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       11 2020.       2019-nCov ( novel coronavirus,  ),     COVID-19 ( coronavirus disease,  ).   ,           ,    .              ,  , ,       .   ,       .

      . ,      20092010  ,   ,     .         頖      H1N1      (      ),     -     .       ,    -    :  ,  ,       ,         .   ,        ,         .           (  cairo garbage,   ).

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    ( MERS Middle East Respiratory Syndrome    ),          ,      .       (,   ),    (,   ..),    (, ),   .      (1, 2, 3, I, II, III, , ).     ,  ,  ,    -    (  , ?).       .   .


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          ࠖ  .   ,       ,     .         ,           (,     ,     ).     ,      ,         ,      .     [2 -               .   :   ,   ,            .      ,      / .              .]  蠖 ,  -  -,    ,   ,    , , ,    .  ,           ,      .             .     ,       ,   .     :  -    (!)  ,   [1 - S.Duffy, Why are RNA virus mutation rates so damn high? PloS Biol., vol. 16, no. 8, p. e3000003, Aug. 2018.].        :      ,  ,                .   -   ,      (      ,    ).    ,       .

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   ⠖   .    ,     , ,    [2 - C. A. Suttle, Viruses in the sea, Nature, vol. 437, no. 7057, pp. 356361, Sep. 2005.],       .     30 .      , , ,      .  , ,    ,    :    ,      . , , , , 蠖    :      ,   .         ,           ,     .     SARS-CoV-2.




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     ,          .  ,        蠖         , , ,       ,   .                      , ,   ,       .     - :      D   1700  ( ).  :    3  .

      ,       :     29000 .    SARS-CoV-229900 ,    16 .    ,     ,    ,    ,       ,       .               :    ,       ,          .             .






.2.  SARS-CoV-2       95       -  120130   .     ,     N-ࠖ          . SARS-CoV-2           SARS    20%.        RaTG13    96%.  ,          ,     SARS-CoV-2



      .   SARS-CoV-2    ,     .        120 ,   . ,         (  ),  -             [3 -   ,  SASR-CoV-2  ,  ,  ,     .      -   .].       ,   -,  S- (  spike ).        -,      .  堖   M- (  membrane protein,  ).   E- (  envelope protein,  ),        . M-, S-  E-    () ,        .     ,        .      ,     :  ⠖   ,   ,     .     ,     N- (  nucleocapsid protein,  ).   .







   ,   SARS-CoV-2   ,       -.  ,     ,   ACE2, , -, 2,    -  2.   -  1 (1,  ACE) ACE2     - ,    .     ,       ,   , :  , ACE2             .

 ACE2  [4 -    ,     .],       ,       .      ,  ,   (),    [5 -       :  ACE2   ,   ,       ?    :    .    ,            ,         .   SARS  c  ,       ACE2 (E. Braun and D. Sauter, Furin-mediated protein processing in infectious diseases and cancer, Clin. Transl. Immunol., vol. 8, no. 8, Jan. 2019.),             .].   ,  SARS-CoV-2      ,  ,  ,    , ,     .      -   :     ,    ,      .      ,     , SARS-CoV-2   .

       ACE2    S-.      ,        S1-.     RBD- (receptor binding domain ,     ),      ACE2,      .          .




 

ACE2   ,    SARS-CoV-2    .   2020  [3 - K. Wang et al., SARS-CoV-2 invades host cells via a novel route: CD147-spike protein, bioRxiv, p. 2020.03.14.988345, Jan. 2020.],        CD147.   : CD147        .       ,    ,         [4 - X. Wang et al., SARS-CoV-2 infects T lymphocytes through its spike protein-mediated membrane fusion, Cell. Mol. Immunol., Apr. 2020.],   .     ,      CD147 ,  , -   .          ,            SARS-CoV-2. , ,     蠖         .  ,   SARS-CoV-2   ,          .


