参考文献/References:
[1]SCHALK A F, HAWN M C. An apparently new respiratory disease of baby chicks[J]. Journal of the American Veterinary Medical Association,1931,78:413-422.
[2]ALMEIDA J D, TYRRELL D A. The morphology of three previously uncharacterized human respiratory viruses that grow in organ culture[J]. Journal of General Virology,1967,1(2):175-178.
[3]MCINTOSH K, KAPIKIAN A Z, TURNER H C, et al. Seroepidemiologic studies of coronavirus infection in adults and children[J]. American Journal of Epidemiology,1970,91(6):585-592.
[4]GRAHAM R L, BARIC R S. Recombination, reservoirs, and the modular spike:mechanisms of coronavirus cross-species transmission[J]. Journal of Virology,2010,84(7):3134-3146.
[5]LI W H, WONG S K, LI F, et al. Animal origins of the severe acute respiratory syndrome coronavirus:insight from ACE2-S-protein interactions[J]. Journal of Virology,2006,80(9):4211-4219.
[6]LI F. Receptor recognition and cross-species infections of SARS coronavirus[J]. Antiviral Research,2013,100(1):246-254.
[7]CHAN J F, TO K K, TSE H, et al. Interspecies transmission and emergence of novel viruses:lessons from bats and birds[J]. Trends in Microbiology,2013,21(10):544-555.
[8]WOO P C, LAU S K, LAM C S, et al. Discovery of seven novel Mammalian and avian coronaviruses in the genus deltacoronavirus supports bat coronaviruses as the gene source of alphacoronavirus and betacoronavirus and avian coronaviruses as the gene source of gammacoronavirus and deltacoronavirus[J]. Journal of Virology,2012,86(7):3995-4008.
[9]CORMAN V M, BALDWIN H J, TATENO A F, et al. Evidence for an ancestral association of human coronavirus 229E with bats[J]. Journal of Virology,2015,89(23):11858-11870.
[10]CUI J, LI F, SHI Z L. Origin and evolution of pathogenic coronaviruses[J]. Nature Reviews Microbiology,2019,17(3):181-192.
[11]GUAN Y, ZHENG B J, HE Y Q, et al. Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China[J]. Science,2003,302(5643):276-278.
[12]ALAGAILI A N, BRIESE T, MISHRA N, et al. Middle East respiratory syndrome coronavirus infection in dromedary camels in Saudi Arabia[J]. mBio,2014,5(2):e00884-14.
[13]VIJGEN L, KEYAERTS E, LEMEY P, et al. Evolutionary history of the closely related group 2 coronaviruses:porcine hemagglutinating encephalomyelitis virus, bovine coronavirus, and human coronavirus OC43[J]. Journal of Virology,2006,80(14):7270-7274.
[14]ZHOU P, FAN H, LAN T, et al. Fatal swine acute diarrhoea syndrome caused by an HKU2-related coronavirus of bat origin[J]. Nature,2018,556(7700):255-258.
[15]NAKAGAKI K, NAKAGAKI K, TAGUCHI F. Receptor-independent spread of a highly neurotropic murine coronavirus JHMV strain from initially infected microglial cells in mixed neural cultures[J]. Journal of Virology,2005,79(10):6102-6110.
[16]STODDART C A, SCOTT F W. Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence[J]. Journal of Virology,1989,63(1):436-440.
[17]LI F. Receptor recognition mechanisms of coronaviruses:a decade of structural studies[J]. Journal of Virology,2015,89(4):1954-1964.
[18]YANG T J, CHANG Y C, KO T P, et al. Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans[J]. Proceedings of the National Academy of Sciences of the United States of America,2020,117(3):1438-1446.
[19]REGUERA J, SANTIAGO C, MUDGAL G, et al. Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies[J]. PLoS Pathogens,2012,8(8):e1002859.
[20]HUANG C Y, DRACZKOWSKI P, WANG Y S, et al. In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM[J]. Nature Communications,2022,13(1):1-15.
