{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T00:38:28Z","timestamp":1793407108707,"version":"4.5.0"},"reference-count":168,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T00:00:00Z","timestamp":1770076800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32172888"],"award-info":[{"award-number":["32172888"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.jbc.2026.111250","type":"journal-article","created":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T00:48:59Z","timestamp":1770252539000},"page":"111250","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["Cell entry mechanisms of porcine enteric coronaviruses"],"prefix":"10.1016","volume":"302","author":[{"given":"Yiping","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fei","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qin","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Senyan","family":"Du","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yiping","family":"Wen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rui","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanjie","family":"Cao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Feng","family":"Cong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8126-0979","authenticated-orcid":false,"given":"Xiaobo","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.111250_bib1","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":"V\u2019kovski","year":"2021","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib2","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.coviro.2018.12.001","article-title":"Emerging and re-emerging coronaviruses in pigs","volume":"34","author":"Wang","year":"2019","journal-title":"Curr. Opin. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib3","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1007\/s12250-021-00364-0","article-title":"Porcine coronaviruses: overview of the state of the art","volume":"36","author":"Turlewicz-Podbielska","year":"2021","journal-title":"Virol. Sin."},{"key":"10.1016\/j.jbc.2026.111250_bib4","doi-asserted-by":"crossref","first-page":"359","DOI":"10.3390\/v15020359","article-title":"Transmissible gastroenteritis virus: an update review and perspective","volume":"15","author":"Chen","year":"2023","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib5","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2023.106185","article-title":"Insights and progress on epidemic characteristics, genotyping, and preventive measures of PEDV in China: a review","volume":"181","author":"Li","year":"2023","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.jbc.2026.111250_bib6","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/s13567-024-01436-1","article-title":"Interplay of swine acute diarrhoea syndrome coronavirus and the host intrinsic and innate immunity","volume":"56","author":"Zhao","year":"2025","journal-title":"Vet. Res."},{"key":"10.1016\/j.jbc.2026.111250_bib7","doi-asserted-by":"crossref","first-page":"79","DOI":"10.3390\/pathogens11010079","article-title":"Porcine deltacoronaviruses: origin, evolution, cross-species transmission and zoonotic potential","volume":"11","author":"Kong","year":"2022","journal-title":"Pathogens"},{"key":"10.1016\/j.jbc.2026.111250_bib8","doi-asserted-by":"crossref","first-page":"12910","DOI":"10.1074\/jbc.REV120.013930","article-title":"The molecular virology of coronaviruses","volume":"295","author":"Hartenian","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111250_bib9","doi-asserted-by":"crossref","first-page":"2914","DOI":"10.1016\/j.immuni.2024.10.001","article-title":"Isolation and escape mapping of broadly neutralizing antibodies against emerging delta-coronaviruses","volume":"57","author":"Rexhepaj","year":"2024","journal-title":"Immunity"},{"key":"10.1016\/j.jbc.2026.111250_bib10","doi-asserted-by":"crossref","first-page":"5330","DOI":"10.1038\/s41467-024-49693-0","article-title":"Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein","volume":"15","author":"Du","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111250_bib11","article-title":"A novel neutralizing antibody recognizing a conserved conformational epitope in PDCoV S1 protein and its therapeutic efficacy in piglets","volume":"99","author":"Chen","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib12","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1038\/nrmicro817","article-title":"Virus entry: molecular mechanisms and biomedical applications","volume":"2","author":"Dimitrov","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib13","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1146\/annurev-biochem-060208-104626","article-title":"Virus entry by endocytosis","volume":"79","author":"Mercer","year":"2010","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jbc.2026.111250_bib14","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/357417a0","article-title":"Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV","volume":"357","author":"Delmas","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111250_bib15","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1128\/JVI.72.1.527-534.1998","article-title":"The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment","volume":"72","author":"Hansen","year":"1998","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib16","doi-asserted-by":"crossref","first-page":"4653","DOI":"10.1096\/fj.201902455R","article-title":"Dynamics of transmissible gastroenteritis virus internalization unraveled by single-virus tracking in live cells","volume":"34","author":"Wang","year":"2020","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2026.111250_bib17","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.antiviral.2010.10.002","article-title":"Cholesterol is important for a post-adsorption step in the entry process of transmissible gastroenteritis virus","volume":"88","author":"Yin","year":"2010","journal-title":"Antivir. Res."},{"key":"10.1016\/j.jbc.2026.111250_bib18","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.virusres.2008.07.023","article-title":"Importance of cholesterol for infection of cells by transmissible gastroenteritis virus","volume":"137","author":"Ren","year":"2008","journal-title":"Virus Res."