     ACE2    . ,    ,   ,    ,          .    [6 - :        , ,      .           (   )   .     .]  ,     :      [7 -     ,   .  -   ,     ,    -  .     ,     ,     ,  .     ,    ,  ,  ,     .         ( , ,     ),     ,    ,       ,  ,       .] ,  .      ,          ⠖   .         ,             ,  ,          .                .      ,   ,     ,        , ,   .            蠖         ,     .

   ,       ,     .          -.    SARS-CoV-2    ,     젖     S-   .  ,    ()     ,                   頖   ,      ,   .   ,      ,          [5 - H. Wang et al., SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway, Cell Res., vol. 18, no. 2, pp. 290301, Feb. 2008.].      ,      .

        : ,     SARS (,      20022004)     TMPRSS2.  SARS-CoV-2    .   -   ,  TMPRSS2,  ,     . ,             ,   :  - TMPRSS2  ,      [6 - M. Hoffmann et al., SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor, Cell, vol. 181, no. 2, pp. 271280.e8, Apr. 2020.].  ,    SARS-CoV-2    .    ,      ,    , RBD-.    -    -,           .     RBD-        ,          , ,     ,      [7 - J. Shang et al., Cell entry mechanisms of SARS-CoV-2, Proc. Natl. Acad. Sci., vol. 117, no. 21, pp. 1172711734, May 2020.].




 

       .    ,       .  ( )    , ,     .         .              ,      ,      .         ,                     .       ():              .  ,       ,  ,     ,        .

      :        .           ,          ,      (     ,         ).           ,      ,       [8 - E. Braun and D. Sauter, Furin-mediated protein processing in infectious diseases and cancer, Clin. Transl. Immunol., vol. 8, no. 8, Jan. 2019.].

 ,          ,  ,             ,        .    堖 -      ⠖            COVID-19,        ,      SARS-CoV-2.      (,   )     ,       [9 - K. Kuba, Y. Imai, and J. M. Penninger, Multiple Functions of Angiotensin-Converting Enzyme 2 and Its Relevance in Cardiovascular Diseases, Circ. J., vol. 77, no. 2, pp. 301308, 2013.][10 - T. Ivanova et al., Optimization of Substrate-Analogue Furin Inhibitors, ChemMedChem, vol. 12, no. 23, pp. 19531968, Dec. 2017.].








  蠖  .  ࠖ      ,       .        [11 - Y. M. Bar-On, A. Flamholz, R. Phillips, and R. Milo, SARS-CoV-2 (COVID-19) by the numbers, Elife, vol. 9, Apr. 2020.]     ,     .       ,   ,          .    ,           .             ,     .         ,  (   )   .          :     .               ,      .       ,  ,        ,   .         .




  

         .        ,     .            ࠖ   .      1,         .       20 ,          .   ,       .         .     ,      ,        ,              .                ,         -   ,      .

          ,    .   -      ,     .     ,      .    .       ,   .       , ,     ,       ,   .  ,    ,     ,            .   SARS-CoV-2      ORF1a  ORF1b (..3). ORF1a         -. ORF1b ,         ORF1a ,         -   ORF1b.  ,           ORF1a    ORF1ab,     ORF1a    ,    ,    ORF1b.





.3.          SARS-CoV-2    .   ,         .         ORF1a  ORF1b,    ORF1b   ORF1a,     .         (  3-)        - -    ,      .      3-,      TRS-B,          TRS-L,   ,    堖    TRS-B.

UTR untranslated region,  ,   .    ,       .

PolyA ()-,  ,    .       



           ORF1a  ORF1ab (..3),          - ,             .      ,    : 1)         2)   -   ,   .  ORF1a  ORF1ab      .      ,         - -               ,     .            .        :         (     ),           .  堖  ,     .




 

      SARS-CoV-2        . - -          (..3).  -       TRS (transcription-regulating sequence ,  ,   )     -   TRS.         TRS,       ,       .   堖  ,              .


    SARS-CoV-2       1.  nsp    (  non-structural proteins).        - -  ,    ,   nsp,            .      .
















