{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T18:24:05Z","timestamp":1778610245989,"version":"3.51.4"},"update-to":[{"DOI":"10.1371\/journal.ppat.1014117","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T00:00:00Z","timestamp":1778544000000}}],"reference-count":93,"publisher":"Public Library of Science (PLoS)","issue":"5","license":[{"start":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T00:00:00Z","timestamp":1777939200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Coronaviruses (CoVs) encode a variety of transmembrane proteins that are translated and processed at the endoplasmic reticulum (ER). Three host ER resident transmembrane proteins, activating transcription factor 6 (ATF6), inositol-requiring enzyme 1 (IRE1), and PKR-like endoplasmic reticulum kinase (PERK), sense the accumulation of unfolded proteins in the ER and initiate the unfolded protein response (UPR) to maintain ER proteostasis. We observed that SARS-CoV-2 Spike broadly activated all three arms of the UPR, whereas the Membrane (M) protein selectively inhibited ATF6. ATF6 has a unique activation mechanism whereby ER stress triggers translocation to the Golgi where ATF6 is processed by resident proteases to release the ATF6-N transcription factor. We observed that M inhibited the stress-induced production of ATF6-N, suggesting that ATF6 failed to engage with Golgi proteases for processing. M also inhibited sterol regulatory element binding protein-2 (SREBP2)-mediated activation of sterol responses and stimulator of interferon response cGAMP interactor 1 (STING)-mediated activation of interferon responses, both of which are activated in the ER and require translocation to the Golgi for interactions that yield transcriptional responses. We observed that M accumulated in the\n                    <jats:italic>cis<\/jats:italic>\n                    -Golgi, and triggered dispersal of the\n                    <jats:italic>trans<\/jats:italic>\n                    -Golgi network (TGN). Using a cargo sorting assay, we determined that ER-to-Golgi cargo trafficking was intact in the presence of M, but cargo accumulated with M in the\n                    <jats:italic>cis<\/jats:italic>\n                    -Golgi and did not proceed further in the secretory pathway. We also observed aberrant cholesterol accumulation at the\n                    <jats:italic>cis<\/jats:italic>\n                    -Golgi with M, consistent with our observation of M association with detergent resistant membranes. Together, these data suggest that CoV M proteins interfere with Golgi architecture and trafficking. Because CoV egress does not require the canonical secretory pathway, this mechanism could allow the virus to selectively interfere with host responses to infection without impeding egress of nascent virions.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1014117","type":"journal-article","created":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T17:38:12Z","timestamp":1778002692000},"page":"e1014117","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Coronavirus M protein disperses the trans-Golgi network and inhibits anterograde protein trafficking in the secretory pathway"],"prefix":"10.1371","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2628-9231","authenticated-orcid":true,"given":"Taylor M.","family":"Caddell","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7358-1331","authenticated-orcid":true,"given":"Rory P.","family":"Mulloy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3764-0218","authenticated-orcid":true,"given":"Jennifer A.","family":"Corcoran","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3667-4595","authenticated-orcid":true,"given":"Eric S.","family":"Pringle","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2794-3722","authenticated-orcid":true,"given":"Craig","family":"McCormick","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2026,5,5]]},"reference":[{"issue":"3","key":"ppat.1014117.ref001","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/s41579-020-00468-6","article-title":"Coronavirus biology and replication: implications for SARS-CoV-2","volume":"19","author":"P V\u2019kovski","year":"2021","journal-title":"Nat Rev Microbiol"},{"issue":"4","key":"ppat.1014117.ref002","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00524-13","article-title":"Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles","volume":"4","author":"MM