Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis
Immune control of Mycobacterium tuberculosis depends on interferon γ (IFN-γ)-producing CD4+ lymphocytes. Previous studies have shown that T cells from patients with tuberculosis produce less IFN-γ, compared with healthy donors, in response to mycobacterial antigens, although IFN-γ responses to mitog...
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paper:paper_00221899_v207_n2_p340_Pasquinelli2023-06-08T14:47:01Z Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis Pasquinelli, Virginia Alvarez, Ivana Belén Jurado, Javier Oscar García, Verónica Edith CREB IFN-γ MAPK signaling Tuberculosis gamma interferon mitogen activated protein kinase mitogen activated protein kinase p38 Mycobacterium antigen small interfering RNA tuberculostatic agent acid fast bacterium article CD4+ T lymphocyte enzyme linked immunosorbent assay flow cytometry interferon production lung tuberculosis lymphocyte activation Mycobacterium tuberculosis nonhuman priority journal protein phosphorylation T lymphocyte Western blotting Immune control of Mycobacterium tuberculosis depends on interferon γ (IFN-γ)-producing CD4+ lymphocytes. Previous studies have shown that T cells from patients with tuberculosis produce less IFN-γ, compared with healthy donors, in response to mycobacterial antigens, although IFN-γ responses to mitogens are preserved. In this work, we found that M. tuberculosis-induced IFN-γ production by human T cells correlated with phosphorylation of the mitogen-activated protein kinases (MAPKs), extracellular signal-regulated kinase (ERK), and p38. Moreover, the majority of IFN-γ-producing T cells expressed signaling lymphocyte activation molecule (SLAM), and SLAM activation further increased ERK phosphorylation. Interestingly, patients with tuberculosis had delayed activation of ERK and p38, and this was most marked in patients with the poorest IFN-γ responses (ie, low responders). Besides, SLAM signaling failed to phosphorylate ERK in low responders. Our findings suggest that activation of p38 and ERK, in part through SLAM, mediates T-cell IFN-γ production in response to M. tuberculosis, a pathway that is defective in patients with tuberculosis. © The Author 2012. Published by Oxford University Press on behalf of the Infectious Diseases Society of America. All rights reserved. Fil:Pasquinelli, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Alvarez, I.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Jurado, J.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:García, V.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221899_v207_n2_p340_Pasquinelli http://hdl.handle.net/20.500.12110/paper_00221899_v207_n2_p340_Pasquinelli |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
CREB IFN-γ MAPK signaling Tuberculosis gamma interferon mitogen activated protein kinase mitogen activated protein kinase p38 Mycobacterium antigen small interfering RNA tuberculostatic agent acid fast bacterium article CD4+ T lymphocyte enzyme linked immunosorbent assay flow cytometry interferon production lung tuberculosis lymphocyte activation Mycobacterium tuberculosis nonhuman priority journal protein phosphorylation T lymphocyte Western blotting |
spellingShingle |
CREB IFN-γ MAPK signaling Tuberculosis gamma interferon mitogen activated protein kinase mitogen activated protein kinase p38 Mycobacterium antigen small interfering RNA tuberculostatic agent acid fast bacterium article CD4+ T lymphocyte enzyme linked immunosorbent assay flow cytometry interferon production lung tuberculosis lymphocyte activation Mycobacterium tuberculosis nonhuman priority journal protein phosphorylation T lymphocyte Western blotting Pasquinelli, Virginia Alvarez, Ivana Belén Jurado, Javier Oscar García, Verónica Edith Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
topic_facet |
CREB IFN-γ MAPK signaling Tuberculosis gamma interferon mitogen activated protein kinase mitogen activated protein kinase p38 Mycobacterium antigen small interfering RNA tuberculostatic agent acid fast bacterium article CD4+ T lymphocyte enzyme linked immunosorbent assay flow cytometry interferon production lung tuberculosis lymphocyte activation Mycobacterium tuberculosis nonhuman priority journal protein phosphorylation T lymphocyte Western blotting |
description |
Immune control of Mycobacterium tuberculosis depends on interferon γ (IFN-γ)-producing CD4+ lymphocytes. Previous studies have shown that T cells from patients with tuberculosis produce less IFN-γ, compared with healthy donors, in response to mycobacterial antigens, although IFN-γ responses to mitogens are preserved. In this work, we found that M. tuberculosis-induced IFN-γ production by human T cells correlated with phosphorylation of the mitogen-activated protein kinases (MAPKs), extracellular signal-regulated kinase (ERK), and p38. Moreover, the majority of IFN-γ-producing T cells expressed signaling lymphocyte activation molecule (SLAM), and SLAM activation further increased ERK phosphorylation. Interestingly, patients with tuberculosis had delayed activation of ERK and p38, and this was most marked in patients with the poorest IFN-γ responses (ie, low responders). Besides, SLAM signaling failed to phosphorylate ERK in low responders. Our findings suggest that activation of p38 and ERK, in part through SLAM, mediates T-cell IFN-γ production in response to M. tuberculosis, a pathway that is defective in patients with tuberculosis. © The Author 2012. Published by Oxford University Press on behalf of the Infectious Diseases Society of America. All rights reserved. |
author |
Pasquinelli, Virginia Alvarez, Ivana Belén Jurado, Javier Oscar García, Verónica Edith |
author_facet |
Pasquinelli, Virginia Alvarez, Ivana Belén Jurado, Javier Oscar García, Verónica Edith |
author_sort |
Pasquinelli, Virginia |
title |
Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
title_short |
Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
title_full |
Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
title_fullStr |
Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
title_full_unstemmed |
Phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
title_sort |
phosphorylation of mitogen-activated protein kinases contributes to interferon γ production in response to mycobacterium tuberculosis |
publishDate |
2013 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221899_v207_n2_p340_Pasquinelli http://hdl.handle.net/20.500.12110/paper_00221899_v207_n2_p340_Pasquinelli |
work_keys_str_mv |
AT pasquinellivirginia phosphorylationofmitogenactivatedproteinkinasescontributestointerferongproductioninresponsetomycobacteriumtuberculosis AT alvarezivanabelen phosphorylationofmitogenactivatedproteinkinasescontributestointerferongproductioninresponsetomycobacteriumtuberculosis AT juradojavieroscar phosphorylationofmitogenactivatedproteinkinasescontributestointerferongproductioninresponsetomycobacteriumtuberculosis AT garciaveronicaedith phosphorylationofmitogenactivatedproteinkinasescontributestointerferongproductioninresponsetomycobacteriumtuberculosis |
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1768546707411304448 |