[21]GUAN H X, WANG Y W, PERCULIJA V, et al. Cryo-electron microscopy structure of the swine acute diarrhea syndrome coronavirus spike glycoprotein provides insights into evolution of unique coronavirus spike proteins[J]. Journal of Virology,2020,94(22):1-13.
[22]SONG X Y, SHI Y J, DING W, et al. Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes[J]. Nature Communications,2021,12(1):1-9.
[23]WU K L, LI W K, PENG G Q, et al. Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor[J]. Proceedings of the National Academy of Sciences of the United States of America,2009,106(47):19970-19974.
[24]SHI J C, HU S Y, WEI H L, et al. Dipeptidyl peptidase 4 interacts with porcine coronavirus PHEV spikes and mediates host range expansion[J]. Journal of Virology,2024,98(7):1-17.
[25]MAH M G, ZELLER M A, ZHANG R, et al. Discordant phylodynamic and spatiotemporal transmission patterns driving the long-term persistence and evolution of human coronaviruses[J]. Npj Viruses,2024,2(1):1-16.
[26]KIRCHDOERFER R N, COTTRELL C A, WANG N S, et al. Pre-fusion structure of a human coronavirus spike protein[J]. Nature,2016,531(7592):118-121.
[27]YUAN Y, CAO D F, ZHANG Y F, et al. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains[J]. Nature Communications,2017,8:1-9.
[28]CAI Y F, ZHANG J, XIAO T S, et al. Distinct conformational states of SARS-CoV-2 spike protein[J]. Science,2020,369(6511):1586-1592.
[29]SHANG J, ZHENG Y, YANG Y, et al. Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins[J]. PLoS Pathogens,2018,14(4):1-19.
[30]SHANG J, ZHENG Y, YANG Y, et al. Cryo-electron microscopy structure of porcine deltacoronavirus spike protein in the prefusion state[J]. Journal of Virology,2018,92(4):1-14.
[31]SCHULTZE B , GROSS H J, BROSSMER R, et al. The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant[J]. Journal of Virology,1991,65(11):6232-6237.
[32]PENG G Q, XU L Q, LIN Y L, et al. Crystal structure of bovine coronavirus spike protein lectin domain[J]. Journal of Biological Chemistry,2012,287(50):41931-41938.
[33]SEYRAN M, TAKAYAMA K, UVERSKY V N, et al. The structural basis of accelerated host cell entry by SARS-CoV-2dagger[J]. FEBS Journal,2021,288(17):5010-5020.
[34]FANTINI J, DI SCALA C, CHAHINIAN H, et al. Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection[J]. International Journal of Antimicrobial Agents,2020,55(5):1-8.
[35]PARK Y J, WALLS A C, WANG Z Q, et al. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors[J]. Nature Structural & Molecular Biology,2019,26(12):1151-1157.
[36]AWASTHI M, GULATI S, SARKAR D P, et al. The sialoside-binding pocket of SARS-CoV-2 spike glycoprotein structurally resembles MERS-CoV[J]. Viruses,2020,12(9):1-10.
[37]MILANETTI E, MIOTTO M, DI RIENZO L, et al. In-silico evidence for a two receptor based strategy of SARS-CoV-2[J]. Frontiers in Molecular Biosciences,2021,8:1-11.
[38]PENG G Q, SUN D W, RAJASHANKAR K R, et al. Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor[J]. Proceedings of the National Academy of Sciences of the United States of America,2011,108(26):10696-10701.
[39]WRAPP D, MCLELLAN J S. The 3.1-angstrom cryo-electron microscopy structure of the porcine epidemic diarrhea virus spike protein in the prefusion conformation[J]. Journal of Virology,2019,93(23):1-13.
[40]KIRCHDOERFER R N, BHANDARI M, MARTINI O, et al. Structure and immune recognition of the porcine epidemic diarrhea virus spike protein[J]. Structure,2021,29(4):385-392.