Angelini","year":"2013","journal-title":"mBio"},{"issue":"9","key":"ppat.1014117.ref003","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.0060226","article-title":"SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum","volume":"6","author":"K Knoops","year":"2008","journal-title":"PLoS Biol"},{"issue":"6","key":"ppat.1014117.ref004","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01658-17","article-title":"Expression and Cleavage of Middle East Respiratory Syndrome Coronavirus nsp3-4 Polyprotein Induce the Formation of Double-Membrane Vesicles That Mimic Those Associated with Coronaviral RNA Replication","volume":"8","author":"D Oudshoorn","year":"2017","journal-title":"mBio"},{"issue":"6","key":"ppat.1014117.ref005","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3000715","article-title":"A unifying structural and functional model of the coronavirus replication organelle: Tracking down RNA synthesis","volume":"18","author":"EJ Snijder","year":"2020","journal-title":"PLoS Biol"},{"issue":"14","key":"ppat.1014117.ref006","doi-asserted-by":"crossref","first-page":"5871","DOI":"10.1073\/pnas.0809524106","article-title":"Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites","volume":"106","author":"S Belouzard","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"42","key":"ppat.1014117.ref007","doi-asserted-by":"crossref","first-page":"15214","DOI":"10.1073\/pnas.1407087111","article-title":"Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein","volume":"111","author":"JK Millet","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1014117.ref008","doi-asserted-by":"crossref","first-page":"100111","DOI":"10.1074\/jbc.RA120.016175","article-title":"The SARS-CoV-2 envelope and membrane proteins modulate maturation and retention of the spike protein, allowing assembly of virus-like particles","volume":"296","author":"B Boson","year":"2021","journal-title":"J Biol Chem"},{"issue":"1","key":"ppat.1014117.ref009","doi-asserted-by":"crossref","first-page":"4399","DOI":"10.1038\/s41467-022-32019-3","article-title":"Structure of SARS-CoV-2 membrane protein essential for virus assembly","volume":"13","author":"Z Zhang","year":"2022","journal-title":"Nat Commun"},{"issue":"10","key":"ppat.1014117.ref010","doi-asserted-by":"crossref","first-page":"6523","DOI":"10.1128\/jvi.68.10.6523-6534.1994","article-title":"Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding","volume":"68","author":"J Klumperman","year":"1994","journal-title":"J Virol"},{"issue":"20","key":"ppat.1014117.ref011","doi-asserted-by":"crossref","first-page":"14094","DOI":"10.1016\/S0021-9258(19)49683-X","article-title":"O-glycosylation of the coronavirus M protein. Differential localization of sialyltransferases in N- and O-linked glycosylation","volume":"267","author":"JK Locker","year":"1992","journal-title":"J Biol Chem"},{"key":"ppat.1014117.ref012","doi-asserted-by":"crossref","first-page":"21911","DOI":"10.1016\/S0021-9258(19)36699-2","article-title":"Membrane assembly of the triple-spanning coronavirus M protein. Individual transmembrane domains show preferred orientation.","volume":"267","author":"JK Locker","year":"1992","journal-title":"Journal of Biological Chemistry"},{"issue":"17","key":"ppat.1014117.ref013","doi-asserted-by":"crossref","first-page":"8127","DOI":"10.1128\/JVI.74.17.8127-8134.2000","article-title":"Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells","volume":"74","author":"K Narayanan","year":"2000","journal-title":"J Virol"},{"issue":"2","key":"ppat.1014117.ref014","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1083\/jcb.131.2.339","article-title":"Envelope glycoprotein interactions in coronavirus assembly","volume":"131","author":"DJ Opstelten","year":"1995","journal-title":"J Cell Biol"},{"issue":"1","key":"ppat.1014117.ref015","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1186\/s12985-019-1182-0","article-title":"Coronavirus envelope protein: current knowledge","volume":"16","author":"D Schoeman","year":"2019","journal-title":"Virol J"},{"issue":"6","key":"ppat.1014117.ref016","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1016\/j.cell.2020.10.039","article-title":"\u03b2-Coronaviruses Use Lysosomes for Egress Instead of the Biosynthetic Secretory Pathway","volume":"183","author":"S Ghosh","year":"2020","journal-title":"Cell"},{"issue":"7","key":"ppat.1014117.ref017","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/nrm2199","article-title":"Signal integration in the endoplasmic reticulum unfolded protein response","volume":"8","author":"D