},{"key":"10.1016\/j.jbc.2026.111250_bib19","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.virol.2018.05.009","article-title":"Epidermal growth factor receptor is a co-factor for transmissible gastroenteritis virus entry","volume":"521","author":"Hu","year":"2018","journal-title":"Virology"},{"key":"10.1016\/j.jbc.2026.111250_bib20","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00256-21","article-title":"Dynamic dissection of the endocytosis of porcine epidemic diarrhea coronavirus cooperatively mediated by clathrin and caveolae as visualized by single-virus tracking","volume":"12","author":"Li","year":"2021","journal-title":"MBio"},{"key":"10.1016\/j.jbc.2026.111250_bib21","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/s13567-020-0739-7","article-title":"PEDV enters cells through clathrin-, caveolae-, and lipid raft-mediated endocytosis and traffics via the endo-\/lysosome pathway","volume":"51","author":"Wei","year":"2020","journal-title":"Vet. Res."},{"key":"10.1016\/j.jbc.2026.111250_bib22","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.virusres.2014.07.022","article-title":"Clathrin- and serine proteases-dependent uptake of porcine epidemic diarrhea virus into vero cells","volume":"191","author":"Park","year":"2014","journal-title":"Virus Res."},{"key":"10.1016\/j.jbc.2026.111250_bib23","doi-asserted-by":"crossref","first-page":"3753","DOI":"10.1007\/s00705-017-3545-4","article-title":"Cellular cholesterol is required for porcine nidovirus infection","volume":"162","author":"Jeon","year":"2017","journal-title":"Arch. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib24","doi-asserted-by":"crossref","first-page":"24779","DOI":"10.1074\/jbc.M116.740746","article-title":"Cell entry of porcine epidemic diarrhea coronavirus is activated by lysosomal proteases","volume":"291","author":"Liu","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111250_bib25","doi-asserted-by":"crossref","first-page":"114","DOI":"10.3390\/v9050114","article-title":"TMPRSS2 and MSPL facilitate trypsin-independent porcine epidemic diarrhea virus replication in vero cells","volume":"9","author":"Shi","year":"2017","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib26","first-page":"e00210","article-title":"Porcine enteric alphacoronavirus entry through multiple pathways (Caveolae, Clathrin, and Macropinocytosis) requires Rab GTPases for endosomal transport","volume":"94","author":"Chen","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib27","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00139-24","article-title":"Functional dissection of the spike glycoprotein S1 subunit and identification of cellular cofactors for regulation of swine acute diarrhea syndrome coronavirus entry","volume":"98","author":"Yang","year":"2024","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib28","doi-asserted-by":"crossref","DOI":"10.1002\/jmv.29712","article-title":"TMPRSS13 promotes the cell entry of swine acute diarrhea syndrome coronavirus","volume":"96","author":"Han","year":"2024","journal-title":"J. Med. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib29","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01957-23","article-title":"Establishment of replication-competent vesicular stomatitis virus recapitulating SADS-CoV entry","volume":"98","author":"Zhu","year":"2024","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib30","doi-asserted-by":"crossref","first-page":"9830","DOI":"10.1074\/jbc.RA119.007779","article-title":"Porcine deltacoronavirus enters cells via two pathways: a protease-mediated one at the cell surface and another facilitated by cathepsins in the endosome","volume":"294","author":"Zhang","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111250_bib31","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01345-21","article-title":"Porcine deltacoronavirus enters porcine IPI-2I intestinal epithelial cells via macropinocytosis and clathrin-mediated endocytosis dependent on pH and dynamin","volume":"95","author":"Fang","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib32","doi-asserted-by":"crossref","DOI":"10.1128\/spectrum.02553-23","article-title":"Porcine deltacoronavirus enters ST cells by clathrin-mediated endocytosis and does not require Rab5, Rab7, or Rab11","volume":"11","author":"Li","year":"2023","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.jbc.2026.111250_bib33","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01055-25","article-title":"Cathepsin L and transmembrane serine protease 11E mediate trypsin-independent entry of porcine deltacoronavirus into Huh7 cells","volume":"99","author":"Xiao","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib34","doi-asserted-by":"crossref","first-page":"3119","DOI":"10.1007\/s00705-018-3967-7","article-title":"Cholesterol is important for the entry process of porcine deltacoronavirus","volume":"163","author":"Jeon","year":"2018","journal-title":"Arch. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib35","doi-asserted-by":"crossref","DOI":"10.1080\/21505594.2024.2407847","article-title":"Integrin \u03b1V\u03b23 mediates porcine deltacoronavirus infection and inflammatory response through activation of the FAK-PI3K-AKT-nf-\u03baB signalling pathway","volume":"15","author":"Jin","year":"2024","journal-title":"Virulence"},{"key":"10.1016\/j.jbc.2026.111250_bib36","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00944-21","article-title":"Aminopeptidase N is an entry co-factor triggering porcine deltacoronavirus entry via an endocytotic pathway","volume":"95","author":"Yang","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib37","doi-asserted-by":"crossref","first-page":"496","DOI":"10.3390\/v14030496","article-title":"Porcine deltacoronavirus (PDCoV) entry into PK-15 cells by caveolae-mediated endocytosis","volume":"14","author":"Li","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib38","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1186\/s13567-024-01442-3","article-title":"Deltacoronavirus HKU11, HKU13, PDCoV (HKU15) and HKU17 spike pseudoviruses enter avian DF-1 cells via clathrin-mediated endocytosis in a Rab5-, Rab7- and pH-dependent manner","volume":"56","author":"Liang","year":"2025","journal-title":"Vet. Res."},{"key":"10.1016\/j.jbc.2026.111250_bib39","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.molmed.2008.06.003","article-title":"The moonlighting enzyme CD13: old and new functions to target","volume":"14","author":"Mina-Osorio","year":"2008","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.jbc.2026.111250_bib40","doi-asserted-by":"crossref","first-page":"26455","DOI":"10.1039\/D5RA03038B","article-title":"Aminopeptidase N: a multifunctional and promising target in medicinal chemistry","volume":"15","author":"Farsa","year":"2025","journal-title":"RSC Adv."