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10.1371/journal.ppat.1009500 http://scihub22266oqcxt.onion/10.1371/journal.ppat.1009500 33886690!8061995!33886690     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33886690&cmd=llinks): Failed to open stream: HTTP request failed! 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The SARS-CoV-2 and other human coronavirus spike proteins are fine-tuned towards temperature and proteases of the human airways |pdf=|usr=}}{{33886690}} gab.com Text The SARS-CoV-2 and other human coronavirus spike proteins are fine-tuned towards temperature and proteases of the human airways JO: PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=33886690 #FOAvip The high transmissibility of SARS-CoV-2 is related to abundant replication in the upper airways, which is not observed for the other highly pathogenic coronaviruses SARS-CoV and MERS-CoV. We here reveal features of the coronavirus spike (S) protein, which optimize the virus towards the human respiratory tract. First, the S proteins exhibit an intrinsic temperature preference, corresponding with the temperature of the upper or lower airways. Pseudoviruses bearing the SARS-CoV-2 spike (SARS-2-S) were more infectious when produced at 33 degrees C instead of 37 degrees C, a property shared with the S protein of HCoV-229E, a common cold coronavirus. In contrast, the S proteins of SARS-CoV and MERS-CoV favored 37 degrees C, in accordance with virus preference for the lower airways. Next, SARS-2-S-driven entry was efficiently activated by not only TMPRSS2, but also the TMPRSS13 protease, thus broadening the cell tropism of SARS-CoV-2. Both proteases proved relevant in the context of authentic virus replication. TMPRSS13 appeared an effective spike activator for the virulent coronaviruses but not the low pathogenic HCoV-229E virus. Activation of SARS-2-S by these surface proteases requires processing of the S1/S2 cleavage loop, in which both the furin recognition motif and extended loop length proved critical. Conversely, entry of loop deletion mutants is significantly increased in cathepsin-rich cells. Finally, we demonstrate that the D614G mutation increases SARS-CoV-2 stability, particularly at 37 degrees C, and, enhances its use of the cathepsin L pathway. This indicates a link between S protein stability and usage of this alternative route for virus entry. Since these spike properties may promote virus spread, they potentially explain why the spike-G614 variant has replaced the early D614 variant to become globally predominant. Collectively, our findings reveal adaptive mechanisms whereby the coronavirus spike protein is adjusted to match the temperature and protease conditions of the airways, to enhance virus transmission and pathology. Twit Text FOAVip The SARS-CoV-2 and other human coronavirus spike proteins are fine-tuned towards temperature and proteases of the human airways ????PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=33886690 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33886690 #FOAvip English Wikipedia <ref>{{Cite pmid|33886690}}</ref> The SARS-CoV-2 and other human coronavirus spike proteins are fine-tuned towards temperature and proteases of the human airways #MMPMID33886690 Laporte M; Raeymaekers V; Van Berwaer R; Vandeput J; Marchand-Casas I; Thibaut HJ; Van Looveren D; Martens K; Hoffmann M; Maes P; Pohlmann S; Naesens L; Stevaert A PLoS Pathog 2021[Apr]; 17 (4): e1009500 PMID33886690show ga The high transmissibility of SARS-CoV-2 is related to abundant replication in the upper airways, which is not observed for the other highly pathogenic coronaviruses SARS-CoV and MERS-CoV. We here reveal features of the coronavirus spike (S) protein, which optimize the virus towards the human respiratory tract. First, the S proteins exhibit an intrinsic temperature preference, corresponding with the temperature of the upper or lower airways. Pseudoviruses bearing the SARS-CoV-2 spike (SARS-2-S) were more infectious when produced at 33 degrees C instead of 37 degrees C, a property shared with the S protein of HCoV-229E, a common cold coronavirus. In contrast, the S proteins of SARS-CoV and MERS-CoV favored 37 degrees C, in accordance with virus preference for the lower airways. Next, SARS-2-S-driven entry was efficiently activated by not only TMPRSS2, but also the TMPRSS13 protease, thus broadening the cell tropism of SARS-CoV-2. Both proteases proved relevant in the context of authentic virus replication. TMPRSS13 appeared an effective spike activator for the virulent coronaviruses but not the low pathogenic HCoV-229E virus. Activation of SARS-2-S by these surface proteases requires processing of the S1/S2 cleavage loop, in which both the furin recognition motif and extended loop length proved critical. Conversely, entry of loop deletion mutants is significantly increased in cathepsin-rich cells. Finally, we demonstrate that the D614G mutation increases SARS-CoV-2 stability, particularly at 37 degrees C, and, enhances its use of the cathepsin L pathway. This indicates a link between S protein stability and usage of this alternative route for virus entry. Since these spike properties may promote virus spread, they potentially explain why the spike-G614 variant has replaced the early D614 variant to become globally predominant. Collectively, our findings reveal adaptive mechanisms whereby the coronavirus spike protein is adjusted to match the temperature and protease conditions of the airways, to enhance virus transmission and pathology. |COVID-19/*metabolism/transmission[MESH] |Coronavirus 229E, Human/metabolism[MESH] |Furin/metabolism[MESH] |Humans[MESH] |Membrane Proteins/metabolism[MESH] |Middle East Respiratory Syndrome Coronavirus/metabolism[MESH] |Peptide Hydrolases/metabolism[MESH] |Respiratory System/*metabolism/*virology[MESH] |SARS-CoV-2/*metabolism[MESH] |Serine Endopeptidases/metabolism[MESH] |Spike Glycoprotein, Coronavirus/genetics/*metabolism[MESH] |Temperature[MESH] |Virus Internalization[MESH]The SARS-CoV-2 and other human coronavirus spike proteins are fine-tun(epmc).pdf DeepDyve Pubget Overpricing