Ron","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"3","key":"ppat.1014117.ref018","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/S1097-2765(03)00105-9","article-title":"An integrated stress response regulates amino acid metabolism and resistance to oxidative stress","volume":"11","author":"HP Harding","year":"2003","journal-title":"Mol Cell"},{"issue":"12","key":"ppat.1014117.ref019","article-title":"Activation of the UPR sensor ATF6\u03b1 is regulated by its redox-dependent dimerization and ER retention by ERp18","volume":"119","author":"OBV Oka","year":"2022","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6","key":"ppat.1014117.ref020","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1016\/S1097-2765(00)00133-7","article-title":"ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs","volume":"6","author":"J Ye","year":"2000","journal-title":"Mol Cell"},{"issue":"1","key":"ppat.1014117.ref021","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1247\/csf.07044","article-title":"ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum","volume":"33","author":"Y Adachi","year":"2008","journal-title":"Cell Struct Funct"},{"issue":"1","key":"ppat.1014117.ref022","first-page":"1","article-title":"A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response","volume":"22","author":"JS Cox","year":"2020","journal-title":"Nat Cell Biol"},{"issue":"24","key":"ppat.1014117.ref023","doi-asserted-by":"crossref","first-page":"2922","DOI":"10.15252\/embj.201490332","article-title":"The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA and controls antibody secretion in plasma cells","volume":"33","author":"J Jurkin","year":"2014","journal-title":"EMBO J"},{"issue":"7","key":"ppat.1014117.ref024","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/S0092-8674(01)00611-0","article-title":"XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor","volume":"107","author":"H Yoshida","year":"2001","journal-title":"Cell"},{"key":"ppat.1014117.ref025","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1101\/gad.964702","article-title":"Ire1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response","volume":"16","author":"K Lee","year":"2002","journal-title":"Genes Dev"},{"key":"ppat.1014117.ref026","doi-asserted-by":"crossref","unstructured":"Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. 1999.","DOI":"10.1038\/16729"},{"issue":"11","key":"ppat.1014117.ref027","doi-asserted-by":"crossref","first-page":"3269","DOI":"10.31557\/APJCP.2019.20.11.3269","article-title":"Prevalence of Human Papilloma Virus Sub Genotypes following Head and Neck Squamous Cell Carcinomas in Asian Continent, A Systematic Review Article","volume":"20","author":"N Bukhari","year":"2019","journal-title":"Asian Pac J Cancer Prev"},{"key":"ppat.1014117.ref028","unstructured":"Krishnamoorthy T, Pavitt GD, Zhang F, Dever TE, Hinnebusch AG. Tight Binding of the Phosphorylated a Subunit of Initiation Factor 2 (eIF2a) to the Regulatory Subunits of Guanine Nucleotide Exchange Factor eIF2B Is Required for Inhibition of Translation Initiation."},{"issue":"31","key":"ppat.1014117.ref029","doi-asserted-by":"crossref","first-page":"11269","DOI":"10.1073\/pnas.0400541101","article-title":"Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells","volume":"101","author":"KM Vattem","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"14","key":"ppat.1014117.ref030","doi-asserted-by":"crossref","first-page":"8124","DOI":"10.1128\/JVI.00626-13","article-title":"Upregulation of CHOP\/GADD153 during coronavirus infectious bronchitis virus infection modulates apoptosis by restricting activation of the extracellular signal-regulated kinase pathway","volume":"87","author":"Y Liao","year":"2013","journal-title":"J Virol"},{"issue":"21","key":"ppat.1014117.ref031","doi-asserted-by":"crossref","first-page":"12752","DOI":"10.1128\/JVI.02138-14","article-title":"The endoplasmic reticulum stress sensor IRE1\u03b1 protects cells from apoptosis induced by the coronavirus infectious bronchitis virus","volume":"88","author":"TS Fung","year":"2014","journal-title":"J Virol"},{"issue":"20","key":"ppat.1014117.ref032","doi-asserted-by":"crossref","first-page":"10981","DOI":"10.1128\/JVI.01033-07","article-title":"The coronavirus spike protein induces endoplasmic reticulum stress and upregulation of intracellular chemokine mRNA concentrations","volume":"81","author":"GA Versteeg","year":"2007","journal-title":"J Virol"},{"issue":"15","key":"ppat.1014117.ref033","article-title":"The PERK Arm of the Unfolded Protein Response Negatively Regulates Transmissible Gastroenteritis