},{"key":"10.1016\/j.jbc.2026.111250_bib41","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1038\/s41426-018-0068-3","article-title":"Contribution of porcine aminopeptidase N to porcine deltacoronavirus infection","volume":"7","author":"Zhu","year":"2018","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.jbc.2026.111250_bib42","first-page":"E5135","article-title":"Broad receptor engagement of an emerging global coronavirus may potentiate its diverse cross-species transmissibility","volume":"115","author":"Li","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib43","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00318-18","article-title":"Porcine deltacoronavirus engages the transmissible gastroenteritis virus functional receptor porcine aminopeptidase N for infectious cellular entry","volume":"92","author":"Wang","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib44","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/s41586-018-0010-9","article-title":"Fatal swine acute diarrhoea syndrome caused by an HKU2-related coronavirus of bat origin","volume":"556","author":"Zhou","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111250_bib45","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01448-19","article-title":"Broad cross-species infection of cultured cells by bat HKU2-related swine acute diarrhea syndrome coronavirus and identification of its replication in murine dendritic cells in vivo highlight its potential for diverse interspecies transmission","volume":"93","author":"Yang","year":"2019","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib46","doi-asserted-by":"crossref","first-page":"12647","DOI":"10.1128\/JVI.78.22.12647-12656.2004","article-title":"Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton\/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor","volume":"78","author":"Chutima","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib47","article-title":"Membrane protein CRISPR screen identifies RPSA as an essential host factor for porcine epidemic diarrhea virus replication","volume":"99","author":"Yu","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib48","doi-asserted-by":"crossref","first-page":"269","DOI":"10.4142\/jvs.2003.4.3.269","article-title":"Identification of a putative cellular receptor 150 kDa polypeptide for porcine epidemic diarrhea virus in porcine enterocytes","volume":"4","author":"Oh","year":"2003","journal-title":"J. Vet. Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib49","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.virol.2007.03.031","article-title":"Porcine aminopeptidase N is a functional receptor for the PEDV coronavirus","volume":"365","author":"Li","year":"2007","journal-title":"Virology"},{"key":"10.1016\/j.jbc.2026.111250_bib50","doi-asserted-by":"crossref","first-page":"6121","DOI":"10.1128\/JVI.00430-15","article-title":"Receptor usage and cell entry of porcine epidemic diarrhea coronavirus","volume":"89","author":"Liu","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib51","doi-asserted-by":"crossref","first-page":"2528","DOI":"10.1099\/jgv.0.000563","article-title":"Porcine aminopeptidase N is not a cellular receptor of porcine epidemic diarrhea virus, but promotes its infectivity via aminopeptidase activity","volume":"97","author":"Shirato","year":"2016","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib52","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.virusres.2017.03.018","article-title":"Aminopeptidase N is not required for porcine epidemic diarrhea virus cell entry","volume":"235","author":"Li","year":"2017","journal-title":"Virus Res."},{"key":"10.1016\/j.jbc.2026.111250_bib53","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.virol.2018.02.019","article-title":"Aminopeptidase-N-independent entry of porcine epidemic diarrhea virus into vero or porcine small intestine epithelial cells","volume":"517","author":"Ji","year":"2018","journal-title":"Virology"},{"key":"10.1016\/j.jbc.2026.111250_bib54","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1013317","article-title":"Resolving the APN controversy in PEDV infection: comparative kinetic characterization through single-virus tracking","volume":"21","author":"An","year":"2025","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111250_bib55","doi-asserted-by":"crossref","first-page":"8669","DOI":"10.1128\/jvi.70.12.8669-8674.1996","article-title":"Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I","volume":"70","author":"Tresnan","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib56","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1012836","article-title":"Cross-species recognition of two porcine coronaviruses to their cellular receptor aminopeptidase N of dogs and seven other species","volume":"21","author":"Tian","year":"2025","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111250_bib57","doi-asserted-by":"crossref","first-page":"e01118","DOI":"10.1128\/JVI.01118-21","article-title":"Roles of two major domains of the porcine deltacoronavirus S1 subunit in receptor binding and neutralization","volume":"95","author":"Liu","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib58","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1038\/s41467-022-29062-5","article-title":"Structures of a deltacoronavirus spike protein bound to porcine and human receptors","volume":"13","author":"Ji","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111250_bib59","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/s41586-021-04111-z","article-title":"Independent infections of porcine deltacoronavirus among Haitian children","volume":"600","author":"Lednicky","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111250_bib60","doi-asserted-by":"crossref","first-page":"3756","DOI":"10.1007\/s11427-025-2985-1","article-title":"Receptor affinity-selective differential dynamics of membrane fusion initiation govern deltacoronavirus cross-species transmission","volume":"68","author":"Peng","year":"2025","journal-title":"Sci. China Life Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib61","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00480-20","article-title":"Aminopeptidase