  SARS-CoV-2    ,  , ,    蠖 ORF9c, ORF10  ORF14.     ,     .

[I] M.-P. Egloff et al., The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world, Proc. Natl. Acad. Sci., vol. 101, no. 11, pp. 37923796, Mar. 2004.

[II] Y. Wang et al., Coronavirus nsp10/nsp16 Methyltransferase Can Be Targeted by nsp10-Derived Peptide In Vitro and In Vivo To Reduce Replication and Pathogenesis, J. Virol., vol. 89, no. 16, pp. 8416 LP-8427, Aug. 2015.

[III]  .

[IV] V. D. Menachery, K. Debbink, and R. S. Baric, Coronavirus non-structural protein 16: Evasion, attenuation, and possible treatments, Virus Res., vol. 194, pp. 191199, Dec. 2014.

[V] K. Siu et al., Severe acute respiratory syndrome Coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC, FASEB J., vol. 33, no. 8, pp. 88658877, Aug. 2019.

[VI] Y. Konno et al., SARS-CoV-2 ORF3b is a potent interferon antagonist whose activity is further increased by a naturally occurring elongation variant, bioRxiv, p. 2020.05.11.088179, Jan. 2020.

[VII] D. Schoeman and B. C. Fielding, Coronavirus envelope protein: current knowledge, Virol. J., vol. 16, no. 1, p. 69, Dec. 2019.

[VIII] UniProtKB P59637 (VEMP_CVHSA). Envelope small membrane protein, UniProt. [Online]. Available: https://www.uniprot.org/uniprot/P59637 (https://www.uniprot.org/uniprot/P59637). [Accessed: 14-Aug-2020].

[XI] M. Frieman, B. Yount, M. Heise, S. A. Kopecky-Bromberg, P. Palese, and R. S. Baric, Severe Acute Respiratory Syndrome Coronavirus ORF6 Antagonizes STAT1 Function by Sequestering Nuclear Import Factors on the Rough Endoplasmic Reticulum/Golgi Membrane, J. Virol., vol. 81, no. 18, pp. 98129824, Sep. 2007.

[X] J. K. Taylor et al., Severe Acute Respiratory Syndrome Coronavirus ORF7a Inhibits Bone Marrow Stromal Antigen 2 Virion Tethering through a Novel Mechanism of Glycosylation Interference, J. Virol., vol. 89, no. 23, pp. 1182011833, Dec. 2015.

[XI] S. R. Schaecher and A. Pekosz, SARS Coronavirus Accessory Gene Expression and Function, in Molecular Biology of the SARS-Coronavirus, Berlin, Heidelberg: Springer Berlin Heidelberg, 2010, pp. 153166.

[XII] C.-S. Shi et al., SARS-Coronavirus Open Reading Frame-9b Suppresses Innate Immunity by Targeting Mitochondria and the MAVS/TRAF3/TRAF6 Signalosome, J. Immunol., vol. 193, no. 6, pp. 30803089, Sep. 2014.

[XIII] C.-S. Shi, N. R. Nabar, N.-N. Huang, and J. H. Kehrl, SARS-Coronavirus Open Reading Frame-8b triggers intracellular stress pathways and activates NLRP3 inflammasomes, Cell Death Discov., vol. 5, no. 1, p. 101, Dec. 2019.



   1,  ,         SARS-CoV-2.      .      ,   SARS.   SARS  SARS-CoV-2   79%[12 - K. B. Anand, S. Karade, S. Sen, and R. M. Gupta, SARS-CoV-2: Camazotzs Curse, Med. J. Armed Forces India, vol. 76, no. 2, pp. 136141, Apr. 2020.],        .  ,            . ,     SARS-CoV-2    ,              [13 - D. E. Gordon et al., A SARS-CoV-2 protein interaction map reveals targets for drug repurposing, Nature, vol. 583, no. 7816, pp. 459468, Jul. 2020.].     ,      ,        ,     .

