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.

[EX Q]: Bioaerosols exposure can lead to many adverse health effects and even result in death if highly infectious agents involved. Apparently, there is a great need for rapid detection of bioaerosols, for which air sampling often is the first critical step. However, currently available samplers often either require an external power and/or with low sampling flow rate, thus falling short of providing a practical solution when response time is of great concern. Here, we have designed and evaluated a new portable high volume bioaerosol sampler named as HighBioTrap through optimizing its operating parameters. The sampler was operated at a sampling flow rate of 1200 L/min, with an impaction velocity of about 10.2 m/s (S/W = 1.5, T/ W = 1), while the weight of the sampler is about 1.9 kg. The performances of the HighBioTrap sampler were tested both in lab controlled and natural environments (outdoor and indoor environments in a university building) along with the reference sampler-the BioStage impactor using aerosolized Polystyrene (PS) uniform microspheres of various sizes, aerosolized bacteria and also ambient air particles. The microbial community structures of collected culturable bacterial aerosol particles both by the HighBioTrap and the BioStage impactor in the natural environments were analyzed using gene sequence method. Experimental results with PS particles showed the HighBioTrap has a cutoff size of~2 µm. The widely used impactor design equation was found to be not applicable for predicting the performance of the HighBioTrap due to its large Reynolds number. When sampling aerosolized individual Pseudomonas fluorescens and Bacillus subtilis bacterial particles, the HighBioTrap had physical collection efficiencies of 10% and 20%, respectively. Despite the higher desiccation effects introduced by higher flow rate, the HighBioTrap was shown to obtain a higher microbial diversity than the BioStage impactor for both in outdoor and indoor environments given the same sampling time (p < 0.01). Our data also showed that most of the desiccation effects might have occurred between 3 and 5 min of the sampling and an impaction velocity of around 10 m/s might be a close-to-optimal impaction velocity for collecting most environmental bacterial aerosols while maximally preserving their culturability. This work contributes to our understanding of microbial sampling stress (impaction velocity and sampling time), while developing a portable high volume sampler. The HighBioTrap sampler could find its great efficiencies in qualitative microbial aerosol detection and analysis, such as investigation of microbial aerosol diversity for a particular environment, or when the low level of pathogens is present and detection time is of great concern.
[EX A]: A high-flow portable biological aerosol trap (HighBioTrap) for rapid microbial detection

[EX Q]: Quinone-methide triterpenes, celastrol (1), pristimerin (2), tingenone (3), and iguesterin (4) were isolated from Triterygium regelii and dihydrocelastrol (5) was synthesized by hydrogenation under palladium catalyst. Isolated quinone-methide triterpenes (1-4) and 5 were evaluated for SARS-CoV 3CL pro inhibitory activities and showed potent inhibitory activities with IC 50 values of 10.3, 5.5, 9.9, and 2.6 lM, respectively, whereas the corresponding 5 having phenol moiety was observed in low activity (IC 50 = 21.7 lM). As a result, quinone-methide moiety in A-ring and more hydrophobic E-ring assist to exhibit potent activity. Also, all quinone-methide triterpenes 1-4 have proven to be competitive by the kinetic analysis.
[EX A]: SARS-CoV 3CL pro inhibitory effects of quinone-methide triterpenes from Tripterygium regelii

[EX Q]: Synthetic decapeptides (N ¼ 206) covering the entire sequence of mouse liver fumarylacetoacetate hydrolase (FAH) were used to analyze the specificities of the autoantibodies (autoAb) elicited towards this enzyme in mice infected with mouse hepatitis virus (MHV). These autoAb bound mainly to N-and C-terminal FAH peptides, the most reactive sequences being 1e50 and 390e420, respectively. Surprisingly, although FAH sequence 1e50 shares a high degree of homology with various MHV proteins, the C-terminal portion does not. Moreover, whereas the autoAb reacted with homologous peptides surrounding residues 70, 160 and 360, non-similar sequences around residues 130, 210, 240, 250, and 300 were also recognized, indicating that autoAb were not restricted to epitopes with sequence homologies. There was also a lack of correlation between the amount of anti-MHV or anti-FAH antibodies produced and the reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice. Results indicated that the induction of the autoAb is not only related to molecular or structural mimicry, but rather supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger the production of autoAb.
[EX A]:
The peptide specificities of the autoantibodies elicited by mouse hepatitis virus A59