VISA Blocking Peptide
- Known as:
- VISA Blocking Peptide
- Catalog number:
- 33r-9412
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- VISA Blocking Peptide
Related genes to: VISA Blocking Peptide
- Gene:
- MAVS NIH gene
- Name:
- mitochondrial antiviral signaling protein
- Previous symbol:
- -
- Synonyms:
- VISA, KIAA1271, IPS-1, Cardif
- Chromosome:
- 20p13
- Locus Type:
- gene with protein product
- Date approved:
- 2009-04-01
- Date modifiied:
- 2017-09-22
Related products to: VISA Blocking Peptide
Related articles to: VISA Blocking Peptide
- Chemotherapy-induced neuropathic pain (CINP) can be triggered by microtubule-targeting agents, including plant-derived vinca alkaloids such as vincristine (VCR). In a male mouse model of VCR-induced neuropathic pain (VINP), mitochondrial antiviral signaling protein (MAVS) expression was upregulated in the spinal cord. Suppression of MAVS significantly increased the pain threshold, alleviated persistent vincristine-induced hyperalgesia, and ameliorated mitochondrial damage in the spinal cord. Through bioinformatic analysis, transcription factor 12 (TCF12) was identified as a transcription factor with high binding potential to the MAVS gene promoter. Dual-luciferase reporter and electrophoretic mobility shift assays (EMSA) confirmed that TCF12 binds to the MAVS promoter region and promotes its transcriptional activation. Furthermore, immunofluorescence double staining demonstrated TCF12 localization in spinal astrocytes of VCR-treated male mice. Knockdown of TCF12 via siRNA attenuated chemotherapy-induced mechanical allodynia and thermal hyperalgesia, and reduced MAVS expression. Notably, in VCR-treated primary astrocytes, GFAP fluorescence intensity was increased and showed enhanced co-localization with TCF12. Silencing either TCF12 or MAVS elevated the mitochondrial membrane potential in primary mouse astrocytes and reduced the levels of pro-inflammatory cytokines such as TNF-α, IL-1β, and CXCL1. In summary, our study reveals that the TCF12-MAVS signaling axis plays a critical role in the development of VINP. Inhibition of this pathway alleviates neuropathic pain and mitochondrial injury caused by chemotherapeutic agents, providing new potential targets and molecular insights for the prevention and treatment of VINP. - Source: PubMed
Publication date: 2026/05/20
Zhou LinLi XiaoLiu HangLi YihengQian MingYang Hui - The matrix protein 2 (M2) is one of the most representative and widely studied ion channel proteins, which plays broad biological roles in the life cycle of the influenza A virus. The M2 protein affects the function of host cells and the regulation of cellular homeostasis in an ion channel activity-dependent or-independent manner and it is also the target for anti-influenza virus drugs, such as amantadine and rimantadine. The focus of this review is to summarize the research progress on the M2 protein, such as structure and function, vaccine and drug development as well as antagonist of host innate immune responses. A particular emphasis is placed on the multifaceted roles of M2 beyond canonical ion conduction. Specifically, M2 modulates the MAVS pathway through direct interaction with MAVS and by inducing ROS production, which amplifies interferon-mediated inflammation while paradoxically disrupting autophagic degradation of MAVS aggregation. Concurrently, the M2 protein orchestrates autophagy regulation by inhibiting autophagosome-lysosome fusion and initiating AKT-mTOR signaling, thus stabilizing the viral polymerase to enhance viral replication. A comprehensive understanding of these mechanisms is essential for advancing universal M2-based vaccine strategies and novel host-directed antiviral therapies. - Source: PubMed
Publication date: 2026/05/20
Ren WeigangWang QinYi YongxiangLi Junwei - Retinoic acid-inducible gene I (RIG-I)-like receptors, including RIG-I and MDA5, are key cytoplasmic pattern-recognition receptors that detect viral RNA in the cytoplasm and trigger the production of interferon (IFN). Among them, MDA5, rather than RIG-I, is considered the primary sensor during picornavirus infection due to the unique features of picornaviral RNA. However, previous studies have indicated that RIG-I also possesses antiviral activity against several picornaviruses, suggesting its potential importance during viral replication. Here, we found that 3A proteins from various picornaviruses, including Senecavirus A (SVA), Enterovirus 71 (EV71), Encephalomyocarditis virus (EMCV), foot-and-mouth disease virus (FMDV), and Coxsackievirus A16 (CA16), directly target RIG-I to suppress RIG-I-like receptor-mediated IFN-β production. Mechanistically, these picornaviral 3A proteins partially share the following similar strategies to dysregulate RIG-I activation: (i) all interact with RIG-I, (ii) EMCV and FMDV 3A reduce RIG-I expression, and (iii) SVA, EV71, EMCV, and FMDV 3A impair the interaction between RIG-I and MAVS by diminishing K63-linked ubiquitination of RIG-I. These findings broaden our understanding of how picornaviruses employ nonstructural proteins to evade innate immune responses during early infection.IMPORTANCEPicornaviruses cause a broad spectrum of human and animal diseases; however, the mechanisms by which they counteract host antiviral defenses remain incompletely understood. Owing to the distinct structural features of picornaviral RNA, MDA5 is widely regarded as