instruction:
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.
question:
The purpose of this study was to compare the biochemical and biological properties of nonstructural protein (nsp) 15 among mouse hepatitis virus (MHV), severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) in virus-infected and ectopically expressed cells. In virus-infected cells, MHV nsp15 distributed unevenly throughout the cytoplasm but predominantly in the perinuclear region. When expressed as N-terminal enhanced green fluorescence protein (EGFP) fusion, it predominantly formed speckles in the cytoplasm. In contrast, SARS-CoV and TGEV EGFP-nsp15s distributed smoothly in the whole cell and did not form speckles. Deletion mapping experiments identified two domains responsible for the speckle formation in MHV EGFP-nsp15: Domain I (aa101-150) and Domain III (aa301-374). Interestingly, Domain II (aa151-250) had an inhibitory effect on Domain IIIbut not on Domain I-mediated speckle formation. Expression of a small (35aa) sequence in Domain III alone was sufficient to form speckles for all 3 viral nsp15s. However, addition of surrounding sequences in Domain III abolished the speckle formation for TGEV nsp15 but not for MHV and SARS-CoV nsp15s. Further domain swapping experiments uncovered additional speckle-inducing and -suppressive elements in nsp15s of SARS-CoV and TGEV. Homotypic interaction involving Domain III of MHV nsp15 was further demonstrated biochemically. Moreover, the biological functions of the expressed nsp15s were assessed in MHV-infected cells. It was found that the effects of EGFP-nsp15s on MHV replication were both virus species-and nsp15 domain-dependent. Collectively these results thus underscore the differential biochemical and biological functions among the nsp15s of MHV, TGEV and SARS-CoV in host cells.
answer:
Comparative in vivo analysis of the nsp15 endoribonuclease of murine, porcine and severe acute respiratory syndrome coronaviruses


question:
Objectives: We compared the expelled air dispersion distances during coughing from a human patient simulator (HPS) lying at 45u with and without wearing a surgical mask or N95 mask in a negative pressure isolation room. Methods: Airflow was marked with intrapulmonary smoke. Coughing bouts were generated by short bursts of oxygen flow at 650, 320, and 220L/min to simulate normal, mild and poor coughing efforts, respectively. The coughing jet was revealed by laser light-sheet and images were captured by high definition video. Smoke concentration in the plume was estimated from the light scattered by smoke particles. Significant exposure was arbitrarily defined where there was $ 20% of normalized smoke concentration. Results: During normal cough, expelled air dispersion distances were 68, 30 and 15 cm along the median sagittal plane when the HPS wore no mask, a surgical mask and a N95 mask, respectively. In moderate lung injury, the corresponding air dispersion distances for mild coughing efforts were reduced to 55, 27 and 14 cm, respectively, p , 0.001. The distances were reduced to 30, 24 and 12 cm, respectively during poor coughing effort as in severe lung injury. Lateral dispersion distances during normal cough were 0, 28 and 15 cm when the HPS wore no mask, a surgical mask and a N95 mask, respectively. Conclusions: Normal cough produced a turbulent jet about 0.7 m towards the end of the bed from the recumbent subject. N95 mask was more effective than surgical mask in preventing expelled air leakage during coughing but there was still significant sideway leakage.
answer:
Exhaled Air Dispersion during Coughing with and without Wearing a Surgical or N95 Mask


question:
Ebolaviruses are non-segmented, negative-sense RNA viruses (NNSVs) within the order 19 Mononegavirales that possess the multifunctional virion protein 35 (VP35), a major determinant 20 of virulence and pathogenesis that is indispensable for viral replication and host innate immune 21 evasion. VP35 is functionally equivalent to the phosphoprotein (P) of other mononegaviruses 22 such as rhabdoviruses and paramyxoviruses. Phosphorylation of the P protein is universally 23 regarded as functionally important however, a regulatory role(s) of phosphorylation on VP35 24 function remains unexplored. Here, we identified a highly conserved Ser129 residue near the 25 homo-oligomerization coiled coil motif, which is essential for VP35 functions. Affinity-purification 26 MS followed by post-translational modification (PTM) analysis predicted phosphorylation of 27 Ser129. Co-immunoprecipitation, cross-linking, and biochemical characterization studies 28 revealed a moderately decreased capacity of VP35-S129A to oligomerize. Functional analysis 29 showed that Ser-to-Ala substitution of Ebola virus (EBOV) VP35 did not affect IFN inhibitory 30 activity but nearly abolished EBOV minigenome activity. Further coimmunoprecipitation studies 31 demonstrated a lost interaction between VP35-S129A and the amino terminus of the viral 32 polymerase but not between viral nucleoprotein (NP) or VP35-WT. Taken together, our findings 33 provide evidence that phosphorylation modulates VP35 function, supporting VP35 as a NNSV P 34 protein and providing a potentially valuable therapeutic target. 35 Importance 36 Ebola virus (EBOV) can cause severe disease in humans. The 2013-2016 West African 37 epidemic and the two recent outbreaks in the Democratic Republic of the Congo underscore the 38 urgent need for effective countermeasures, which remain lacking. A better understanding of 39 EBOV biology and the modulation of multifunctional viral proteins is desperately needed to 40 develop improved therapeutics. We provide evidence here that function of virion protein 35 41 (VP35) is modulated by phosphorylation of Ser129, a conserved residue among other 42 ebolavirus species. These findings shed light on EBOV biology and present a potential target for 43 broad acting anti-ebolavirus therapeutics. 44 45 46 47 48 49
answer:

Mutation of Ebola virus VP35 Ser129 uncouples interferon antagonist and replication functions