Proteomics in immunity and herpes simplex encephalitis

Diego, Rebeca Pérez de; Mulvey, Claire M.; Casanova, Jean‐Laurent; Godovac‐Zimmermann, Jasminka

doi:10.1586/14789450.2014.864954

Cited by 5 publications

(5 citation statements)

References 38 publications

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“…In addition, the enteroviral +ssRNA genome can also be sensed by TLR3 through its incomplete stem structures (Tatematsu et al 2013). TLR3 activation leads to innate immune responses against the invaded pathogens, including triggering inflammation by NF-κB signaling cascade and inducing type I IFN expression by activating IRF3 and IRF7 (Pérez De Diego et al 2014). However, in the present study, our evidence indicates that miR-146a could doubly block the NF-κB pathway by targeting TLR3 and its downstream player TRAF6.…”

Section: Discussioncontrasting

confidence: 71%

MiR-146a down-regulates inflammatory response by targeting TLR3 and TRAF6 in Coxsackievirus B infection

Fei

Chaulagain

Wang

et al. 2019

RNA

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Coxsackievirus B (CVB) is the major cause of human myocarditis and dilated cardiomyopathy. Toll-like receptor 3 (TLR3) is an intracellular sensor to detect pathogen's dsRNA. TLR3, along with TRAF6, triggers an inflammatory response through NF-κB signaling pathway. In the cells infected with CVB type 3 (CVB3), the abundance of miR-146a was significantly increased. The role of miR-146a in CVB infection is unclear. In this study, TLR3 and TRAF6 were identified as the targets of miR-146a. The elevated miR-146a inhibited NF-κB translocation and subsequently down-regulated proinflammatory cytokine expression in the CVB3-infected cells. Therefore, the NF-κB pathway can be doubly blocked by miR-146a through targeting of TLR3 and TRAF6. MiR-146a may be a negative regulator on inflammatory response and an intrinsic protective factor in CVB infection.

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Section: Discussioncontrasting

confidence: 71%

MiR-146a down-regulates inflammatory response by targeting TLR3 and TRAF6 in Coxsackievirus B infection

Fei

Chaulagain

Wang

et al. 2019

RNA

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“…Recently, GWAS approaches to complex diseases are less and less focused on individual associations, and more addressed at the biological pathways and networks suggested by genetic associations (Ramanan & Saykin, ). Thus, recent hypotheses that complex diseases might be influenced by a highly personalized combination of variants—some common and others rare, some protective and others deleterious—stimulate the integration of genetic associations with further investigations based on transcriptomic, metabolomics, and proteomic approaches in order to get pathway‐ and network‐driven models that can explain the broad molecular underpinnings of disease (Scholz et al, ; Perez de Diego et al, ). Crucial, widespread processes, such as translational control of expression, post‐translational modifications including redox‐related changes, and spatial switching of moonlighting proteins between different functions, are essentially invisible to transcriptomics and must be addressed directly by proteomics.…”

Section: Complexity and Spatial Proteomics Of Cellsmentioning

confidence: 99%

Spatial perspectives in the redox code—Mass spectrometric proteomics studies of moonlighting proteins