Virus Replication by Suppressing Protein Translation and Promoting Type I Interferon Production","volume":"92","author":"M Xue","year":"2018","journal-title":"J Virol"},{"issue":"2","key":"ppat.1014117.ref034","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.virol.2009.09.026","article-title":"A human coronavirus OC43 variant harboring persistence-associated mutations in the S glycoprotein differentially induces the unfolded protein response in human neurons as compared to wild-type virus","volume":"395","author":"DJ Favreau","year":"2009","journal-title":"Virology"},{"issue":"10","key":"ppat.1014117.ref035","doi-asserted-by":"crossref","first-page":"6180","DOI":"10.1128\/JVI.79.10.6180-6193.2005","article-title":"Comparative host gene transcription by microarray analysis early after infection of the Huh7 cell line by severe acute respiratory syndrome coronavirus and human coronavirus 229E","volume":"79","author":"BSF Tang","year":"2005","journal-title":"J Virol"},{"issue":"9","key":"ppat.1014117.ref036","doi-asserted-by":"crossref","first-page":"4492","DOI":"10.1128\/JVI.00017-08","article-title":"Coronavirus infection modulates the unfolded protein response and mediates sustained translational repression","volume":"82","author":"J Bechill","year":"2008","journal-title":"J Virol"},{"issue":"18","key":"ppat.1014117.ref037","doi-asserted-by":"crossref","first-page":"9279","DOI":"10.1128\/JVI.00659-06","article-title":"Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein","volume":"80","author":"C-P Chan","year":"2006","journal-title":"J Virol"},{"issue":"1","key":"ppat.1014117.ref038","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/2045-3701-4-3","article-title":"Comparative analysis of the activation of unfolded protein response by spike proteins of severe acute respiratory syndrome coronavirus and human coronavirus HKU1","volume":"4","author":"K-L Siu","year":"2014","journal-title":"Cell Biosci"},{"issue":"12","key":"ppat.1014117.ref039","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1016\/j.bbagen.2008.07.009","article-title":"A SARS-CoV protein, ORF-6, induces caspase-3 mediated, ER stress and JNK-dependent apoptosis","volume":"1780","author":"Z Ye","year":"2008","journal-title":"Biochim Biophys Acta"},{"issue":"12","key":"ppat.1014117.ref040","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0008342","article-title":"The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor","volume":"4","author":"R Minakshi","year":"2009","journal-title":"PLoS One"},{"issue":"2","key":"ppat.1014117.ref041","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/j.virol.2009.02.021","article-title":"The 8ab protein of SARS-CoV is a luminal ER membrane-associated protein and induces the activation of ATF6","volume":"387","author":"S-C Sung","year":"2009","journal-title":"Virology"},{"issue":"7816","key":"ppat.1014117.ref042","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/s41586-020-2286-9","article-title":"A SARS-CoV-2 protein interaction map reveals targets for drug repurposing","volume":"583","author":"DE Gordon","year":"2020","journal-title":"Nature"},{"issue":"1","key":"ppat.1014117.ref043","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1021\/acs.jproteome.3c00600","article-title":"Expression of SARS-CoV-2 Nonstructural Proteins 3 and 4 Can Tune the Unfolded Protein Response in Cell Culture","volume":"23","author":"JP Davies","year":"2024","journal-title":"J Proteome Res"},{"key":"ppat.1014117.ref044","doi-asserted-by":"crossref","first-page":"7602","DOI":"10.1093\/nar\/gkad483","article-title":"Nsp14 of SARS-CoV-2 inhibits mRNA processing and nuclear export by targeting the nuclear cap-binding complex","volume":"51","author":"J Katahira","year":"2023","journal-title":"Nucleic Acids Research"},{"issue":"19","key":"ppat.1014117.ref045","doi-asserted-by":"crossref","DOI":"10.1016\/j.molcel.2023.09.002","article-title":"Universal features of Nsp1-mediated translational shutdown by coronaviruses","volume":"83","author":"K Schubert","year":"2023","journal-title":"Mol Cell"},{"issue":"6","key":"ppat.1014117.ref046","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2017715118","article-title":"Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation","volume":"118","author":"CP Lapointe","year":"2021","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6","key":"ppat.1014117.ref047","doi-asserted-by":"crossref","DOI":"10.1016\/j.molcel.2020.10.034","article-title":"Nonstructural Protein 1 of SARS-CoV-2 Is a Potent Pathogenicity Factor Redirecting Host Protein Synthesis Machinery toward Viral RNA","volume":"80","author":"S Yuan","year":"2020","journal-title":"Mol Cell"},{"issue":"10","key":"ppat.1014117.ref048","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1038\/s41594-020-0511-8","article-title":"SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation","volume":"27","author":"K Schubert","year":"2020","journal-title":"Nat Struct Mol Biol"},{"key":"ppat.1014117.ref049","unstructured":"Thoms M, et al. Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2."},{"issue":"26","key":"ppat.1014117.ref050","doi-asserted-by":"crossref","first-page":"17067","DOI":"10.1016\/S0021-9258(19)47340-7","article-title":"Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps","volume":"266","author":"J Lytton","year":"1991","journal-title":"J Biol Chem"},{"issue":"11","key":"ppat.1014117.ref051","doi-asserted-by":"crossref","first-page":"2186","DOI":"10.1021\/bi00578a008","article-title":"Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase","volume":"18","author":"A Heifetz","year":"1979","journal-title":"Biochemistry"},{"issue":"7","key":"ppat.1014117.ref052","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1016\/S0092-8674(00)81304-5","article-title":"Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment","volume":"85","author":"J Sakai","year":"1996","journal-title":"Cell"},{"issue":"3","key":"ppat.1014117.ref053","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/S0092-8674(00)81362-8","article-title":"Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein","volume":"87","author":"X Hua","year":"1996","journal-title":"Cell"},{"issue":"7213","key":"ppat.1014117.ref054","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1038\/nature07317","article-title":"STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling","volume":"455","author":"H Ishikawa","year":"2008","journal-title":"Nature"},{"issue":"7748","key":"ppat.1014117.ref055","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/s41586-019-0998-5","article-title":"Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP","volume":"567","author":"G Shang","year":"2019","journal-title":"Nature"},{"key":"ppat.1014117.ref056","doi-asserted-by":"crossref","first-page":"11932","DOI":"10.1038\/ncomms11932","article-title":"Activation of STING requires palmitoylation at the Golgi","volume":"7","author":"K Mukai","year":"2016","journal-title":"Nat Commun"},{"issue":"6227","key":"ppat.1014117.ref057","article-title":"Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation","volume":"347","author":"S Liu","year":"2015","journal-title":"Science"},{"issue":"1","key":"ppat.1014117.ref058","doi-asserted-by":"crossref","first-page":"107492","DOI":"10.1016\/j.celrep.2020.03.056","article-title":"TBK1 and IKK\u03b5 Act Redundantly to Mediate STING-Induced NF-\u03baB Responses in Myeloid Cells","volume":"31","author":"KR Balka","year":"2020","journal-title":"Cell Rep"},{"issue":"6402","key":"ppat.1014117.ref059","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1038\/360350a0","article-title":"Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein","volume":"360","author":"JG Donaldson","year":"1992","journal-title":"Nature"},{"issue":"6402","key":"ppat.1014117.ref060","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/360352a0","article-title":"Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF","volume":"360","author":"JB Helms","year":"1992","journal-title":"Nature"},{"issue":"1","key":"ppat.1014117.ref061","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1083\/jcb.146.1.71","article-title":"GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5","volume":"146","author":"A Claude","year":"1999","journal-title":"J Cell Biol"},{"issue":"3","key":"ppat.1014117.ref062","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/ncb1366","article-title":"GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution","volume":"8","author":"MA Puthenveedu","year":"2006","journal-title":"Nat Cell Biol"},{"key":"ppat.1014117.ref063","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1013295","article-title":"SARS-CoV-2 remodels the Golgi apparatus to facilitate viral assembly and secretion","author":"J Zhang","year":"2025"},{"issue":"9","key":"ppat.1014117.ref064","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.3390\/v13091798","article-title":"Disruption of the Golgi Apparatus and Contribution of the Endoplasmic Reticulum to the SARS-CoV-2 Replication Complex","volume":"13","author":"T