperatures typical for flight, IgG from the bat species Myotis myotis and Nyctalus noctula show elevated antigen binding strength and diversity, recognizing both pathogen-derived antigens and autoantigens. The opposite is observed at temperatures reflecting inactive physiological states. IgG antibodies of human and other mammals, or antibodies of birds do not appear to behave in a similar way. Importantly, diversification of bat antibody specificities results in preferential recognition of damaged endothelial and epithelial cells, indicating an anti-inflammatory function. The temperature-sensitivity of bat antibodies is mediated by the variable regions of immunoglobulin molecules. Additionally, we uncover specific molecular features of bat IgG, such as low thermodynamic stability and implication of hydrophobic interactions in antigen binding as well as high prevalence of polyreactivity. Overall, our results extend the understanding of bat tolerance to disease and inflammation and highlight the link between metabolism and immunity. |
format |
Article in Journal/Newspaper |
author |
Nia Toshkova Violeta Zhelyzkova Alejandra Reyes-Ruiz Eline Haerens Marina de Castro Deus Robin V. Lacombe Maxime Lecerf Gaelle Gonzalez Nolwenn Jouvenet Cyril Planchais Jordan D. Dimitrov |
author_facet |
Nia Toshkova Violeta Zhelyzkova Alejandra Reyes-Ruiz Eline Haerens Marina de Castro Deus Robin V. Lacombe Maxime Lecerf Gaelle Gonzalez Nolwenn Jouvenet Cyril Planchais Jordan D. Dimitrov |
author_sort |
Nia Toshkova |
title |
Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
title_short |
Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
title_full |
Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
title_fullStr |
Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
title_full_unstemmed |
Temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
title_sort |
temperature sensitivity of bat antibodies links metabolic state of bats with antigen-recognition diversity |
publisher |
Nature Portfolio |
publishDate |
2024 |
url |
https://doi.org/10.1038/s41467-024-50316-x https://doaj.org/article/13f32342da5a482e90b688394328e434 |
genre |
Nyctalus noctula |
genre_facet |
Nyctalus noctula |
op_source |
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024) |
op_relation |
https://doi.org/10.1038/s41467-024-50316-x https://doaj.org/toc/2041-1723 doi:10.1038/s41467-024-50316-x 2041-1723 https://doaj.org/article/13f32342da5a482e90b688394328e434 |
op_doi |
https://doi.org/10.1038/s41467-024-50316-x |
container_title |
Nature Communications |
container_volume |
15 |
container_issue |
1 |
_version_ |
1810468641987100672 |