Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens.
Fever is a regulated increase of the body temperature resulting from both infectious and non-infectious causes. Fever is known to play a role in modulating immune responses to infection, but the potential of febrile temperatures in regulating antigen binding affinity to antibodies has not been explo...
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2019-04-01
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Series: | PLoS Neglected Tropical Diseases |
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doaj-d28a145eb7514548be282ba0cc7e40c22020-11-24T21:58:33ZengPublic Library of Science (PLoS)PLoS Neglected Tropical Diseases1935-27271935-27352019-04-01134e000723910.1371/journal.pntd.0007239Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens.Razvan C StanKatia S FrançosoRubens P S AlvesLuís Carlos S FerreiraIrene S SoaresMaristela M de CamargoFever is a regulated increase of the body temperature resulting from both infectious and non-infectious causes. Fever is known to play a role in modulating immune responses to infection, but the potential of febrile temperatures in regulating antigen binding affinity to antibodies has not been explored. Here we investigated this process under in vitro conditions using Isothermal titration calorimetry and ELISA. We used selected malarial and dengue antigens against specific monoclonal antibodies, and observed a marked increase in the affinity of these antibody-antigen complexes at 40°C, compared to physiological (37°C) or pathophysiological temperatures (42°C). Induced thermal equilibration of the protein partners at these temperatures in vitro, prior to measurements, further increased their binding affinity. These results suggest another positive and adaptive role for fever in vivo, and highlight the favourable role of thermal priming in enhancing protein-protein affinity for samples with limited availability.http://europepmc.org/articles/PMC6464238?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Razvan C Stan Katia S Françoso Rubens P S Alves Luís Carlos S Ferreira Irene S Soares Maristela M de Camargo |
spellingShingle |
Razvan C Stan Katia S Françoso Rubens P S Alves Luís Carlos S Ferreira Irene S Soares Maristela M de Camargo Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. PLoS Neglected Tropical Diseases |
author_facet |
Razvan C Stan Katia S Françoso Rubens P S Alves Luís Carlos S Ferreira Irene S Soares Maristela M de Camargo |
author_sort |
Razvan C Stan |
title |
Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. |
title_short |
Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. |
title_full |
Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. |
title_fullStr |
Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. |
title_full_unstemmed |
Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. |
title_sort |
febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Neglected Tropical Diseases |
issn |
1935-2727 1935-2735 |
publishDate |
2019-04-01 |
description |
Fever is a regulated increase of the body temperature resulting from both infectious and non-infectious causes. Fever is known to play a role in modulating immune responses to infection, but the potential of febrile temperatures in regulating antigen binding affinity to antibodies has not been explored. Here we investigated this process under in vitro conditions using Isothermal titration calorimetry and ELISA. We used selected malarial and dengue antigens against specific monoclonal antibodies, and observed a marked increase in the affinity of these antibody-antigen complexes at 40°C, compared to physiological (37°C) or pathophysiological temperatures (42°C). Induced thermal equilibration of the protein partners at these temperatures in vitro, prior to measurements, further increased their binding affinity. These results suggest another positive and adaptive role for fever in vivo, and highlight the favourable role of thermal priming in enhancing protein-protein affinity for samples with limited availability. |
url |
http://europepmc.org/articles/PMC6464238?pdf=render |
work_keys_str_mv |
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