TASK DEFINITION: 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.
PROBLEM: Rift Valley fever virus (RVFV) (genus Phlebovirus, family Bunyaviridae) is a negative-stranded RNA virus with a tripartite genome. RVFV is transmitted by mosquitoes and causes fever and severe hemorrhagic illness among humans, and fever and high rates of abortions in livestock. A nonstructural RVFV NSs protein inhibits the transcription of host mRNAs, including interferon-b mRNA, and is a major virulence factor. The present study explored a novel function of the RVFV NSs protein by testing the replication of RVFV lacking the NSs gene in the presence of actinomycin D (ActD) or a-amanitin, both of which served as a surrogate of the host mRNA synthesis suppression function of the NSs. In the presence of the hosttranscriptional inhibitors, the replication of RVFV lacking the NSs protein, but not that carrying NSs, induced doublestranded RNA-dependent protein kinase (PKR)-mediated eukaryotic initiation factor (eIF)2a phosphorylation, leading to the suppression of host and viral protein translation. RVFV NSs promoted post-transcriptional downregulation of PKR early in the course of the infection and suppressed the phosphorylated eIF2a accumulation. These data suggested that a combination of RVFV replication and NSs-induced host transcriptional suppression induces PKR-mediated eIF2a phosphorylation, while the NSs facilitates efficient viral translation by downregulating PKR and inhibiting PKR-mediated eIF2a phosphorylation. Thus, the two distinct functions of the NSs, i.e., the suppression of host transcription, including that of type I interferon mRNAs, and the downregulation of PKR, work together to prevent host innate antiviral functions, allowing efficient replication and survival of RVFV in infected mammalian hosts.

SOLUTION: Rift Valley Fever Virus NSs Protein Promotes Post-Transcriptional Downregulation of Protein Kinase PKR and Inhibits eIF2a Phosphorylation

PROBLEM: Coronavirus particles serve three fundamentally important functions in infection. The virion provides the means to deliver the viral genome across the plasma membrane of a host cell. The virion is also a means of escape for newly synthesized genomes. Lastly, the virion is a durable vessel that protects the genome on its journey between cells. This review summarizes the available X-ray crystallography, NMR, and cryoelectron microscopy structural data for coronavirus structural proteins, and looks at the role of each of the major structural proteins in virus entry and assembly. The potential wider conservation of the nucleoprotein fold identified in the Arteriviridae and Coronaviridae families and a speculative model for the evolution of corona-like virus architecture are discussed.

SOLUTION: Supramolecular Architecture of the Coronavirus Particle

PROBLEM: This article examines the history of dog mess in Paris, from its 'discovery' in the late 1920s to the management regime of the early twenty-first century. Mayor Jacques Chirac's anti-excrement campaigns in the 1980s are a particular focus. Situating the meaning and management of dog mess within histories of public hygiene and disgust, and mobilising insights from work on public hygiene, biopolitics and governmentality, this article shows how Chirac's attempt to produce self-regulating and responsible dog owners through education failed to persuade them to overcome their disgust at their pets' excrement. Fining alongside education proved a more effective management strategy. The history of dog mess in Paris highlights the biopolitical problems raised by animal excrement decades after the apogee of the public hygiene movement, and shows how human-animal partnerships expose the limits of governmentality approaches to public hygiene and neo-liberal urban governance.

SOLUTION:
Combating Canine 'Visiting Cards': Public Hygiene and the Management of Dog Mess in Paris since the 1920s