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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Main Authors: Razvan C Stan, Katia S Françoso, Rubens P S Alves, Luís Carlos S Ferreira, Irene S Soares, Maristela M de Camargo
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2019-04-01
Series:PLoS Neglected Tropical Diseases
Online Access:http://europepmc.org/articles/PMC6464238?pdf=render
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spelling 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
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