[41]ZHANG K M, LI S S, PINTILIE G, et al. A 3.4-A cryo-electron microscopy structure of the human coronavirus spike trimer computationally derived from vitrified NL63 virus particles[J]. Quality Review Board,2020,1:e11.
[42]WALLS A C, TORTORICI M A, FRENZ B, et al. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy[J]. Nature Structural & Molecular Biology,2016,23(10):899-905.
[43]SONG W F, GUI M, WANG X Q, et al. Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2[J]. PLoS Pathogens,2018,14(8):1-19.
[44]GUI M, SONG W F, ZHOU H X, et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding[J]. Cell Research,2017,27(1):119-129.
[45]LU G W, HU Y W, WANG Q H, et al. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26[J]. Nature,2013,500(7461):227-231.
[46]WANG N S, SHI X L, JIANG L W, et al. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4[J]. Cell Research,2013,23(8):986-993.
[47]CHEN Y Q, RAJASHANKAR K R, YANG Y, et al. Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus[J]. Journal of Virology,2013,87(19):10777-10783.
[48]TRESNAN D B, LEVIS R, HOLMES K V. Feline aminopeptidase N serves as a receptor for feline,canine,porcine,and human coronaviruses in serogroup I[J]. Journal of Virology,1996,70(12):8669-8674.
[49]REGAN A D, WHITTAKER G R. Utilization of DC-SIGN for entry of feline coronaviruses into host cells[J]. Journal of Virology,2008,82(23):11992-11996.
[50]DE HAAN C A, HAIJEMA B J, SCHELLEN P, et al. Cleavage of group 1 coronavirus spike proteins:how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation[J]. Journal of Virology,2008,82(12):6078-6083.
[51]DELMAS B, GELFI J, L’HARIDON R, et al. Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV[J]. Nature,1992,357(6377):417-420.
[52]KREMPL C, SCHULTZE B, LAUDE H, et al. Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus[J]. Journal of Virology,1997,71(4):3285-3287.
[53]HUAN C C, WANG Y, NI B, et al. Porcine epidemic diarrhea virus uses cell-surface heparan sulfate as an attachment factor[J]. Archives of Virology,2015,160(7):1621-1628.
[54]ZHAO P W, XU L D, ZHANG Y T, et al. 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[J]. Microbial Pathogenesis,2021,157:104956.
[55]PENG J Y, PUNYADARSANIYA D, SHIN D L, et al. The cell tropism of porcine respiratory coronavirus for airway epithelial cells is determined by the expression of porcine aminopeptidase N[J]. Viruses,2020,12(11):1-12.
[56]LI F. Structure, Function, and evolution of coronavirus spike proteins[J]. Annual Review of Virology,2016,3(1):237-261.
[57]YANG Y L, WANG B, LI W T, et al. Functional dissection of the spike glycoprotein S1 subunit and identification of cellular cofactors for regulation of swine acute diarrhea syndrome coronavirus entry[J]. Journal of Virology,2024,98(4):1-22.
[58]YEAGER C L, ASHMUN R A, WILLIAMS R K, et al. Human aminopeptidase N is a receptor for human coronavirus 229E[J]. Nature,1992,357(6377):420-422.
[59]LI Z J, TOMLINSON A C, WONG A H, et al. The human coronavirus HCoV-229E S-protein structure and receptor binding[J]. Elife,2019,8:1-22.
[60]FUOCHI V, FLORESTA G, EMMA R, et al. Heparan sulfate and enoxaparin interact at the interface of the spike protein of HCoV-229E but not with HCoV-OC43[J]. Viruses,2023,15(3):1-16.
[61]HOFMANN H, PYRC K, VAN DER HOEK L, et al. Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry[J]. Proceedings of the National Academy of Sciences of the United States of America,2005,102(22):7988-7993.
[62]MILEWSKA A, ZAREBSKI M, NOWAK P, et al. Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells[J]. Journal of Virology,2014,88(22):13221-13230.
