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Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress

Heat shock proteins (Hsps) are among the most widely distributed and evolutionary conserved proteins. Hsps are essential regulators of diverse constitutive metabolic processes and are markedly upregulated during stress. A 62 kDa Hsp (Hsp60) of Histoplasma capsulatum (Hc) is an immunodominant antigen...

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Autores principales: Guimarães, Allan Jefferson, Nakayasu, Ernesto S., Sobreira, Tiago J. P., Cordero, Radames J. B., Nimrichter, Leonardo, Almeida, Igor C., Nosanchuk, Joshua Daniel
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3037374/
https://www.ncbi.nlm.nih.gov/pubmed/21347364
http://dx.doi.org/10.1371/journal.pone.0014660
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author Guimarães, Allan Jefferson
Nakayasu, Ernesto S.
Sobreira, Tiago J. P.
Cordero, Radames J. B.
Nimrichter, Leonardo
Almeida, Igor C.
Nosanchuk, Joshua Daniel
author_facet Guimarães, Allan Jefferson
Nakayasu, Ernesto S.
Sobreira, Tiago J. P.
Cordero, Radames J. B.
Nimrichter, Leonardo
Almeida, Igor C.
Nosanchuk, Joshua Daniel
author_sort Guimarães, Allan Jefferson
collection PubMed
description Heat shock proteins (Hsps) are among the most widely distributed and evolutionary conserved proteins. Hsps are essential regulators of diverse constitutive metabolic processes and are markedly upregulated during stress. A 62 kDa Hsp (Hsp60) of Histoplasma capsulatum (Hc) is an immunodominant antigen and the major surface ligand to CR3 receptors on macrophages. However little is known about the function of this protein within the fungus. We characterized Hc Hsp60-protein interactions under different temperature to gain insights of its additional functions oncell wall dynamism, heat stress and pathogenesis. We conducted co-immunoprecipitations with antibodies to Hc Hsp60 using cytoplasmic and cell wall extracts. Interacting proteins were identified by shotgun proteomics. For the cell wall, 84 common interactions were identified among the 3 growth conditions, including proteins involved in heat-shock response, sugar and amino acid/protein metabolism and cell signaling. Unique interactions were found at each temperature [30°C (81 proteins), 37°C (14) and 37/40°C (47)]. There were fewer unique interactions in cytoplasm [30°C (6), 37°C (25) and 37/40°C (39)] and four common interactions, including additional Hsps and other known virulence factors. These results show the complexity of Hsp60 function and provide insights into Hc biology, which may lead to new avenues for the management of histoplasmosis.
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spelling pubmed-30373742011-02-23 Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress Guimarães, Allan Jefferson Nakayasu, Ernesto S. Sobreira, Tiago J. P. Cordero, Radames J. B. Nimrichter, Leonardo Almeida, Igor C. Nosanchuk, Joshua Daniel PLoS One Research Article Heat shock proteins (Hsps) are among the most widely distributed and evolutionary conserved proteins. Hsps are essential regulators of diverse constitutive metabolic processes and are markedly upregulated during stress. A 62 kDa Hsp (Hsp60) of Histoplasma capsulatum (Hc) is an immunodominant antigen and the major surface ligand to CR3 receptors on macrophages. However little is known about the function of this protein within the fungus. We characterized Hc Hsp60-protein interactions under different temperature to gain insights of its additional functions oncell wall dynamism, heat stress and pathogenesis. We conducted co-immunoprecipitations with antibodies to Hc Hsp60 using cytoplasmic and cell wall extracts. Interacting proteins were identified by shotgun proteomics. For the cell wall, 84 common interactions were identified among the 3 growth conditions, including proteins involved in heat-shock response, sugar and amino acid/protein metabolism and cell signaling. Unique interactions were found at each temperature [30°C (81 proteins), 37°C (14) and 37/40°C (47)]. There were fewer unique interactions in cytoplasm [30°C (6), 37°C (25) and 37/40°C (39)] and four common interactions, including additional Hsps and other known virulence factors. These results show the complexity of Hsp60 function and provide insights into Hc biology, which may lead to new avenues for the management of histoplasmosis. Public Library of Science 2011-02-10 /pmc/articles/PMC3037374/ /pubmed/21347364 http://dx.doi.org/10.1371/journal.pone.0014660 Text en Guimarães 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
Guimarães, Allan Jefferson
Nakayasu, Ernesto S.
Sobreira, Tiago J. P.
Cordero, Radames J. B.
Nimrichter, Leonardo
Almeida, Igor C.
Nosanchuk, Joshua Daniel
Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress
title Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress
title_full Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress
title_fullStr Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress
title_full_unstemmed Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress
title_short Histoplasma capsulatum Heat-Shock 60 Orchestrates the Adaptation of the Fungus to Temperature Stress
title_sort histoplasma capsulatum heat-shock 60 orchestrates the adaptation of the fungus to temperature stress
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3037374/
https://www.ncbi.nlm.nih.gov/pubmed/21347364
http://dx.doi.org/10.1371/journal.pone.0014660
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