N expression, not interferon responses, determines the intestinal segmental tropism of porcine deltacoronavirus","volume":"94","author":"Yin","year":"2020","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib62","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/S0092-8674(04)00343-5","article-title":"Balancing acts: molecular control of mammalian iron metabolism","volume":"117","author":"Hentze","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.111250_bib63","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0378-1135(99)00199-6","article-title":"Isolation of porcine epidemic diarrhea virus in porcine cell cultures and experimental infection of pigs of different ages","volume":"72","author":"Shibata","year":"2000","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib64","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.tvjl.2015.02.017","article-title":"Porcine epidemic diarrhea virus infection: etiology, epidemiology, pathogenesis and immunoprophylaxis","volume":"204","author":"Jung","year":"2015","journal-title":"Vet. J."},{"key":"10.1016\/j.jbc.2026.111250_bib65","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0139266","article-title":"Effect of porcine epidemic diarrhea virus infectious doses on infection outcomes in na\u00efve conventional neonatal and weaned pigs","volume":"10","author":"Thomas","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.111250_bib66","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.prevetmed.2017.12.012","article-title":"Investigation of three outbreaks of porcine epidemic diarrhea in Germany in 2016 demonstrates age dependent differences in the development of humoral immune response","volume":"150","author":"Stadler","year":"2018","journal-title":"Prev. Vet. Med."},{"key":"10.1016\/j.jbc.2026.111250_bib67","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/nature05539","article-title":"Transferrin receptor 1 is a cellular receptor for new world haemorrhagic fever arenaviruses","volume":"446","author":"Radoshitzky","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111250_bib68","doi-asserted-by":"crossref","first-page":"10777","DOI":"10.1073\/pnas.1301764110","article-title":"Identification of transferrin receptor 1 as a hepatitis C virus entry factor","volume":"110","author":"Martin","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib69","first-page":"e01612","article-title":"Transferrin receptor protein 1 is an entry factor for rabies virus","volume":"97","author":"Wang","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib70","article-title":"Transferrin receptor protein 1 cooperates with mGluR2 to mediate the internalization of rabies virus and SARS-CoV-2","volume":"97","author":"Wang","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib71","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2214936120","article-title":"Influenza A virus exploits transferrin receptor recycling to enter host cells","volume":"120","author":"Mazel-Sanchez","year":"2023","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib72","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2317026121","article-title":"Human transferrin receptor can mediate SARS-CoV-2 infection","volume":"121","author":"Liao","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib73","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00671-25","article-title":"Transferrin receptor 1 (TfR1) functions as an entry receptor for scale drop disease virus to invade the host cell via clathrin-mediated endocytosis","volume":"99","author":"Chen","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib74","doi-asserted-by":"crossref","DOI":"10.1016\/j.vetmic.2025.110698","article-title":"Transferrin receptor 1 is an entry factor for Japanese encephalitis virus","volume":"309","author":"Yang","year":"2025","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib75","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.bbagen.2011.10.013","article-title":"Regulation of iron transport and the role of transferrin","volume":"1820","author":"Gkouvatsos","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.111250_bib76","doi-asserted-by":"crossref","first-page":"11714","DOI":"10.1073\/pnas.1511701112","article-title":"Noncanonical role of transferrin receptor 1 is essential for intestinal homeostasis","volume":"112","author":"Chen","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib77","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008682","article-title":"Transferrin receptor 1 levels at the cell surface influence the susceptibility of newborn piglets to PEDV infection","volume":"16","author":"Zhang","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111250_bib78","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1186\/s12964-018-0283-5","article-title":"Transferrin receptor 1 is a supplementary receptor that assists transmissible gastroenteritis virus entry into porcine intestinal epithelium","volume":"16","author":"Zhang","year":"2018","journal-title":"Cell Commun. Signal."},{"key":"10.1016\/j.jbc.2026.111250_bib79","doi-asserted-by":"crossref","DOI":"10.1002\/mco2.161","article-title":"Heat shock proteins: biological functions, pathological roles, and therapeutic opportunities","volume":"3","author":"Hu","year":"2022","journal-title":"MedComm."},{"key":"10.1016\/j.jbc.2026.111250_bib80","doi-asserted-by":"crossref","first-page":"4209","DOI":"10.3390\/ijms25084209","article-title":"Heat shock response and heat shock proteins: current understanding and future opportunities in human diseases","volume":"25","author":"Singh","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib81","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00128-23","article-title":"The TGEV membrane protein interacts with HSC70 to direct virus internalization through clathrin-mediated endocytosis","volume":"97","author":"Ji","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib82","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00549-23","article-title":"HSPA5 promotes attachment and internalization of porcine epidemic diarrhea virus through interaction with the spike protein and the endo-\/lysosomal pathway","volume":"97","author":"Zhou","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib83","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1152\/physrev.00030.2015","article-title":"Expression