Pinto

Radulović

Godovac‐Zimmermann

2016

Mass Spectrometry Reviews

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The Redox Code involves specific, reversible oxidative changes in proteins that modulate protein tertiary structure, interactions, trafficking, and activity, and hence couple the proteome to the metabolic/oxidative state of cells. It is currently a major focus of study in cell biology. Recent studies of dynamic cellular spatial reorganization with MS-based subcellular-spatial-razor proteomics reveal that protein constituents of many subcellular structures, including mitochondria, the endoplasmic reticulum, the plasma membrane, and the extracellular matrix, undergo changes in their subcellular abundance/distribution in response to oxidative stress. These proteins are components of a diverse variety of functional processes spatially distributed across cells. Many of the same proteins are involved in response to suppression of DNA replication indicate that oxidative stress is strongly intertwined with DNA replication/proliferation. Both are replete with networks of moonlighting proteins that show coordinated changes in subcellular location and that include primary protein actuators of the redox code involved in the processing of NAD /NADH, NADP /NADPH, Cys/CySS, and GSH/GSSG redox couples. Small groups of key proteins such as {KPNA2, KPNB1, PCNA, PTMA, SET} constitute "spatial switches" that modulate many nuclear processes. Much of the functional response involves subcellular protein trafficking, including nuclear import/export processes, vesicle-mediated trafficking, the endoplasmic reticulum/Golgi pathway, chaperone-assisted processes, and other transport systems. This is not visible to measurements of total protein abundance by transcriptomics or proteomics. Comprehensive pictures of cellular function will require collection of data on the subcellular transport and local functions of many moonlighting proteins, especially of those with critical roles in spatial coordination across cells. The proteome-wide analysis of coordinated changes in abundance and trafficking of proteins offered by MS-based proteomics has a unique, crucial role to play in deciphering the complex adaptive systems that underlie cellular function. © 2016 Wiley Periodicals, Inc. Mass Spec Rev.

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“…Moreover, 30% of HSE patients do not have deficiencies in TLR3 induced type I and III IFN production. These observations prompted Pérez de Diego et al to use MSBP to search for other factors regulating the TLR3 signaling pathway or other independent pathways that may be associated with HSE susceptibility [80]. The proteomic changes in fibroblasts from healthy and HSE patients were compared after TLR3 activation.…”

Section: The Innate Immune System Controls Herpes Simplex Encephalitismentioning

confidence: 99%

“…Herpes simplex virus encephalitis (HSE), a disease caused by the rare infection of the CNS by HSV, may result from deficiency of type I and III IFN production in response to Toll‐like respector 3 (TLR3) activation during HSV‐1 infection . This conclusion follows from five genetic etiologies of HSE (UNC‐93B, TLR3, TRAF3, TRIF, TBK1) that are all involved in TLR3 signaling.…”

Section: Cell Response To Viral Infectionmentioning

confidence: 99%

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Investigating the biology of alpha herpesviruses with MS‐based proteomics

et al. 2015

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Viruses are intracellular parasites that can only replicate and spread in cells of susceptible hosts. Alpha herpesviruses (α-HVs) contain double stranded DNA genomes of at least 120 kb, encoding for 70 or more genes. The viral genome is contained in an icosahedral capsid that is surrounded by a proteinaceous tegument layer and a lipid envelope. Infection starts in epithelial cells and spreads to the peripheral nervous system (PNS). In the natural host, α-HVs establish a chronic latent infection that can be reactivated, rarely spread to the central nervous system (CNS). In the non-natural host, viral infection will in most cases spread to the CNS with often fatal outcome. The host response plays a crucial role in the outcome of viral infection. α-HVs do not encode all the genes required for viral replication and spread. They need a variety of host gene products including RNA polymerase, ribosomes, dynein, and kinesin. As a result, the infected cell is dramatically different from the uninfected cell revealing a complex and dynamic interplay of viral and host components required to complete the virus life cycle. In this review, we describe the pivotal contribution of mass spectrometry-based proteomics (MSBP) studies over the past 15 years to understanding the complicated life cycle and pathogenesis of four α-HV species from the alphaherpesvirinae subfamily: Herpes simplex virus-1 (HSV-1), varicella zoster virus (VZV), pseudorabies virus (PRV) and bovine herpes virus (BHV-1). We describe the viral proteome dynamics during host infection and the host proteomic response to counteract such pathogens.

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Proteomics in immunity and herpes simplex encephalitis

Cited by 5 publications

References 38 publications

MiR-146a down-regulates inflammatory response by targeting TLR3 and TRAF6 in Coxsackievirus B infection

MiR-146a down-regulates inflammatory response by targeting TLR3 and TRAF6 in Coxsackievirus B infection

Spatial perspectives in the redox code—Mass spectrometric proteomics studies of moonlighting proteins

Investigating the biology of alpha herpesviruses with MS‐based proteomics

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