       .  nsp14 ,   ,     .     ,  -     .        ʠ     - -, ,      .  , ,  -,    ,     [8 -       ,  -   : ,     .].  ,     :    ,     ,           .    - (  proofreading,    ,      ).     -    .          䠖     ,  ,   ,      .       SARS, , ,     .   ,     -    .




 

 SARS-CoV-2          .       (.. 1).       ,     ,      ,      ( ),     -.       SARS  MERS,       :  ORF8  ,          [14 - Y. Zhang et al., The ORF8 Protein of SARS-CoV-2 Mediates Immune Evasion through Potently Downregulating MHCI, bioRxiv, p. 2020.05.24.111823, Jan. 2020.].     ,         , ,           .    ࠖ                  - (  -).        ,      ,            MHC I (major histocompatibility complex class I,      I). -    MHC I, ,  -       (     ,     -),   . ORF8    MHC I,        I      ,      .   MHC I, SARS-CoV-2 ,  -        -   .

      ,    .        MHC I      , ,   ,    ,          .       SARS-CoV-2:    ,           ,             .





  


       : SARS-CoV-2         蠖  .   ,       ,    .            -,       .             .           .    SARS-CoV-2    ,     N-  ʠ     .       ꠖ  ,         ,     .    ,         .    .






.4.    -     ACE2 (1),     TMPRSS2   (   )        .  ,         ((2),  ),    ,        ((2),  ).   ,      ,       ,           (3).      ⠖ ,        (4).      - -,          (5.)        (5.).     ,       (6).     ,           ,       N- (7).   ()        ,    ,        (8)






 SARS-CoV-2  


      ,          .                 [9 - , ,          100% .].          . ,    ,    ,  蠖 SARS, MERS   SARS-CoV-2   ,     . SARS  10%  , MERS 34%,  SARS-CoV-2 , ,  1%  (      ,     ).         ⠖ SARS-CoV-2,         . SARS    MERS    .

               SARS-CoV-2?       [15 - A. B. Gussow, N. Auslander, G. Faure, Y. I. Wolf, F. Zhang, and E. V. Koonin, Genomic determinants of pathogenicity in SARS-CoV-2 and other human coronaviruses, Proc. Natl. Acad. Sci., vol. 117, no. 26, pp. 1519315199, Jun. 2020.]        .      ,      .           11 ,      .     N-堖       ʠ   S-,  ,         ACE2.     , N-       ,         (NLS-, nuclear localization sequence),   ,               .

,   N-  NLS-      ,   ,  .           .      ,                :       .    , ,   , N- -       ⠖ ,       .         ,      .

      S-.       頖         .  ,             ,    .                 .  :   - MERS   .  , ,               .




 

 ,       ,  ,               . ,        .   ,       ,          .  ,       ,        (       ).   ,              (   ,   )  ,      .  ,   , .   99,9%  ,  -   .    ,      , ,      ,   (  ). ,        ,      ,   .


,            ,         .           ,        (,        ),                  ,  ,  . ,   ,         ,   .      ,        .        ?   ?.

       SARS-CoV-2       ,     .  ,        ,     .            .                   .          .      ,      ,       .    SARS-CoV-2      . ,      ,   .




 3.   



    ,       . ,       .    ,        .        5,3    [10 -      ,   ,       堖  ,    .     ,      ,       .           - ,           .]  , ,  ,   [16 - M. J. Costello, R. M. May, and N. E. Stork, Can We Name Earths Species Before They Go Extinct? Science, vol. 339, no. 6118, pp. 413416, Jan. 2013.].   [17 - K. J. Locey and J. T. Lennon, Scaling laws predict global microbial diversity, Proc. Natl. Acad. Sci., vol. 113, no. 21, pp. 59705975, May 2016.],       8,7.   ,   99,9%  -   ,    .           , ,          ,    .         .   ,      ,    - ,        ,       .      . ,          ,            ,            .         ,     . ,        ,       ,       ,         .        ,        .

