In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Q: Infectious bronchitis virus (IBV) infection has been a major threat to the poultry industry worldwide. Current commercially available ELISA kits detect group-specific antibodies; however, to understand the status of field infection, a monoclonal antibody (mAb) blocking ELISA (b-ELISA) against local IBVs was developed. The selected mAb showed specificity to Taiwan IBV strains but had no cross-reactivity with the vaccine strain H120. Using the hemagglutination inhibition (HI) test as a standard, the cut-off value, sensitivity, and specificity of a b-ELISA using this mAb were evaluated in 390 field samples. The typespecificity of detection was validated using a panel of chicken hyperimmune sera. The results showed that the b-ELISA demonstrated high sensitivity (98.0%) and specificity (97.2%) of detection. The agreement between the results of the b-ELISA and the HI test was statistically significant (Kappa = 0.95), and there was no significant difference between these two methods (McNemar p = 0.72). The b-ELISA specifically detected Taiwan IBV serotypes but not three non-Taiwan IBV serotypes nor sera against other avian pathogens. This b-ELISA provides type-specific antibody detection of local IBV strains. It has the potential to serve as a rapid and reliable diagnostic method for IBV clinical infections in the field in Taiwan.

A: A type-specific blocking ELISA for the detection of infectious bronchitis virus antibody
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Q: All coronaviruses (CoVs), including the causative agent of severe acute respiratory syndrome (SARS), encode a nucleocapsid (N) protein that harbors two independent RNA binding domains of known structure, but poorly characterized RNA binding properties. We show here that the Nterminal domain (NTD) of N protein from mouse hepatitis virus (MHV), a virus most closely related to SARS-CoV, employs aromatic amino acidnucleobase stacking interactions with a triple adenosine motif to mediate high-affinity binding to single-stranded RNAs containing the transcriptional regulatory sequence (TRS) or its complement (cTRS). Stoichiometric NTD fully unwinds a TRS-cTRS duplex that mimics a transiently formed transcription intermediate in viral subgenomic RNA synthesis. Mutation of the solvent-exposed Y127, positioned on the β-platform surface of our 1.75 Å structure, binds the TRS far less tightly and is severely crippled in its RNA unwinding activity. In contrast, the C-terminal domain (CTD) exhibits no RNA unwinding activity. Viruses harboring Y127A N mutation are strongly selected against and Y127A N does not support an accessory function in MHV replication. We propose that the helix melting activity of the coronavirus N protein NTD plays a critical accessory role in subgenomic RNA synthesis and other processes requiring RNA remodeling.

A: Coronavirus N Protein N-Terminal Domain (NTD) Specifically Binds the Transcriptional Regulatory Sequence (TRS) and Melts TRS-cTRS RNA Duplexes
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Q: Arenaviruses cause severe diseases in humans but establish asymptomatic, lifelong infections in rodent reservoirs. Persistently-infected rodents harbor high levels of defective interfering (DI) particles, which are thought to be important for establishing persistence and mitigating virus-induced cytopathic effect. Little is known about what drives the production of DI particles. We show that neither the PPXY late domain encoded within the lymphocytic choriomeningitis virus (LCMV) matrix protein nor a functional endosomal sorting complex transport (ESCRT) pathway is absolutely required for the generation of standard infectious virus particles. In contrast, DI particle release critically requires the PPXY late domain and is ESCRT-dependent. Additionally, the terminal tyrosine in the PPXY motif is reversibly phosphorylated and our findings indicate that this posttranslational modification may regulate DI particle formation. Thus we have uncovered a new role for the PPXY late domain and a possible mechanism for its regulation. Arenaviruses cause severe and often fatal diseases in humans yet typically establish lifelong, asymptomatic infections in their rodent reservoirs. Several families of enveloped RNA viruses, including the arenaviruses, encode short amino acid motifs, called late domains, to hijack host proteins in the endosomal sorting complex required for transport (ESCRT) to drive the release of virus particles from the host cell's outer membrane. Many late domain-containing viruses produce defective interfering (DI) particles in addition to standard, infectious virus. DI particles cannot self-replicate but interfere with the production of infectious virus and mitigate virus-induced cytopathic effect. Arenaviruses such as PLOS Pathogens | lymphocytic choriomeningitis virus (LCMV) generate high levels of DI particles, yet, the mechanism that drives their formation is not known. We show that LCMV's only encoded late domain, PPXY, and a functional ESCRT pathway are critical for DI particle production, but in contrast, are not absolutely required for infectious virus production. We also demonstrate that the LCMV PPXY late domain is phosphorylated and that this modification may regulate DI particle production. In summary, we have discovered a new and unexpected role for a viral late domain in selectively driving the production of DI particles independently of standard infectious virus particles. Arenaviruses are a family of rodent-borne viruses with a worldwide distribution. These viruses typically establish persistent, asymptomatic infections in rodent reservoir species [1]. In contrast, arenaviruses cause severe and often fatal diseases in humans. Several arenaviruses, including Lassa virus and Junín virus, cause hemorrhagic fever syndromes whereas infection with the prototypic arenavirus, lymphocytic choriomeningitis virus (LCMV), can lead to aseptic meningitis in immunocompetent individuals, high lethality in immunocompromised individuals, or severe birth defects in the developing fetus [2,3]. U.S. Food and Drug Administration-approved vaccines do not exist for the prevention of arenavirus infection and effective antiviral therapies have been limited to the use of ribavirin for Lassa virus [4] or immune plasma for Junín virus [5] . Arenaviruses are enveloped viruses with a single-stranded, bi-segmented RNA genome that encodes four proteins in an ambisense manner. The small (S) segment encodes the nucleoprotein (NP) and glycoprotein (GP) while the large (L) segment encodes the RNAdependent RNA polymerase (L) and the matrix protein (Z) [6] . Arenaviruses enter cells via receptor-mediated endocytosis [7], undergo genomic replication and transcription in the cytoplasm [6], and assemble and bud new particles at the plasma membrane [8] . The Z protein, which lines the luminal side of the viral membrane, is responsible for a number of critical functions in the virus life cycle, including driving the process of viral particle assembly and budding [9] . Accordingly, Z can form virus-like particles (VLPs) in the absence of other viral proteins and is thought to be both necessary and sufficient for driving the budding process [10, 11] . Several VLP-based studies indicate that Z drives viral particle release by virtue of one or more encoded viral late domain(s) (P(S/T)AP, YXXL, and/or PPXY), which can recruit proteins from the cellular endosomal sorting complex required for transport (ESCRT) pathway [10] [11] [12] . ESCRT machinery is required for most cellular membrane scission events that result in separation away from the cytosol including multivesicular body formation and cellular abscission [13] [14] [15] . Many enveloped viruses are known to hijack cellular ESCRT machinery via their late domains to complete the final membrane scission step required for virions to bud from host membranes (for review see [16] ). Viruses from diverse families, including arenaviruses, produce defective interfering (DI) particles in addition to standard, infectious virus during the normal course of infection [17] . DI particles are largely similar to standard virus particles in their appearance and viral protein content but cannot self-replicate, and interfere with the production of homologous standard virus [17] . In many cases, the primary difference between DI particles and standard virus is thought to be the presence of deletions in the viral genome [18] . With regard to LCMV, small deletions in the terminal untranslated regions of genomic and antigenomic RNAs have been PPXY Late Domain Drives the Release of LCMV DI Particles PLOS Pathogens |

A:
The Lymphocytic Choriomeningitis Virus Matrix Protein PPXY Late Domain Drives the Production of Defective Interfering Particles
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