[63]HOFMANN H, SIMMONS G, RENNEKAMP A J, et al. Highly conserved regions within the spike proteins of human coronaviruses 229E and NL63 determine recognition of their respective cellular receptors[J]. Journal of Virology,2006,80(17):8639-8652.
[64]SCHULTZE B, HERRLER G. Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells[J]. Journal of General Virology,1992,73(Pt4):901-906.
[65]TAGUCHI F, HIRAI-YUKI A. Mouse hepatitis virus receptor as a determinant of the mouse susceptibility to MHV infection[J]. Frontiers in Microbiology,2012,3(68):1-4.
[66]QING E, HANTAK M, PERLMAN S, et al. Distinct roles for sialoside and protein receptors in coronavirus infection[J]. mBio,2020,11(1):1-18.
[67]SCHICKLI J H, THACKRAY L B, SAWICKI S G, et al. The N-terminal region of the murine coronavirus spike glycoprotein is associated with the extended host range of viruses from persistently infected murine cells[J]. Journal of Virology,2004,78(17):9073-9083.
[68]DE HAAN C A, LI Z, TE LINTELO E, et al. Murine coronavirus with an extended host range uses heparan sulfate as an entry receptor[J]. Journal of Virology,2005,79(22):14451-14456.
[69]HULSWIT R J G, LANG Y F, BAKKERS M J G, et al. Human coronaviruses OC43 and HKU1 bind to 9-O-acetylated sialic acids via a conserved receptor-binding site in spike protein domain A[J]. Proceedings of the National Academy of Sciences of the United States of America,2019,116(7):2681-2690.
[70]TORTORICI M A, WALLS A C, LANG Y F, et al. Structural basis for human coronavirus attachment to sialic acid receptors[J]. Nature Structural & Molecular Biology,2019,26(6):481-489.
[71]SAUNDERS N, FERNANDEZ I, PLANCHAIS C, et al. TMPRSS2 is a functional receptor for human coronavirus HKU1[J]. Nature,2023,624(7990):207-214.
[72]MCCALLUM M, PARK Y J, STEWART C, et al. Human coronavirus HKU1 recognition of the TMPRSS2 host receptor[J]. Cell,2024,187(16):4231-4245.
[73]LI W H, MOORE M J, VASILIEVA N, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus[J]. Nature,2003,426(6965):450-454.
[74]ZHOU P, YANG X L, WANG X G, et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin[J]. Nature,2020,579(7798):270-273.
[75]LANG J S, YANG N, DENG J J, et al. Inhibition of SARS pseudovirus cell entry by lactoferrin binding to heparan sulfate proteoglycans[J]. PLoS One,2011,6(8):1-11.
[76]JEFFERS S A, TUSELL S M, GILLIM-ROSS L, et al. CD209L(L-SIGN)is a receptor for severe acute respiratory syndrome coronavirus[J]. Proceedings of the National Academy of Sciences of the United States of America,2004,101(44):15748-15753.
[77]HAN D P, LOHANI M, CHO M W. Specific asparagine-linked glycosylation sites are critical for DC-SIGN- and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry[J]. Journal of Virology,2007,81(21):12029-12039.
[78]HOFFMANN M, KLEINE-WEBER H, SCHROEDER S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor[J]. Cell,2020,181(2):271-280.
[79]LAN J, CHEN P, LIU W M, et al. Structural insights into the binding of SARS-CoV-2,SARS-CoV,and hCoV-NL63 spike receptor-binding domain to horse ACE2[J]. Structure,2022,30(10):1432-1442.
[80]SUN X L. The role of cell surface sialic acids for SARS-CoV-2 infection[J]. Glycobiology,2021,31(10):1245-1253.
[81]DALY J L, SIMONETTI B, KLEIN K, et al. Neuropilin-1 is a host factor for SARS-CoV-2 infection[J]. Science,2020,370(6518):861-865.
[82]CANTUTI-CASTELVETRI L, OJHA R, PEDRO L D, et al. Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity[J]. Science,2020,370(6518):856-860.