and function of the epidermal growth factor receptor in physiology and disease","volume":"96","author":"Chen","year":"2016","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.jbc.2026.111250_bib84","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1080\/08977194.2022.2063123","article-title":"The roles of epidermal growth factor receptor in viral infections","volume":"40","author":"Lai","year":"2022","journal-title":"Growth Factors"},{"key":"10.1016\/j.jbc.2026.111250_bib85","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2021.820355","article-title":"Role of EGF receptor regulatory networks in the host response to viral infections","volume":"11","author":"Carlin","year":"2022","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib86","doi-asserted-by":"crossref","first-page":"1766","DOI":"10.3390\/biom13121766","article-title":"Role of virus-induced EGFR trafficking in proviral functions","volume":"13","author":"Noh","year":"2023","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2026.111250_bib87","doi-asserted-by":"crossref","first-page":"12206","DOI":"10.18632\/oncotarget.7723","article-title":"The epidermal growth factor receptor regulates cofilin activity and promotes transmissible gastroenteritis virus entry into intestinal epithelial cells","volume":"7","author":"Hu","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.jbc.2026.111250_bib88","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02095-17","article-title":"Porcine epidemic diarrhea virus-induced epidermal growth factor receptor activation impairs the antiviral activity of type I interferon","volume":"92","author":"Yang","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib89","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1111\/1753-0407.13052","article-title":"COVID-19 and comorbidities: a role for dipeptidyl peptidase 4 (DPP4) in disease severity?","volume":"12","author":"Bassendine","year":"2020","journal-title":"J. Diabetes"},{"key":"10.1016\/j.jbc.2026.111250_bib90","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1186\/s13098-024-01412-x","article-title":"The multiple actions of dipeptidyl peptidase 4 (DPP-4) and its pharmacological inhibition on bone metabolism: a review","volume":"16","author":"Pechmann","year":"2024","journal-title":"Diabetol. Metab. Syndr."},{"key":"10.1016\/j.jbc.2026.111250_bib91","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/nature12005","article-title":"Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC","volume":"495","author":"Raj","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111250_bib92","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/j.chom.2014.08.009","article-title":"Bat origins of MERS-CoV supported by bat coronavirus HKU4 usage of human receptor CD26","volume":"16","author":"Wang","year":"2014","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.jbc.2026.111250_bib93","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1038\/s41467-020-20458-9","article-title":"Isolation of MERS-related coronavirus from lesser bamboo bats that uses DPP4 and infects human-DPP4-transgenic mice","volume":"12","author":"Lau","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111250_bib94","doi-asserted-by":"crossref","DOI":"10.1016\/j.vetmic.2025.110370","article-title":"Dipeptidyl peptidase 4 is a cofactor for porcine epidemic diarrhea virus infection","volume":"301","author":"Huang","year":"2025","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib95","doi-asserted-by":"crossref","first-page":"26915","DOI":"10.1073\/pnas.2001046117","article-title":"Swine acute diarrhea syndrome coronavirus replication in primary human cells reveals potential susceptibility to infection","volume":"117","author":"Edwards","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib96","doi-asserted-by":"crossref","first-page":"2339","DOI":"10.1007\/s00018-018-2805-0","article-title":"Follistatin-like 1 in development and human diseases","volume":"75","author":"Mattiotti","year":"2018","journal-title":"Cell. Mol. Life. Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib97","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.2174\/1389557519666190312161551","article-title":"Follistatin-like 1 in cardiovascular disease and inflammation","volume":"19","author":"Peters","year":"2019","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.jbc.2026.111250_bib98","doi-asserted-by":"crossref","DOI":"10.1016\/j.gene.2024.148263","article-title":"FSTL1: a double-edged sword in cancer development","volume":"906","author":"Du","year":"2024","journal-title":"Gene"},{"key":"10.1016\/j.jbc.2026.111250_bib99","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01837-24","article-title":"FSTL1 and TLR4 interact with PEDV structural proteins to promote virus adsorption to host cells","volume":"99","author":"Liu","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib100","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1186\/s12979-023-00383-3","article-title":"Toll-like receptor 4 (TLR4): new insight immune and aging","volume":"20","author":"Kim","year":"2023","journal-title":"Immun. Ageing"},{"key":"10.1016\/j.jbc.2026.111250_bib101","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/s41577-021-00626-8","article-title":"Lessons in self-defence: inhibition of virus entry by intrinsic immunity","volume":"22","author":"Majdoul","year":"2022","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.jbc.2026.111250_bib102","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102741","article-title":"IFITM proteins: understanding their diverse roles in viral infection, cancer, and immunity","volume":"299","author":"G\u00f3mez-Herranz","year":"2023","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111250_bib103","doi-asserted-by":"crossref","DOI":"10.1016\/j.vetmic.2022.109622","article-title":"IFITM3 is a host restriction factor that inhibits porcine transmissible gastroenteritis virus infection","volume":"277","author":"Yan","year":"2023","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib104","doi-asserted-by":"crossref","first-page":"6756","DOI":"10.1073\/pnas.1320856111","article-title":"Interferon induction of IFITM proteins promotes infection by human coronavirus OC43","volume":"111","author":"Zhao","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib105","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.1128\/JVI.03416-14","article-title":"Human