the primary sensor mediating antiviral responses during picornavirus infection. However, accumulating evidence suggests that RIG-I also contributes to antiviral defense. Picornaviruses have evolved various means to suppress RIG-I and MDA5 activity, thereby facilitating evasion of the innate immune response and underscoring the importance of RIG-I during picornavirus infection. This study identifies RIG-I as a conserved target of the nonstructural protein 3A from multiple picornaviruses, including Senecavirus A, Enterovirus 71, Encephalomyocarditis virus, foot-and-mouth disease virus, and Coxsackievirus A16, and uncovers both shared and virus-specific strategies that dysregulate RIG-I-mediated interferon production. Collectively, these findings expand our understanding of the antagonistic mechanisms of how picornaviruses manipulate the host innate immune system. - Source: PubMed
Publication date: 2026/05/20
Zhang XiangleZhao ZhenxiangLi KangliChen WenzheWang GuanshunYang FanZhu GuoliangHe JijunLan XiZheng HaixueLi PengfeiZhu Zixiang - Heterogenous transcription start site (TSS) usage dictates the 5' leader structure and function of unspliced HIV-1 RNAs (usRNA). We and others have previously reported that expression and Rev/CRM1-mediated nuclear export of HIV-1 usRNA in macrophages activates MDA5, MAVS, and innate immune signaling cascades. In this study, we reveal that MDA5 sensing of viral usRNA is largely determined by TSS and cytoplasmic RNA function in macrophages. We show that HIV-1 usRNAs (1G) that are preferentially destined for dimerization and viral genome packaging are specifically targeted by MDA5, while efficiently translated (3G) usRNAs are immunologically silent. Using mutant viruses which generate usRNA with altered 5' leader structure, or inclusion of a retroviral constitutive transport element which drives mRNA-like NXF1-dependent nuclear export of viral usRNA, we show that transcription initiation site and nuclear export pathway choice are major determinants of both HIV-1 usRNA immunogenicity and cytoplasmic function. In total, we identify innate immune response modulation as a consequence of the well-conserved heterogenous TSS usage among ancestral and extant HIV-1 isolates in humans, and shed light on how MDA5 discriminates between self and non-self RNAs. - Source: PubMed
Publication date: 2026/05/19
Hughes Ivy KKharytonchyk SiarheiRamaswamy SitaJalloh SallieuHood James BHe XianbaoHenderson Andrew JAkiyama HisashiTelesnitsky AliceGummuluru Suryaram - Equine arteritis virus (EAV) is a positive-sense, single-stranded RNA virus that belongs to the family , which also includes porcine reproductive and respiratory syndrome virus (PRRSV). EAV is the causative agent of equine viral arteritis (EVA), an economically important systemic, reproductive, and respiratory disease of equids. EAV infection triggers host innate immunity, yet the precise strategies employed by the virus to evade immune defenses and achieve productive infection are poorly characterized. In this study, it was observed that EAV infection can induce a cellular IFN response; however, EAV simultaneously significantly suppresses the expression of IFN-β in host cells. Our findings indicate that host cells sense EAV and elicit an IFN response via mitochondrial antiviral-signaling protein (MAVS)-mediated signal, but the virus can dampen this signaling to enhance infection. Further investigation showed that EAV nsp10 protein could interact with MAVS and promote its degradation. By screening, we found that the E3 ubiquitin ligases Smurf1 and MARCH5 are recruited by nsp10 to polyubiquitinate and degrade MAVS. Interestingly, the degradation of MAVS promoted by nsp10 depends on the dimerization of nsp10, which occurs through the interactions of zinc finger motifs. The CARD or PRR domain of MAVS and the 1A domain of nsp10 are responsible for the interaction between MAVS and nsp10. Moreover, we have identified the key amino acid residues that mediate the interactions between nsp10 and its binding partners. Specifically, D249, S287, and the S1/F39/N41 sites are critical for its binding to MAVS, Smurf1, and MARCH5, respectively. This study demonstrated a novel role for the arteriviral RNA helicase nsp10 in targeting MAVS to counteract innate immunity and reveals the mechanism by which EAV antagonizes MAVS.IMPORTANCEDue to the MAVS functions as a "switch" in the immune signal transduction against RNA viruses, MAVS has emerged as the central regulatory target by viruses. Recently, researchers show increasing interest in viral evasion strategies targeting MAVS. The method of antagonism of MAVS by EAV is still unknown. To date, the roles of arteriviral RNA helicases, such as the EAV helicase nsp10, in regulating host cellular responses have received little research attention. In this study, we found that EAV nsp10 could mediate MAVS degradation through the proteasome via the E3 ubiquitin ligases Smurf1 and MARCH5. This is the first time that an arteriviral RNA helicase has been found to have an antagonistic effect on the innate immunity signaling pathway. Overall, our study reveals a novel mechanism by which EAV can evade host innate immunity and provides insight into potential therapeutic strategies for the control of arterivirus infection. - Source: PubMed
Publication date: 2026/05/19
Zhou BingqianChen KeweiLiang HaibingQi TingGuo XingWen Yong-JunDu ChengWang Xiaojun