In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".

Input: Consider Input: Paragraph: The present study was undertaken to evaluate chikungunya virus (CHIKV) proteins for RNAi suppressor activity. We systematically analyzed all nine CHIKV proteins for RNAi suppressor activity using Sf21 RNAi sensor cell line based assay. Two non-structural proteins, namely, nsP2 and nsP3 were found to exhibit RNAi suppressor activity. We further validated the findings in natural hosts, namely in Aedes and in mammalian cell lines and further through EMSA and Agrobacterium infiltration in GFP silenced transgenic tobacco plants. Domains responsible for maximum RNAi suppressor activity were also identified within these proteins. RNA binding motifs in these domains were identified and their participation in RNAi suppression evaluated using site directed mutagenesis. Sequence alignment of these motifs across all species of known alphaviruses revealed conservation of these motifs emphasizing on a similar role of action in other species of alphaviruses as well. Further validation of RNAi suppressor activity of these proteins awaits establishment of specific virus infection models. RNA interference (RNAi) is a conserved evolutionary mechanism designed to impart an antiviral defence system across organisms ranging from plants, fungi, arthropods and nematodes 1-4 . The phenomenon, triggered by the production of double stranded RNA (dsRNA) by the pathogen upon infection, leads to the activation of the RNA interference silencing complex (RISC) by loading of dsRNA/siRNA into the complex ultimately leading to cleavage of the viral RNA 5,6,7 . Several components of RISC participate in the cleavage, most important being ribonuclease III Dicer (DCR) and Argonaute protein (AGO). Dicer acts on dsRNA to generate small RNA (sRNA) that are loaded into the AGO, resulting in cleavage 8,9 ; however, some RNAi pathways are independent of Dicer and other components like RNA-dependent RNA polymerase (RdRP) produce short RNA transcripts that directly bind to AGO 10 . Similarly, much is now known about the Piwi pathway that is specifically active in the germline 11 . In response to RNAi in plants and insects, viruses infecting these systems utilise some of their own proteins/sequence elements that counteract the antiviral RNAi pathway 12 . These viral suppressors of RNAi (VSRs) act through different mechanisms, either by binding to long dsRNA and protecting them from Dicer 7,13 or short RNAs 14 or through multi-mode mechanisms 15,16 . Recently it has been shown that some viruses encode host-specific VSRs due to co-evolution of the virus and the host, emphasising on the importance of analysing suppressor activity in relevant host 17 . Amongst medically important pathogenic viruses, arboviruses form an important subset of viruses due to the complexity of their host preferences 18 . These viruses, mainly constituted by genera flavivirus and alphavirus, 
 Title: Analysis of chikungunya virus proteins reveals that non-structural proteins nsP2 and nsP3 exhibit RNA interference (RNAi) suppressor activity OPEN

Output: False


Input: Consider Input: Paragraph: Seasonal hyperacute panuveitis (SHAPU) is a potentially blinding ocular disease occurring in Nepal that principally affects young children. Random amplification of partially purified vitreous fluid (VF)-derived nucleic acid revealed the presence of human anelloviruses in VF of SHAPU patients. In a comparative study of patients with different ocular pathologies, SHAPU patients were at highest risk of harboring anelloviruses in their eyes. The majority of SHAPU patients had multiple anelloviruses in their VF. The ocular anellovirus load in SHAPU and non-SHAPU patients did not differ and no SHAPU-specific anellovirus variant was detected. Analysis of paired serum and VF samples from SHAPU and non-SHAPU patients showed that the anellovirus detected in VF samples most likely originated from the systemic viral pool during viremia, potentially through breakdown of the blood-ocular barrier. The detection of anelloviruses in VF samples of uveitis patients, profoundly so in SHAPU patients, is imperative and warrants elucidation of its clinical significance. 
 Title: High Prevalence of Anelloviruses in Vitreous Fluid of Children With Seasonal Hyperacute Panuveitis