cytomegalovirus exploits interferon-induced transmembrane proteins to facilitate morphogenesis of the virion assembly compartment","volume":"89","author":"Xie","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib106","doi-asserted-by":"crossref","first-page":"727","DOI":"10.3390\/v14040727","article-title":"IFITM3 interacts with the HBV\/HDV receptor NTCP and modulates virus entry and infection","volume":"14","author":"Palatini","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib107","doi-asserted-by":"crossref","DOI":"10.1016\/j.biocel.2022.106325","article-title":"IFITM3 promotes NiV envelope protein-mediated entry into MDCK cells and interacts with the fusion subunit of the F protein","volume":"153","author":"Xu","year":"2022","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"10.1016\/j.jbc.2026.111250_bib108","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.02028-24","article-title":"IFITM proteins are key entry factors for porcine epidemic diarrhea coronavirus","volume":"99","author":"Lv","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib109","doi-asserted-by":"crossref","first-page":"7743","DOI":"10.1038\/s41467-024-52049-3","article-title":"The V-ATPase complex component RNAseK is required for lysosomal hydrolase delivery and autophagosome degradation","volume":"15","author":"Makar","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111250_bib110","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1016\/j.celrep.2015.06.076","article-title":"RNASEK is a V-ATPase-associated factor required for endocytosis and the replication of rhinovirus, influenza A virus, and dengue virus","volume":"12","author":"Perreira","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.111250_bib111","doi-asserted-by":"crossref","first-page":"7797","DOI":"10.1073\/pnas.1424098112","article-title":"RNASEK is required for internalization of diverse acid-dependent viruses","volume":"112","author":"Hackett","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib112","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01760-24","article-title":"RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis","volume":"99","author":"Qin","year":"2025","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib113","doi-asserted-by":"crossref","first-page":"1740","DOI":"10.1093\/infdis\/jiy081","article-title":"The role of heparan sulfate proteoglycans as an attachment factor for rabies virus entry and infection","volume":"217","author":"Sasaki","year":"2018","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jbc.2026.111250_bib114","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1038\/s41421-020-00222-5","article-title":"Heparan sulfate assists SARS-CoV-2 in cell entry and can be targeted by approved drugs in vitro","volume":"6","author":"Zhang","year":"2020","journal-title":"Cell Discov."},{"key":"10.1016\/j.jbc.2026.111250_bib115","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.cell.2020.09.033","article-title":"SARS-CoV-2 infection depends on cellular heparan sulfate and ACE2","volume":"183","author":"Clausen","year":"2020","journal-title":"Cell."},{"key":"10.1016\/j.jbc.2026.111250_bib116","doi-asserted-by":"crossref","DOI":"10.1016\/j.vetmic.2022.109616","article-title":"Porcine deltacoronavirus uses heparan sulfate as an attachment receptor","volume":"276","author":"Xiao","year":"2023","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib117","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1007\/s00705-015-2408-0","article-title":"Porcine epidemic diarrhea virus uses cell-surface heparan sulfate as an attachment factor","volume":"160","author":"Huan","year":"2015","journal-title":"Arch. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib118","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00880-24","article-title":"Cell-surface d-glucuronyl C5-epimerase binds to porcine deltacoronavirus spike protein facilitating viral entry","volume":"98","author":"Xiao","year":"2024","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib119","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/s41420-024-02180-3","article-title":"Biological function of sialic acid and sialylation in human health and disease","volume":"10","author":"Zhu","year":"2024","journal-title":"Cell Death Discov"},{"key":"10.1016\/j.jbc.2026.111250_bib120","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1038\/s41538-025-00390-2","article-title":"The physiological characteristics and applications of sialic acid","volume":"9","author":"Wang","year":"2025","journal-title":"NPJ Sci. Food"},{"key":"10.1016\/j.jbc.2026.111250_bib121","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1016\/j.tim.2016.07.005","article-title":"Effects of sialic acid modifications on virus binding and infection","volume":"24","author":"Wasik","year":"2016","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib122","doi-asserted-by":"crossref","first-page":"262","DOI":"10.3390\/v13020262","article-title":"Sialic acid receptors: the key to solving the enigma of zoonotic virus spillover","volume":"13","author":"Kuchipudi","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib123","doi-asserted-by":"crossref","first-page":"5634","DOI":"10.1128\/jvi.70.8.5634-5637.1996","article-title":"Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity","volume":"70","author":"Schultze","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib124","doi-asserted-by":"crossref","first-page":"6037","DOI":"10.1128\/JVI.76.12.6037-6043.2002","article-title":"Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins","volume":"76","author":"Schwegmann-We\u00dfels","year":"2002","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib125","doi-asserted-by":"crossref","first-page":"3285","DOI":"10.1128\/jvi.71.4.3285-3287.1997","article-title":"Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus","volume":"71","author":"Krempl","year":"1997","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib126","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.virusres.2016.05.031","article-title":"Cellular entry of the porcine epidemic diarrhea virus","volume":"226","author":"Li","year":"2016","journal-title":"Virus Res."