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NLRP3 炎性体激活半胱天冬酶-1 调控 NADPH 氧化酶 NOX2 以控制吞噬体功能。

Activation of caspase-1 by the NLRP3 inflammasome regulates the NADPH oxidase NOX2 to control phagosome function.

机构信息

Developmental Immunology and Center for Computational and Integrative Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA.

出版信息

Nat Immunol. 2013 Jun;14(6):543-53. doi: 10.1038/ni.2595. Epub 2013 May 5.

DOI:10.1038/ni.2595
PMID:23644505
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3708594/
Abstract

Phagocytosis is a fundamental cellular process that is pivotal for immunity as it coordinates microbial killing, innate immune activation and antigen presentation. An essential step in this process is phagosome acidification, which regulates many functions of these organelles that allow phagosomes to participate in processes that are essential to both innate and adaptive immunity. Here we report that acidification of phagosomes containing Gram-positive bacteria is regulated by the NLRP3 inflammasome and caspase-1. Active caspase-1 accumulates on phagosomes and acts locally to control the pH by modulating buffering by the NADPH oxidase NOX2. These data provide insight into a mechanism by which innate immune signals can modify cellular defenses and establish a new function for the NLRP3 inflammasome and caspase-1 in host defense.

摘要

吞噬作用是一种基本的细胞过程，对于免疫至关重要，因为它协调了微生物的杀伤、先天免疫的激活和抗原呈递。这个过程中的一个关键步骤是吞噬体酸化，它调节这些细胞器的许多功能，使吞噬体能够参与先天免疫和适应性免疫都必不可少的过程。在这里，我们报告含有革兰氏阳性菌的吞噬体酸化受 NLRP3 炎性体和半胱天冬酶-1 调节。活性半胱天冬酶-1 在吞噬体上积累，并通过调节 NADPH 氧化酶 NOX2 的缓冲作用来局部控制 pH 值。这些数据提供了一种机制的见解，即先天免疫信号可以修饰细胞防御，并为 NLRP3 炎性体和半胱天冬酶-1 在宿主防御中的新功能奠定了基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/f3d15a15959e/nihms-461789-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/78c3ace442d2/nihms-461789-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/672ebe0b9786/nihms-461789-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/e8edafccb9fb/nihms-461789-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/f01ef02452b7/nihms-461789-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/a121df8e3373/nihms-461789-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/001434cbd11e/nihms-461789-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/f3d15a15959e/nihms-461789-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/78c3ace442d2/nihms-461789-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/672ebe0b9786/nihms-461789-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/e8edafccb9fb/nihms-461789-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/f01ef02452b7/nihms-461789-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/a121df8e3373/nihms-461789-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/001434cbd11e/nihms-461789-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ebe/3708594/f3d15a15959e/nihms-461789-f0007.jpg

相似文献

[1]
Activation of caspase-1 by the NLRP3 inflammasome regulates the NADPH oxidase NOX2 to control phagosome function.

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[3]
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[6]
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[10]
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[3]
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[4]
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[5]
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[6]
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[7]
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[8]
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[9]
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[10]
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本文引用的文献

[1]
Measurement of phagocytosis, phagosome acidification, and intracellular killing of Staphylococcus aureus.

Curr Protoc Immunol. 2012-11

[2]
Caspase-11 promotes the fusion of phagosomes harboring pathogenic bacteria with lysosomes by modulating actin polymerization.

Immunity. 2012-5-31

[3]
Phagosomal degradation increases TLR access to bacterial ligands and enhances macrophage sensitivity to bacteria.

J Immunol. 2011-10-26

[4]
A role for mitochondria in NLRP3 inflammasome activation.

Nature. 2010-12-1

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TLR9 is actively recruited to Aspergillus fumigatus phagosomes and requires the N-terminal proteolytic cleavage domain for proper intracellular trafficking.

J Immunol. 2010-11-8

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Inflammasome inhibition as a pathogenic stealth mechanism.

Cell Host Microbe. 2010-7-22

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Inflammasome activation in NADPH oxidase defective mononuclear phagocytes from patients with chronic granulomatous disease.

Blood. 2010-5-21

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Phagocytosis and phagosome acidification are required for pathogen processing and MyD88-dependent responses to Staphylococcus aureus.

J Immunol. 2010-5-17

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Curr Opin Immunol. 2010-2-18

[10]
Staphylococcus aureus evades lysozyme-based peptidoglycan digestion that links phagocytosis, inflammasome activation, and IL-1beta secretion.

Cell Host Microbe. 2010-1-21

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