        . ,     ,   FPLV (  feline panleukopenia virus,   )     .    1940- ,  ,   FPLV,     ,    80%,   ,    .  30       ,     ,       [18 - Y. Ikeda, Feline Host Range of Canine parvovirus: Recent Emergence of New Antigenic Types in Cats, Emerg. Infect. Dis., vol. 8, no. 4, pp. 341346, Apr. 2002.].    MEV,    CPV-2.   ,  MEV  CPV-2    FPLV: ,     ,              [19 - . Leal et al., Regional adaptations and parallel mutations in Feline panleukopenia virus strains from China revealed by nearly-full length genome analysis, PLoS One, vol. 15, no. 1, p. e0227705, Jan. 2020.].

       .  ,      ,  .   ,      ,        .   ,    ,      蠖  , ,        .     .

  ,      .  ,             [20 - K. E. Jones et al., Global trends in emerging infectious diseases, Nature, vol. 451, no. 7181, pp. 990993, Feb. 2008.].      .  ,            .     ,   ,        ,     .      ,  ,    ,   ,     ,    .  100      . ,           .  335   ,     1940  2004, 60,3%     [11 - ,           ,       .].    ,  71,8%        [21 - K. E. Jones et al., Global trends in emerging infectious diseases, Nature, vol. 451, no. 7181, pp. 990993, Feb. 2008.].

          .            .             ࠖ   ,            - .                 .        ,             ,      .   ,   ,      .         Batwoman,  ࠖ  .

 2005     [22 - W. Li, Bats Are Natural Reservoirs of SARS-Like Coronaviruses, Science (80-.)., vol. 310, no. 5748, pp. 676679, Oct. 2005.]  Science,     ,    ,   .           ,   408     ,       .  , ,       ,        .        S-,  ,       -    .             90%,         40%.     ,      S- ,          .  ,     ,      ,      .  ,         .

        -    ,    (       , ,      ).     ,           .    (     )         .    :  ,             .      ,      S-,   ,    ,      ,      ,     .

   ,      ,  (        ),    ,   -      ,    .  ,             ,           .    ,      ,    2,7%     [23 - N. Wang et al., Serological Evidence of Bat SARS-Related Coronavirus Infection in Humans, China, Virol. Sin., vol. 33, no. 1, pp. 104107, Feb. 2018.].   , ,          .    SARS-CoV-2.

    ?           ?   . :   .    20%     .       堖 -  .     .    ,   :    ,       , , ,            ,    30  .         ,      .    (, , )   . ,        ,   ,    ,      .




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   ,     (https://www.litres.ru/pages/biblio_book/?art=63420236)  .

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notes









1


       .




2


              .   :   ,   ,            .      ,      / .              .




3


  ,  SASR-CoV-2  ,  ,  ,     .      -   .




4


   ,     .




5


      :  ACE2   ,   ,       ?    :    .    ,            ,         .   SARS  c  ,       ACE2 (E. Braun and D. Sauter, Furin-mediated protein processing in infectious diseases and cancer, Clin. Transl. Immunol., vol. 8, no. 8, Jan. 2019.),             .




6


:        , ,      .           (   )   .     .




7


    ,   .  -   ,     ,    -  .     ,     ,     ,  .     ,    ,  ,  ,     .         ( , ,     ),     ,    ,       ,  ,       .




8


      ,  -   : ,     .




9


, ,          100% .




10


     ,   ,       堖  ,    .     ,      ,       .           - ,           .




11


,           ,       .










1


S.Duffy, Why are RNA virus mutation rates so damn high? PloS Biol., vol. 16, no. 8, p. e3000003, Aug. 2018.




2


C. A. Suttle, Viruses in the sea, Nature, vol. 437, no. 7057, pp. 356361, Sep. 2005.




3


K. Wang et al., SARS-CoV-2 invades host cells via a novel route: CD147-spike protein, bioRxiv, p. 2020.03.14.988345, Jan. 2020.