},{"key":"10.1016\/j.jbc.2026.111250_bib127","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.01628-25","article-title":"Genome-wide CRISPR screen reveals key role of sialic acids in PEDV and porcine coronavirus infections","volume":"16","author":"Guo","year":"2025","journal-title":"MBio"},{"key":"10.1016\/j.jbc.2026.111250_bib128","doi-asserted-by":"crossref","first-page":"2442","DOI":"10.3390\/v13122442","article-title":"Porcine deltacoronavirus utilizes sialic acid as an attachment receptor and trypsin can influence the binding activity","volume":"13","author":"Yuan","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib129","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01626-22","article-title":"Genome-wide CRISPR\/Cas9 screen reveals a role for SLC35A1 in the adsorption of porcine deltacoronavirus","volume":"96","author":"Wang","year":"2022","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib130","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.125962","article-title":"Genome-scale CRISPR screen identifies TRIM2 and SLC35A1 associated with porcine epidemic diarrhoea virus infection","volume":"250","author":"Wang","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.jbc.2026.111250_bib131","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2021.635411","article-title":"The role of lectin receptors and their ligands in controlling allergic inflammation","volume":"12","author":"Peters","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/j.jbc.2026.111250_bib132","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1111\/1574-6976.12052","article-title":"Bitter-sweet symphony: glycan-lectin interactions in virus biology","volume":"38","author":"Van Breedam","year":"2014","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.jbc.2026.111250_bib133","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s00418-016-1523-7","article-title":"C-type lectins: their network and roles in pathogen recognition and immunity","volume":"147","author":"Mayer","year":"2017","journal-title":"Histochem. Cell Biol."},{"key":"10.1016\/j.jbc.2026.111250_bib134","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.3390\/ijms23031451","article-title":"Systemic lectin-glycan interaction of pathogenic enteric bacteria in the gastrointestinal tract","volume":"23","author":"Cho","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib135","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2021.104956","article-title":"Expression of the human or porcine C-type lectins DC-SIGN\/L-SIGN confers susceptibility to porcine epidemic diarrhea virus entry and infection in otherwise refractory cell lines","volume":"157","author":"Zhao","year":"2021","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.jbc.2026.111250_bib136","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1007\/s00018-025-05672-2","article-title":"Siglec-15 is a putative receptor for porcine epidemic diarrhea virus infection","volume":"82","author":"Feng","year":"2025","journal-title":"Cell. Mol. Life. Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib137","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.3390\/v4061011","article-title":"Mechanisms of coronavirus cell entry mediated by the viral spike protein","volume":"4","author":"Belouzard","year":"2012","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib138","doi-asserted-by":"crossref","first-page":"2176","DOI":"10.1080\/22221751.2022.2114850","article-title":"Furin cleavage is required for swine acute diarrhea syndrome coronavirus spike protein-mediated cell\u2013cell fusion","volume":"11","author":"Kim","year":"2022","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.jbc.2026.111250_bib139","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.virol.2006.02.003","article-title":"Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry","volume":"350","author":"Follis","year":"2006","journal-title":"Virology"},{"key":"10.1016\/j.jbc.2026.111250_bib140","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1007\/s13365-020-00913-5","article-title":"Potential neuroinvasive and neurotrophic properties of SARS-CoV-2 in pediatric patients: comparison of SARS-CoV-2 with non-segmented RNA viruses","volume":"26","author":"Chen","year":"2020","journal-title":"J. Neurovirol."},{"key":"10.1016\/j.jbc.2026.111250_bib141","doi-asserted-by":"crossref","first-page":"8077","DOI":"10.1128\/JVI.00356-15","article-title":"A single point mutation creating a furin cleavage site in the spike protein renders porcine epidemic diarrhea coronavirus trypsin independent for cell entry and fusion","volume":"89","author":"Li","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib142","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.3390\/v14081744","article-title":"PEDV: insights and advances into types, function, structure, and receptor recognition","volume":"14","author":"Lin","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib143","doi-asserted-by":"crossref","first-page":"7952","DOI":"10.1128\/JVI.00297-14","article-title":"Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture","volume":"88","author":"Wicht","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib144","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1007\/s00705-011-1044-6","article-title":"Receptor-bound porcine epidemic diarrhea virus spike protein cleaved by trypsin induces membrane fusion","volume":"156","author":"Park","year":"2011","journal-title":"Arch. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib145","doi-asserted-by":"crossref","DOI":"10.1016\/j.virol.2025.110453","article-title":"Revisiting the roles of trypsin in the productive infection of porcine deltacoronavirus in porcine-derived cells","volume":"604","author":"Xiao","year":"2025","journal-title":"Virology"},{"key":"10.1016\/j.jbc.2026.111250_bib146","doi-asserted-by":"crossref","first-page":"e00916","DOI":"10.1128\/jvi.00916-23","article-title":"N-linked glycoproteins and host proteases are involved in swine acute diarrhea syndrome coronavirus entry","volume":"97","author":"Chen","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib147","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1007\/s12250-020-00321-3","article-title":"Broad cell tropism of SADS-CoV in vitro implies its potential cross-species infection risk","volume":"36","author":"Luo","year":"2021","journal-title":"Virol. Sin."