Hackstadt","year":"2021","journal-title":"Viruses"},{"issue":"7","key":"ppat.1014117.ref065","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00478-24","article-title":"Human coronavirus OC43 infection remodels connexin 43-mediated gap junction intercellular communication in vitro","volume":"98","author":"S Karmakar","year":"2024","journal-title":"J Virol"},{"issue":"22","key":"ppat.1014117.ref066","doi-asserted-by":"crossref","first-page":"11383","DOI":"10.1128\/JVI.01986-15","article-title":"The ns12.9 Accessory Protein of Human Coronavirus OC43 Is a Viroporin Involved in Virion Morphogenesis and Pathogenesis","volume":"89","author":"R Zhang","year":"2015","journal-title":"J Virol"},{"issue":"5","key":"ppat.1014117.ref067","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/nmeth.1928","article-title":"Synchronization of secretory protein traffic in populations of cells","volume":"9","author":"G Boncompain","year":"2012","journal-title":"Nat Methods"},{"issue":"9","key":"ppat.1014117.ref068","doi-asserted-by":"crossref","DOI":"10.1016\/j.cell.2021.03.035","article-title":"ER-to-Golgi protein delivery through an interwoven, tubular network extending from ER","volume":"184","author":"AV Weigel","year":"2021","journal-title":"Cell"},{"issue":"6","key":"ppat.1014117.ref069","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1002\/1873-3468.14560","article-title":"The structure of COPI vesicles and regulation of vesicle turnover","volume":"597","author":"RJ Taylor","year":"2023","journal-title":"FEBS Lett"},{"key":"ppat.1014117.ref070","article-title":"COPI coat assembly occurs on liquid-disordered domains and the associated membrane deformations are limited by membrane tension","volume":"70","author":"J-B Manneville","year":"2023","journal-title":"Cell Biology"},{"issue":"52","key":"ppat.1014117.ref071","doi-asserted-by":"crossref","first-page":"53112","DOI":"10.1074\/jbc.M300402200","article-title":"Intra-Golgi protein transport depends on a cholesterol balance in the lipid membrane","volume":"278","author":"E St\u00fcven","year":"2003","journal-title":"J Biol Chem"},{"issue":"20","key":"ppat.1014117.ref072","doi-asserted-by":"crossref","DOI":"10.1016\/j.devcel.2021.09.016","article-title":"S-acylation controls SARS-CoV-2 membrane lipid organization and enhances infectivity","volume":"56","author":"FS Mesquita","year":"2021","journal-title":"Dev Cell"},{"issue":"7","key":"ppat.1014117.ref073","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1242\/jcs.164715","article-title":"Complementary probes reveal that phosphatidylserine is required for the proper transbilayer distribution of cholesterol","volume":"128","author":"M Maekawa","year":"2015","journal-title":"J Cell Sci"},{"issue":"11","key":"ppat.1014117.ref074","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1111\/j.1600-0854.2008.00801.x","article-title":"BODIPY-cholesterol: a new tool to visualize sterol trafficking in living cells and organisms","volume":"9","author":"M H\u00f6ltt\u00e4-Vuori","year":"2008","journal-title":"Traffic"},{"issue":"1","key":"ppat.1014117.ref075","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.micinf.2018.06.002","article-title":"Organelle dynamics and viral infections: at cross roads","volume":"21","author":"RS Glingston","year":"2019","journal-title":"Microbes Infect"},{"issue":"1","key":"ppat.1014117.ref076","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jsb.2010.11.021","article-title":"A structural analysis of M protein in coronavirus assembly and morphology","volume":"174","author":"BW Neuman","year":"2011","journal-title":"J Struct Biol"},{"key":"ppat.1014117.ref077","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.81702","article-title":"Structure of SARS-CoV-2 M protein in lipid nanodiscs","volume":"11","author":"KA Dolan","year":"2022","journal-title":"eLife"},{"issue":"8058","key":"ppat.1014117.ref078","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1038\/s41586-025-08773-x","article-title":"A coronavirus assembly inhibitor that targets the viral membrane protein","volume":"640","author":"M Laporte","year":"2025","journal-title":"Nature"},{"issue":"8058","key":"ppat.1014117.ref079","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1038\/s41586-025-08651-6","article-title":"A small-molecule SARS-CoV-2 inhibitor targeting the membrane protein","volume":"640","author":"E Van Damme","year":"2025","journal-title":"Nature"},{"key":"ppat.1014117.ref080","doi-asserted-by":"crossref","DOI":"10.1101\/2024.11.04.620124","article-title":"Direct lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly","author":"M