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[[File:SARS virion.gif|thumb|SARS-CoV dưới kính hiển vi|upright]]
TheHình morphologythái ofcủa the SARSSARSr-relatedCoV coronavirustuân istheo characteristictính ofchất thechung coronaviruscủa familyhọ asvirus a wholecorona. TheVirus virusescó aredạng largecác [[Pleomorphismhạt (cytology)|pleomorphic]]đa sphericalhình particleslớn withvới bulbouscấu surfacetrúc projectionsbề thatmặt rộng tạo formthành ahào quang (corona) aroundxung thequanh particleskhi innhìn từ kính hiển vi electronđiện micrographstử.<ref>{{cite journal | vauthors = Goldsmith CS, Tatti KM, Ksiazek TG, Rollin PE, Comer JA, Lee WW, Rota PA, Bankamp B, Bellini WJ, Zaki SR | display-authors = 6 | title = Ultrastructural characterization of SARS coronavirus | journal = Emerging Infectious Diseases | volume = 10 | issue = 2 | pages = 320–6 | date = February 2004 | pmid = 15030705 | pmc = 3322934 | doi = 10.3201/eid1002.030913 | quote = Virions acquired an envelope by budding into the cisternae and formed mostly spherical, sometimes pleomorphic, particles that averaged 78 nm in diameter (Figure 1A). }}</ref> TheKích sizethước ofcác thehạt virus particlestrong is in thekhoảng 80–90 nm range. The envelope of the virus in electron micrographs appears as a distinct pair of electron dense shells.<ref>{{cite journal | vauthors = Neuman BW, Adair BD, Yoshioka C, Quispe JD, Orca G, Kuhn P, Milligan RA, Yeager M, Buchmeier MJ | display-authors = 6 | title = Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy | journal = Journal of Virology | volume = 80 | issue = 16 | pages = 7918–28 | date = August 2006 | pmid = 16873249 | pmc = 1563832 | doi = 10.1128/JVI.00645-06 | quote = Particle diameters ranged from 50 to 150 nm, excluding the spikes, with mean particle diameters of 82 to 94 nm; Also See Figure 1 for double shell. }}</ref>
The [[viralMàng envelopebọc virus]] consistsbao ofgồm amột [[lớp lipid bilayerkép]] wherelà thenơi các protein membranemàng (M), envelopemàng bọc (E) andvà [[Peplomer|spikegai (S)]] proteins arebám anchoredvào.<ref name="Lai_1997">{{cite journal | vauthors = Lai MM, Cavanagh D | title = The molecular biology of coronaviruses | journal = Advances in Virus Research | volume = 48 | issue = | pages = 1–100 | date = 1997 | pmid = 9233431 | doi = 10.1016/S0065-3527(08)60286-9 | isbn = 9780120398485 }}</ref> TheCác spikeprotein proteinsgai providegiúp thecho virus withcó itsđược bulbouscấu surfacetrúc projectionsbề mặt rộng. TheSự spiketương tác của protein's interactiongai withvới itsthụ complementthể [[Viraltương entry|hostứng cellcủa receptor]]tế isbào centralchủ inlà điểm quan trọng trong determiningviệc thexác định [[tissue tropism]], [[infectivity]], and [[Host tropism|species range]] of thecủa virus.<ref>{{cite book | vauthors = Masters PS | title = The molecular biology of coronaviruses | volume = 66 | pages = 193–292 | date = 2006-01-01 | pmid = 16877062 | doi = 10.1016/S0065-3527(06)66005-3 | publisher = Academic Press | isbn = 9780120398690 | quote = Nevertheless, the interaction between S protein and receptor remains the principal, if not sole, determinant of coronavirus host species range and tissue tropism. | series = Advances in Virus Research }}</ref><ref>{{cite journal | vauthors = Cui J, Li F, Shi ZL | title = Origin and evolution of pathogenic coronaviruses | journal = Nature Reviews. Microbiology | volume = 17 | issue = 3 | pages = 181–192 | date = March 2019 | pmid = 30531947 | doi = 10.1038/s41579-018-0118-9 | quote = Different SARS-CoV strains isolated from several hosts vary in their binding affinities for human ACE2 and consequently in their infectivity of human cells76,78 (Fig. 6b) }}</ref>
InsideBên trong themàng envelope,bọc there is thelà [[Capsidvỏ bọc|nucleocapsidvỏ bọc nhân]], whichđược iscấu formedtạo fromtừ multiplenhiều copiesbản ofsao theprotein nucleocapsid (N) protein, whichcó aretác bounddụng tobảo thevệ positive-sensecho single-strandedbộ gen ARN chuỗi đơn dương (~30 [[BaseCặp pairbazơ|kb]]) RNAđược genometổ inchức adưới continuousdạng [[Bead|beads-on-a-string]]chuỗi typeliên conformationtục.<ref>{{cite journal | vauthors = Fehr AR, Perlman S | title = An Overview of Their Replication and Pathogenesis; Section 2 Genomic Organization | journal = Methods in Molecular Biology | volume = 1282 | pages = 1–23 | date = 2015 | pmid = 25720466 | pmc = 4369385 | doi = 10.1007/978-1-4939-2438-7_1 | publisher = Springer | isbn = 978-1-4939-2438-7 | editor-first = Helena Jane | editor-last = Maier | editor2-first = Erica | editor2-last = Bickerton | editor3-first = Paul | editor3-last = Britton | name-list-format = vanc | quote = See section: Virion Structure. }}</ref><ref>{{cite journal | vauthors = Chang CK, Hou MH, Chang CF, Hsiao CD, Huang TH | title = The SARS coronavirus nucleocapsid protein--forms and functions | journal = Antiviral Research | volume = 103 | pages = 39–50 | date = March 2014 | pmid = 24418573 | doi = 10.1016/j.antiviral.2013.12.009 | quote = See Figure 4c. }}</ref> TheLớp màng lipid bilayer envelopekép, membranecác proteins,protein andmàng nucleocapsidvà protectvỏ thebọc virusnhân bảo vệ cho virus whenkhi itở isbên outsidengoài thevật hostchủ.<ref>{{cite journal | vauthors = Neuman BW, Kiss G, Kunding AH, Bhella D, Baksh MF, Connelly S, Droese B, Klaus JP, Makino S, Sawicki SG, Siddell SG, Stamou DG, Wilson IA, Kuhn P, Buchmeier MJ | display-authors = 6 | title = A structural analysis of M protein in coronavirus assembly and morphology | journal = Journal of Structural Biology | volume = 174 | issue = 1 | pages = 11–22 | date = April 2011 | pmid = 21130884 | pmc = 4486061 | doi = 10.1016/j.jsb.2010.11.021 | quote = See Figure 10. }}</ref>
== Vòng đời ==
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