Output: True


Input: Consider Input: Paragraph: Mammalian cells recognize virus-derived nucleic acids using a defined set of intracellular sensors including the DNA sensors cyclic GMP-AMP (cGAMP) synthase (cGAS) and interferon gamma (IFNγ)-inducible protein 16 (IFI16) as well as viral RNA receptors of the retinoic acid-inducible gene I (RIG-I)-like receptor (RLR) family. Following innate immune recognition, these sensors launch an immune response that is characterized by the transcriptional upregulation of many antiviral molecules, including proinflammatory cytokines, chemokines, and IFN-stimulated genes. Recent studies have demonstrated that the signal transduction initiated by these sensors is sophisticatedly regulated by post-translational modifications (PTMs) resulting in a robust yet 'tunable' cytokine response to maintain immune homeostasis. Here we summarize recent advances in our understanding of how PTMs and regulatory enzymes control the signaling activity of RLRs, cGAS, and IFI16 as well as their proximal adaptor proteins. [1, 5] . In vitro studies and studies in mice demonstrated that recognition of viral RNA PAMPs by RIG-I and MDA5 confers resistance to a wide spectrum of RNA viruses, including flaviviruses, influenza viruses, rhabdoviruses, paramyxoviruses, and picornaviruses. In addition, RLRs are involved in detecting DNA virus infections, a mechanism that, in the case of RIG-I, relies on the recognition of RNA polymerase IIIgenerated viral transcripts, at least for some DNA viruses (e.g., adenoviruses, Epstein-Barr virus). RIG-I and MDA5 are DExD/H-box-containing RNA helicases with similar structures: both possess two N-terminal caspase activation and recruitment domains (CARDs) for initiating downstream signaling and a central helicase domain and carboxy-terminal domain (CTD) [in the case of RIG-I also called the 'repressor domain' (RD)], which are both required for RNA binding. Although they recognize different ligands, RIG-I and MDA5 interact with a common adaptor protein, mitochondrial antiviral signaling protein (MAVS) (also known as IPS-1, CARDIF, or VISA) which serves as a scaffold for protein complex assembly at the mitochondria and mitochondria-associated membranes (MAMs) to trigger an antiviral program [6] . It has been demonstrated that the interaction of RIG-I with the chaperone protein 14-3-3ε mediates RIG-I translocation from the cytosol to mitochondria and MAMs to initiate signaling [7] . MAVS then recruits the IKK-related serine/threonine kinases TANK-binding kinase 1 (TBK1) and IKKε, which phosphorylate and activate IRF3 or IRF7. Furthermore, the tripartite IKKα-IKKβ-IKKγ complex is activated by MAVS, ultimately resulting in nuclear factor kappa B (NF-κB) activation. NF-κB and IRFs then translocate into the nucleus and cooperatively induce the gene expression of type I IFNs (IFNα subtypes and IFNβ), proinflammatory cytokines (e.g., tumor necrosis factor superfamily proteins and interleukins) and chemokines, for the initiation of the antiviral response. More recently, cGAS and IFI16 have been identified as intracellular DNA sensors that mediate a type I IFN response via the recruitment and activation of their shared adaptor protein stimulator of IFN genes (STING) (also known as MITA or TMEM173) [8-10]. Following recognition of viral dsDNA -derived from either a DNA virus (e.g., herpesviruses) or retroviral infection -cytoplasmic cGAS catalyzes the formation of the second messenger cGAMP, which binds to and activates STING. The binding of cGAMP to STING results in the translocation of the adaptor protein from the endoplasmic reticulum to the Golgi and perinuclear sites. Activated STING dimerizes and binds to TBK1, resulting in IRF3 activation and IFNα/β gene expression. The sensor IFI16 is reportedly localized in both the cytoplasm and the nucleus and detects viral dsDNA via its hematopoietic expression, IFN-inducible nature, and nuclear localization (HIN) domain followed by signaling to STING to initiate an IFN-mediated antiviral response. In addition to its ability to elicit type I IFN induction, IFI16 also leads to IL-1β secretion via activation of caspase 1dependent inflammasomes (reviewed in [4]). PTMs are key regulatory events in which proteins are enzymatically modified to reversibly modulate the activity, subcellular localization, conformation, and/or protein-protein interactions of the target protein. Thus, PTMs are crucial for the dynamic regulation of signal transduction pathways. Each step of the intracellular pathogen sensing pathways is regulated by a complex network of PTMs resulting in a controlled yet effective antiviral Chiang and Gack 
 Title: Post-translational Control of Intracellular Pathogen Sensing Pathways HHS Public Access


Output: False