[83]RAHIMI N. C-type Lectin CD209L/L-SIGN and CD209/DC-SIGN:cell adhesion molecules turned to pathogen recognition receptors[J]. Biology (Basel),2020,10(1):1-15.
[84]WIDAGDO W, OKBA N M A, LI W, et al. Species-specific colocalization of middle east respiratory syndrome coronavirus attachment and entry receptors[J]. Journal of Virology,2019,93(16):1-12.
[85]LI W T, HULSWIT R J G, WIDJAJA I, et al. Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein[J]. Proceedings of the National Academy of Sciences of the United States of America,2017,114(40):E8508-E8517.
[86]WINTER C, SCHWEGMANN-WESSELS C, CAVANAGH D, et al. Sialic acid is a receptor determinant for infection of cells by avian Infectious bronchitis virus[J]. Journal of General Virology,2006,87:1209-1216.DOI:10.1099/vir.0.81651-0.
[87]MADU I G, CHU V C, LEE H, et al. Heparan sulfate is a selective attachment factor for the avian coronavirus infectious bronchitis virus Beaudette[J]. Avian Diseases,2007,51(1):45-51.
[88]BICKERTON E, MAIER H J, STEVENSON-LEGGETT P, et al. The S2 subunit of infectious bronchitis virus beaudette is a determinant of cellular tropism[J]. Journal of Virology,2018,92(19):1-18.
[89]ZHANG Y T, BUCKLES E, WHITTAKER G R. Expression of the C-type lectins DC-SIGN or L-SIGN alters host cell susceptibility for the avian coronavirus,infectious bronchitis virus[J]. Veterinary Microbiology,2012,157(3/4):285-293.
[90]WANG B, LIU Y, JI C M, et al. Porcine deltacoronavirus engages the transmissible gastroenteritis virus functional receptor porcine aminopeptidase N for infectious cellular entry[J]. Journal of Virology,2018,92(12):1-13.
[91]LI W T, HULSWIT R J G, KENNEY S P, et al. Broad receptor engagement of an emerging global coronavirus may potentiate its diverse cross-species transmissibility[J]. Proceedings of the National Academy of Sciences of the United States of America,2018,115(22):E5135-E5143.
[92]JI W W, PENG Q, FANG X Q, et al. Structures of a deltacoronavirus spike protein bound to porcine and human receptors[J]. Nature Communications,2022,13(1467):1-11.
[93]LIU Y, WANG B, LIANG Q Z, et al. Roles of two major domains of the porcine deltacoronavirus S1 subunit in receptor binding and neutralization[J]. Journal of Virology,2021,95(24):1-17.
[94]XIAO W W, HUANG W, CHEN C Q, et al. Porcine deltacoronavirus uses heparan sulfate as an attachment receptor[J]. Veterinary Microbiology,2023,276:109616.
[95]NOCEK B, MULLIGAN R, BARGASSA M, et al. Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis[J]. Proteins,2008,70(1):273-279.
[96]LUAN Y P, XU W F. The structure and main functions of aminopeptidase N[J]. Current Medicinal Chemistry,2007,14(6):639-647.
[97]CHEN L, LIN Y L, PENG G Q, et al. Structural basis for multifunctional roles of mammalian aminopeptidase N [J]. Proceedings of the National Academy of Sciences of the United States of America,2012,109 (44):17966-17971.
[98]TRESNAN D B, HOLMES K V. Feline aminopeptidase N is a receptor for all group I coronaviruses[J]. Advances in Experimental Medicine and Biology,1998,440:69-75.
[99]CHEN L, LIN Y L, PENG G Q, et al. Structural basis for multifunctional roles of mammalian aminopeptidase N[J]. Proceedings of the National Academy of Sciences of the United States of America,2012,109(44):17966-17971.
[100]TUSELL S M, SCHITTONE S A, HOLMES K V. Mutational analysis of aminopeptidase N, a receptor for several group 1 coronaviruses, identifies key determinants of viral host range[J]. Journal of Virology,2007,81(3):1261-1273.