4


X. Wang et al., SARS-CoV-2 infects T lymphocytes through its spike protein-mediated membrane fusion, Cell. Mol. Immunol., Apr. 2020.




5


H. Wang et al., SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway, Cell Res., vol. 18, no. 2, pp. 290301, Feb. 2008.




6


M. Hoffmann et al., SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor, Cell, vol. 181, no. 2, pp. 271280.e8, Apr. 2020.




7


J. Shang et al., Cell entry mechanisms of SARS-CoV-2, Proc. Natl. Acad. Sci., vol. 117, no. 21, pp. 1172711734, May 2020.




8


E. Braun and D. Sauter, Furin-mediated protein processing in infectious diseases and cancer, Clin. Transl. Immunol., vol. 8, no. 8, Jan. 2019.




9


K. Kuba, Y. Imai, and J. M. Penninger, Multiple Functions of Angiotensin-Converting Enzyme 2 and Its Relevance in Cardiovascular Diseases, Circ. J., vol. 77, no. 2, pp. 301308, 2013.




10


T. Ivanova et al., Optimization of Substrate-Analogue Furin Inhibitors, ChemMedChem, vol. 12, no. 23, pp. 19531968, Dec. 2017.




11


Y. M. Bar-On, A. Flamholz, R. Phillips, and R. Milo, SARS-CoV-2 (COVID-19) by the numbers, Elife, vol. 9, Apr. 2020.




12


K. B. Anand, S. Karade, S. Sen, and R. M. Gupta, SARS-CoV-2: Camazotzs Curse, Med. J. Armed Forces India, vol. 76, no. 2, pp. 136141, Apr. 2020.




13


D. E. Gordon et al., A SARS-CoV-2 protein interaction map reveals targets for drug repurposing, Nature, vol. 583, no. 7816, pp. 459468, Jul. 2020.




14


Y. Zhang et al., The ORF8 Protein of SARS-CoV-2 Mediates Immune Evasion through Potently Downregulating MHCI, bioRxiv, p. 2020.05.24.111823, Jan. 2020.




15


A. B. Gussow, N. Auslander, G. Faure, Y. I. Wolf, F. Zhang, and E. V. Koonin, Genomic determinants of pathogenicity in SARS-CoV-2 and other human coronaviruses, Proc. Natl. Acad. Sci., vol. 117, no. 26, pp. 1519315199, Jun. 2020.




16


M. J. Costello, R. M. May, and N. E. Stork, Can We Name Earths Species Before They Go Extinct? Science, vol. 339, no. 6118, pp. 413416, Jan. 2013.




17


K. J. Locey and J. T. Lennon, Scaling laws predict global microbial diversity, Proc. Natl. Acad. Sci., vol. 113, no. 21, pp. 59705975, May 2016.




18


Y. Ikeda, Feline Host Range of Canine parvovirus: Recent Emergence of New Antigenic Types in Cats, Emerg. Infect. Dis., vol. 8, no. 4, pp. 341346, Apr. 2002.




19


. Leal et al., Regional adaptations and parallel mutations in Feline panleukopenia virus strains from China revealed by nearly-full length genome analysis, PLoS One, vol. 15, no. 1, p. e0227705, Jan. 2020.




20


K. E. Jones et al., Global trends in emerging infectious diseases, Nature, vol. 451, no. 7181, pp. 990993, Feb. 2008.




21


K. E. Jones et al., Global trends in emerging infectious diseases, Nature, vol. 451, no. 7181, pp. 990993, Feb. 2008.




22


W. Li, Bats Are Natural Reservoirs of SARS-Like Coronaviruses, Science (80-.)., vol. 310, no. 5748, pp. 676679, Oct. 2005.




23


N. Wang et al., Serological Evidence of Bat SARS-Related Coronavirus Infection in Humans, China, Virol. Sin., vol. 33, no. 1, pp. 104107, Feb. 2018.