},{"key":"10.1016\/j.jbc.2026.111250_bib148","article-title":"DYRK1A: the double-edged kinase as a protagonist in cell growth and tumorigenesis","volume":"2","author":"Fern\u00e1ndez-Mart\u00ednez","year":"2015","journal-title":"Mol. Cell. Oncol"},{"key":"10.1016\/j.jbc.2026.111250_bib149","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3002097","article-title":"DYRK1A promotes viral entry of highly pathogenic human coronaviruses in a kinase-independent manner","volume":"21","author":"Strine","year":"2023","journal-title":"Plos Biol."},{"key":"10.1016\/j.jbc.2026.111250_bib150","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01239-23","article-title":"DYRK1A is a multifunctional host factor that regulates coronavirus replication in a kinase-independent manner","volume":"98","author":"Fu","year":"2024","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib151","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a041053","article-title":"The death receptor pathway of apoptosis","volume":"14","author":"Green","year":"2022","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.111250_bib152","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2417372122","article-title":"DR5 is a restriction factor for human herpesviruses","volume":"122","author":"Han","year":"2025","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib153","doi-asserted-by":"crossref","first-page":"2724","DOI":"10.3390\/v14122724","article-title":"Death receptor DR5 as a proviral factor for viral entry and replication of coronavirus PEDV","volume":"14","author":"Zhang","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.111250_bib154","doi-asserted-by":"crossref","first-page":"6869","DOI":"10.1007\/s00018-021-03938-z","article-title":"Control of the eIF4E activity: structural insights and pharmacological implications","volume":"78","author":"Romagnoli","year":"2021","journal-title":"Cell. Mol. Life. Sci."},{"key":"10.1016\/j.jbc.2026.111250_bib155","article-title":"Phospho-eIF4E stimulation regulates coronavirus entry by selective expression of cell membrane-residential factors","volume":"98","author":"Zhang","year":"2024","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib156","doi-asserted-by":"crossref","first-page":"2669","DOI":"10.1007\/s00705-015-2579-8","article-title":"Beyond RGD: virus interactions with integrins","volume":"160","author":"Hussein","year":"2015","journal-title":"Arch. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib157","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1038\/s41573-021-00284-4","article-title":"Emerging therapeutic opportunities for integrin inhibitors","volume":"21","author":"Slack","year":"2022","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.jbc.2026.111250_bib158","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41392-022-01259-6","article-title":"Targeting integrin pathways: mechanisms and advances in therapy","volume":"8","author":"Pang","year":"2023","journal-title":"Signal Transduct. Target. Ther."},{"key":"10.1016\/j.jbc.2026.111250_bib159","doi-asserted-by":"crossref","first-page":"3587","DOI":"10.1128\/JVI.72.5.3587-3594.1998","article-title":"Foot-and-mouth disease virus virulent for cattle utilizes the integrin \u03b1v\u03b23 as its receptor","volume":"72","author":"Neff","year":"1998","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.111250_bib160","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1038\/nm1236","article-title":"Integrin \u03b1v\u03b23 is a coreceptor for human cytomegalovirus","volume":"11","author":"Wang","year":"2005","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2026.111250_bib161","doi-asserted-by":"crossref","first-page":"14644","DOI":"10.1073\/pnas.250299897","article-title":"Integrin \u03b1v\u03b23 mediates rotavirus cell entry","volume":"97","author":"Guerrero","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111250_bib162","doi-asserted-by":"crossref","first-page":"54533","DOI":"10.1074\/jbc.M410208200","article-title":"Interaction of West Nile virus with \u03b1v\u03b23 integrin mediates virus entry into cells","volume":"279","author":"Chu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111250_bib163","doi-asserted-by":"crossref","DOI":"10.1016\/j.vetmic.2019.108400","article-title":"Integrin \u03b1v\u03b23 enhances replication of porcine epidemic diarrhea virus on vero E6 and porcine intestinal epithelial cells","volume":"237","author":"Li","year":"2019","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.111250_bib164","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ceb.2015.12.001","article-title":"The ESCRT machinery: new roles at new holes","volume":"38","author":"Olmos","year":"2016","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.jbc.2026.111250_bib165","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/s41580-019-0177-4","article-title":"The many functions of ESCRTs","volume":"21","author":"Vietri","year":"2020","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"10.1016\/j.jbc.2026.111250_bib166","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1012103","article-title":"ALIX and TSG101 are essential for cellular entry and replication of two porcine alphacoronaviruses","volume":"20","author":"Chen","year":"2024","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111250_bib167","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s11248-018-0100-3","article-title":"Resistance to coronavirus infection in amino peptidase N-deficient pigs","volume":"28","author":"Whitworth","year":"2019","journal-title":"Transgenic Res."},{"key":"10.1016\/j.jbc.2026.111250_bib168","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-49838-y","article-title":"Aminopeptidase N-null neonatal piglets are protected from transmissible gastroenteritis virus but not porcine epidemic diarrhea virus","volume":"9","author":"Luo","year":"2019","journal-title":"Sci. Rep."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826001201?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826001201?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T23:15:08Z","timestamp":1776381308000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826001201"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":168,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2026,3]]}},"alternative-id":["S0021925826001201"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.111250","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cell entry mechanisms of porcine enteric coronaviruses","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.111250","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"111250"}}