Capsid proteins of foot-and-mouth disease virus interact with TLR2 and CD14 to induce cytokine production

Lin, Yi-Te; Chen, Yen‐Po; Fang, Chia-Hsun; Huang, Pau-Yi; Liang, Shu‐Mei

doi:10.1016/j.imlet.2020.04.008

Cited by 8 publications

(8 citation statements)

References 29 publications

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“…We provide evidence that CapRels and their phage-encoded triggers are engaged in a 'Red Queen conflict' 5 , revealing a new front in the intense coevolutionary battle between phages and bacteria. Given that capsid proteins of some eukaryotic viruses are known to stimulate innate immune signalling in mammalian hosts [6][7][8][9][10] , our results reveal a deeply conserved facet of immunity.…”

mentioning

confidence: 83%

Direct activation of a bacterial innate immune system by a viral capsid protein

Zhang

Tamman

Wallant

et al. 2022

Nature

114

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Bacteria have evolved diverse immunity mechanisms to protect themselves against the constant onslaught of bacteriophages1–3. Similar to how eukaryotic innate immune systems sense foreign invaders through pathogen-associated molecular patterns4 (PAMPs), many bacterial immune systems that respond to bacteriophage infection require phage-specific triggers to be activated. However, the identities of such triggers and the sensing mechanisms remain largely unknown. Here we identify and investigate the anti-phage function of CapRelSJ46, a fused toxin–antitoxin system that protects Escherichia coli against diverse phages. Using genetic, biochemical and structural analyses, we demonstrate that the C-terminal domain of CapRelSJ46 regulates the toxic N-terminal region, serving as both antitoxin and phage infection sensor. Following infection by certain phages, newly synthesized major capsid protein binds directly to the C-terminal domain of CapRelSJ46 to relieve autoinhibition, enabling the toxin domain to pyrophosphorylate tRNAs, which blocks translation to restrict viral infection. Collectively, our results reveal the molecular mechanism by which a bacterial immune system directly senses a conserved, essential component of phages, suggesting a PAMP-like sensing model for toxin–antitoxin-mediated innate immunity in bacteria. We provide evidence that CapRels and their phage-encoded triggers are engaged in a ‘Red Queen conflict’5, revealing a new front in the intense coevolutionary battle between phages and bacteria. Given that capsid proteins of some eukaryotic viruses are known to stimulate innate immune signalling in mammalian hosts6–10, our results reveal a deeply conserved facet of immunity.

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mentioning

confidence: 83%

Direct activation of a bacterial innate immune system by a viral capsid protein

Zhang

Tamman

Wallant

et al. 2022

Nature

114

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“…NOD2 binding to a viral ssRNA also induces its homo- or heterodimerisation with NOD1, allowing receptor-interacting serine/threonine-protein kinase 2 (RIP2) recruitment via an interaction between their CARD domains and promoting its autophosphorylation [ 33 ]. Endosomal RNAs are detected by membrane toll-like receptors (TLRs) receptors, such as TLR3, TLR7 and TLR8, while the structural proteins VP1 and VP3 can be recognised by TRL2 and TRL4 receptors, respectively [ 34 , 35 , 36 , 37 ]. Upon activation by ligand recognition, these TLRs interact with adaptor proteins, namely TIR domain-containing adapter molecule 1 (TRIF) and myeloid differentiation primary response protein MyD88 (MYD88), itself associated with interleukin-1 receptor-associated kinase 1 (IRAK1) and IRAK4.…”

Section: Fmdv and Innate Immunitymentioning

confidence: 99%

“…This protein is among the first to be detected by the host cell. Indeed, VP1, is specifically recognised by human TLR2, through cooperation with TLR1 and TLR6 [ 36 ]. After adhesion of the capsid protein to TRL2, MyD88, a receptor-associated protein induces the recruitment of IRAK1 IRAK4, leading to the IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation.…”

Section: Fmdv and Innate Immunitymentioning

confidence: 99%

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Foot-and-Mouth Disease Virus: Molecular Interplays with IFN Response and the Importance of the Model

Sarry

Vitour

Zientara

et al. 2022

Viruses

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Foot-and-mouth disease (FMD) is a highly contagious viral disease of cloven-hoofed animals with a significant socioeconomic impact. One of the issues related to this disease is the ability of its etiological agent, foot-and-mouth disease virus (FMDV), to persist in the organism of its hosts via underlying mechanisms that remain to be elucidated. The establishment of a virus–host equilibrium via protein–protein interactions could contribute to explaining these phenomena. FMDV has indeed developed numerous strategies to evade the immune response, especially the type I interferon response. Viral proteins target this innate antiviral response at different levels, ranging from blocking the detection of viral RNAs to inhibiting the expression of ISGs. The large diversity of impacts of these interactions must be considered in the light of the in vitro models that have been used to demonstrate them, some being sometimes far from biological systems. In this review, we have therefore listed the interactions between FMDV and the interferon response as exhaustively as possible, focusing on both their biological effect and the study models used.

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“…The liquid component in the blood vessel. Cytokines ( 12 ) and proteins such as cellulose and various inflammatory cells enter the tissue through the blood vessel wall, causing an increase in local tissue components, which is manifested as edema. Highly expressed IL-1 cytokines play a key role in the pathogenesis of vesicular lesions by FMDV infection ( 13 ).…”

Section: Introductionmentioning

confidence: 99%

Component Identification and Analysis of Vesicular Fluid From Swine Infected by Foot-and-Mouth Disease Virus

Zhang

Yang

et al. 2022

Front. Vet. Sci.

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Foot-and-mouth disease (FMD) is induced by FMD virus (FMDV) and characterized by fever and vesicular (blister-like) lesions. However, the exact composition of the vesicular fluid in pigs infected with FMDV remains unclear. To identify and analyze the components of the vesicular fluid in FMDV-infected domestic pigs, the fluid was collected and subjected to mass spectrometry. Further analyses were conducted using Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genome (KEGG), and protein–protein interaction (PPI). Quantitative ELISA kit for TNF-α, and IFN-α, IFN-β, IL-6, IL-10, IL-1β, and IFN-γ were used to verify the mass spectrometry results. Results showed that 937 proteins were identified in the vesicular fluid from swine after FMDV infection, and bioinformatics analysis indicated that these proteins are related to the innate immune and inflammation pathways. The levels of cytokines involved in the disease-related pathways, tumor necrosis factors, and IL-6 in the fluid samples were significantly increased. This study identified and analyzed the composition of vesicular fluid in pigs after FMD infection for the first time and provided interesting information that help understand the infection and pathogenesis mechanism of FMD. These information will eventually contribute to the prevention and control of FMD.

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Capsid proteins of foot-and-mouth disease virus interact with TLR2 and CD14 to induce cytokine production

Cited by 8 publications

References 29 publications

Direct activation of a bacterial innate immune system by a viral capsid protein

Direct activation of a bacterial innate immune system by a viral capsid protein

Foot-and-Mouth Disease Virus: Molecular Interplays with IFN Response and the Importance of the Model

Component Identification and Analysis of Vesicular Fluid From Swine Infected by Foot-and-Mouth Disease Virus

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