Dutta","year":"2024"},{"issue":"4","key":"ppat.1014117.ref081","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1016\/j.cell.2024.11.028","article-title":"Global organelle profiling reveals subcellular localization and remodeling at proteome scale","volume":"188","author":"MY Hein","year":"2025","journal-title":"Cell"},{"issue":"3","key":"ppat.1014117.ref082","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1083\/jcb.151.3.507","article-title":"Evidence for segregation of sphingomyelin and cholesterol during formation of COPI-coated vesicles","volume":"151","author":"B Br\u00fcgger","year":"2000","journal-title":"J Cell Biol"},{"key":"ppat.1014117.ref083","article-title":"Host protein ARF1 is a proviral factor for SARS-CoV-2 and a candidate broad-spectrum therapeutic target.","author":"YJ Ning","year":"2024"},{"key":"ppat.1014117.ref084","doi-asserted-by":"crossref","DOI":"10.1101\/2025.02.15.638421","article-title":"A truncated SARS-CoV-2 nucleocapsid protein enhances virus fitness by evading antiviral responses","author":"RP Mulloy","year":"2025"},{"issue":"8","key":"ppat.1014117.ref085","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010724","article-title":"Human coronaviruses disassemble processing bodies","volume":"18","author":"M Kleer","year":"2022","journal-title":"PLoS Pathog"},{"issue":"2","key":"ppat.1014117.ref086","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01671-24","article-title":"A yeast-based reverse genetics system to generate HCoV-OC43 reporter viruses encoding an eighth subgenomic RNA","volume":"99","author":"BA Duguay","year":"2025","journal-title":"J Virol"},{"issue":"9","key":"ppat.1014117.ref087","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010832","article-title":"Thiopurines inhibit coronavirus Spike protein processing and incorporation into progeny virions","volume":"18","author":"ES Pringle","year":"2022","journal-title":"PLoS Pathog"},{"issue":"12","key":"ppat.1014117.ref088","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008185","article-title":"KSHV activates unfolded protein response sensors but suppresses downstream transcriptional responses to support lytic replication","volume":"15","author":"BP Johnston","year":"2019","journal-title":"PLoS Pathog"},{"issue":"12","key":"ppat.1014117.ref089","doi-asserted-by":"crossref","first-page":"3228","DOI":"10.1128\/iai.56.12.3228-3234.1988","article-title":"Cloning and expression in Escherichia coli of the perfringolysin O (theta-toxin) gene from Clostridium perfringens and characterization of the gene product","volume":"56","author":"RK Tweten","year":"1988","journal-title":"Infect Immun"},{"issue":"3","key":"ppat.1014117.ref090","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/S0092-8674(00)81660-8","article-title":"The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins","volume":"99","author":"O Shatursky","year":"1999","journal-title":"Cell"},{"issue":"16","key":"ppat.1014117.ref091","doi-asserted-by":"crossref","first-page":"3373","DOI":"10.1021\/bi3003132","article-title":"Modifications in perfringolysin O domain 4 alter the cholesterol concentration threshold required for binding","volume":"51","author":"BB Johnson","year":"2012","journal-title":"Biochemistry"},{"issue":"9","key":"ppat.1014117.ref092","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1038\/nprot.2007.294","article-title":"Detergent resistance as a tool in membrane research","volume":"2","author":"D Lingwood","year":"2007","journal-title":"Nat Protoc"},{"key":"ppat.1014117.ref093","article-title":"Dataset associated with the manuscript entitled \u201cCoronavirus M protein disperses the trans-Golgi network and inhibits anterograde protein trafficking in the secretory pathway\u201d","author":"T Caddell","year":"2026","journal-title":"Dryad"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1014117","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T00:00:00Z","timestamp":1778544000000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1014117","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T17:47:47Z","timestamp":1778608067000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1014117"}},"subtitle":[],"editor":[{"given":"George A.","family":"Belov","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2026,5,5]]},"references-count":93,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2026,5,5]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1014117","relation":{},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,5]]}}}