ABSTRACT
Recently, because of the outbreak of COVID‐19, the demand for various types of filter elements in protective materials has increased globally. Furthermore, new requirements for the filtration performance of PM2.5 liquid (oil) particles have been put forward. In this work, Superhydrophobic and superoleophobic composite nanofibers with excellent filtration capacity for oil and salt particles are developed through the modification of polyacrylonitrile (PAN) by fluoro‐polyurethane (FPU) doping. The results show that the PAN/FPU composite nanofibers doped with 9 wt% FPU has a uniform fiber morphology with a diameter of 240 ± 30 nm. Compared to the pure PAN nanofibers, the water‐based contact angle of PAN/FPU increases from 90 ± 5° to 151 ± 5°, and the oil‐based contact angle increases from 58 ± 2° to 152 ± 3°. Importantly, at a high flow rate of 95 L min−1, the filtration efficiency of the PAN/FPU nanofiber membrane for 0.3 µm oil particles increases from 92 ± 1% to 99.2 ± 0.1%. After cyclic loading, the filtration efficiency of 0.3 µm oil particles remains above 98%. Meanwhile, the filtration efficiency for 0.3 µm salt particles remains at 98.23 ± 0.1%. The PAN/FPU nanofiber membrane developed in this work is effective in applications and has good market prospects as a protective filtration material. [ABSTRACT FROM AUTHOR] Copyright of Macromolecular Materials & Engineering is the property of John Wiley & Sons, Inc. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
ABSTRACT
SARS-CoV-2 is the causative agent for the COVID-19 pandemic and there is an urgent need to understand the cellular response to SARS-CoV-2 infection. Beclin-1 is an essential scaffold autophagy protein that forms two distinct subcomplexes with modulators Atg14 and UVRAG, responsible for autophagosome formation and maturation, respectively. In the present study, we found that SARS-CoV-2 infection triggers an incomplete autophagy response, elevated autophagosome formation but impaired autophagosome maturation, and declined autophagy by genetic knockout of essential autophagic genes reduces SARS-CoV-2 replication efficiency. By screening 28 viral proteins of SARS-CoV-2, we demonstrated that expression of ORF3a alone is sufficient to induce incomplete autophagy. Mechanistically, SARS-CoV-2 ORF3a interacts with autophagy regulator UVRAG to facilitate Beclin-1-Vps34-Atg14 complex but selectively inhibit Beclin-1-Vps34-UVRAG complex. Interestingly, although SARS-CoV ORF3a shares 72.7% amino acid identity with the SARS-CoV-2 ORF3a, the former had no effect on cellular autophagy response. Thus, our findings provide the mechanistic evidence of possible takeover of host autophagy machinery by ORF3a to facilitate SARS-CoV-2 replication and raises the possibility of targeting the autophagic pathway for the treatment of COVID-19.
Subject(s)
COVID-19ABSTRACT
SARS-CoV-2 is the causative agent for the COVID-19 pandemic and there is an urgent need to understand the cellular response to SARS-CoV-2 infection. Beclin-1 is an essential scaffold autophagy protein that forms two distinct subcomplexes with modulators Atg14 and UVRAG, responsible for autophagosome formation and maturation, respectively. In the present study, we found that SARS-CoV-2 infection triggers an incomplete autophagy response, elevated autophagosome formation but impaired autophagosome maturation, and declined autophagy by genetic knockout of essential autophagic genes reduces SARS-CoV-2 replication efficiency. By screening 28 viral proteins of SARS-CoV-2, we demonstrated that expression of ORF3a alone is sufficient to induce incomplete autophagy. Mechanistically, SARS-CoV-2 ORF3a interacts with autophagy regulator UVRAG to facilitate Beclin-1-Vps34-Atg14 complex but selectively inhibit Beclin-1-Vps34-UVRAG complex. Interestingly, although SARS-CoV ORF3a shares 72.7% amino acid identity with the SARS-CoV-2 ORF3a, the former had no effect on cellular autophagy response. Thus, our findings provide the mechanistic evidence of possible takeover of host autophagy machinery by ORF3a to facilitate SARS-CoV-2 replication and raises the possibility of targeting the autophagic pathway for the treatment of COVID-19.