{"paper_id":"bd79d7c8-304d-4008-be85-95328d4b5160","body_text":"Sequence and Structural Analysis of COVID-19 E and M Protein With MERS Virus E and M Protein – A Comparative Study | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research article Sequence and Structural Analysis of COVID-19 E and M Protein With MERS Virus E and M Protein – A Comparative Study Ebtisam A. Aldaais, Subha Yegnaswamy, Fatimah Albahrani, Fatima Alsowaiket, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-108454/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract The outbreak of SARS in 2003, MERS in 2012, and now COVID-19 in 2019 have demonstrated that Coronaviruses are capable of causing primary lethal infections in humans, and the pandemic is now a global concern. The COVID-19 belongs to the beta coronavirus family encoding 29 proteins, of which 4 are structural, the Spike, Membrane, Envelope, and Nucleocapsid proteins. Here we have analyzed and compared the Membrane (M) and Envelope (E) proteins of COVID-19 and MERS with SARS and Bat viruses. The sequence analysis of conserved regions of both E and M protein revealed that many regions of COVID-19 are similar to Bat and SARS viruses while the MERS virus showed variations. The essential binding motifs found in SARS-CoV appeared in COVID-19. Besides, the M protein of COVID- 19 showed a distinct serine phosphorylation site in the C-terminal domain, which looked like a catalytic triad seen in serine proteases. A Dileucine motif occurred many times in the sequence of the M protein of all the four viruses compared. Concerning the structural part, the COVID-19 E protein showed more similarity to Bat while MERS shared similarity with the SARS virus. The M protein of both COVID-19 and MERS displayed variations in the structure. The interaction between M and E protein was also studied to know the additional binding regions. Our study highlights the critical motifs and structural regions to be considered for further research to design better inhibitors for the infection caused by these viruses. Molecular Biology General Cell Biology & Physiology COVID-19 Beta coronaviruses E protein M protein sequence and structural analysis Figures Figure 1 Figure 2 Figure 3 Figure 4 Figure 5 Figure 6 Figure 7 Figure 8 Figure 9 Full Text Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {\"props\":{\"pageProps\":{\"initialData\":{\"identity\":\"rs-108454\",\"acceptedTermsAndConditions\":true,\"allowDirectSubmit\":true,\"archivedVersions\":[],\"articleType\":\"Research article\",\"associatedPublications\":[],\"authors\":[{\"id\":4775132,\"identity\":\"1addcd9e-55b2-4c0f-a664-6878a958c338\",\"order_by\":0,\"name\":\"Ebtisam A. Aldaais\",\"email\":\"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA10lEQVRIiWNgGAWjYFAC5gYJBgYJBn4QO6GAKC2MEC2SDSAtBsRrYWAwOAAmidDAz36w8caPGgt74/OrEz88MGCQ5xc7gF+LZE9is2XPMYnEbTfebpYAOsxw5uwE/FoMDiS2SfCwSSSY3Ti7AaQlweA2AS325x+2Sf75J2FvPOPs5h9EaTGQSGyT5m2TYNzA37uNOFskbjxstpbtk0iccYN3m0WCgQRhv/D3Jx+8+eZbnT1//9nNN39U2MjzSxPQgmQfWKUEscrB9h0gRfUoGAWjYBSMJAAAO2VESstJJo8AAAAASUVORK5CYII=\",\"orcid\":\"https://orcid.org/0000-0003-3627-7805\",\"institution\":\"Imam Abdulrahman Bin Faisal University\",\"correspondingAuthor\":true,\"submittingAuthor\":false,\"prefix\":\"\",\"firstName\":\"Ebtisam\",\"middleName\":\"A.\",\"lastName\":\"Aldaais\",\"suffix\":\"\"},{\"id\":4775133,\"identity\":\"ef1f482c-59f5-4d94-a2d8-e9732d45b6a5\",\"order_by\":1,\"name\":\"Subha Yegnaswamy\",\"email\":\"\",\"orcid\":\"\",\"institution\":\"Aldaais Research Group\",\"correspondingAuthor\":false,\"submittingAuthor\":false,\"prefix\":\"\",\"firstName\":\"Subha\",\"middleName\":\"\",\"lastName\":\"Yegnaswamy\",\"suffix\":\"\"},{\"id\":4775134,\"identity\":\"a51b0480-f3b8-4167-a759-c4b16108aab6\",\"order_by\":2,\"name\":\"Fatimah Albahrani\",\"email\":\"\",\"orcid\":\"\",\"institution\":\"Imam Abdulrahman Bin Faisal University College of Engineering\",\"correspondingAuthor\":false,\"submittingAuthor\":false,\"prefix\":\"\",\"firstName\":\"Fatimah\",\"middleName\":\"\",\"lastName\":\"Albahrani\",\"suffix\":\"\"},{\"id\":4775135,\"identity\":\"401e9410-f975-4cc2-90bb-869c7b8c535b\",\"order_by\":3,\"name\":\"Fatima Alsowaiket\",\"email\":\"\",\"orcid\":\"\",\"institution\":\"Imam Abdulrahman Bin Faisal University College of Engineering\",\"correspondingAuthor\":false,\"submittingAuthor\":false,\"prefix\":\"\",\"firstName\":\"Fatima\",\"middleName\":\"\",\"lastName\":\"Alsowaiket\",\"suffix\":\"\"},{\"id\":4775136,\"identity\":\"59062c18-549a-46d1-966a-895001122597\",\"order_by\":4,\"name\":\"Sarah Alramadan\",\"email\":\"\",\"orcid\":\"\",\"institution\":\"Imam Abdulrahman Bin Faisal University College of Engineering\",\"correspondingAuthor\":false,\"submittingAuthor\":false,\"prefix\":\"\",\"firstName\":\"Sarah\",\"middleName\":\"\",\"lastName\":\"Alramadan\",\"suffix\":\"\"}],\"badges\":[],\"createdAt\":\"2020-11-14 14:43:05\",\"currentVersionCode\":1,\"declarations\":\"\",\"doi\":\"10.21203/rs.3.rs-108454/v1\",\"doiUrl\":\"https://doi.org/10.21203/rs.3.rs-108454/v1\",\"draftVersion\":[],\"editorialEvents\":[],\"editorialNote\":\"\",\"failedWorkflow\":false,\"files\":[{\"id\":3776287,\"identity\":\"23249b53-636d-4975-9d78-123ecef4963e\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:17\",\"extension\":\"jpg\",\"order_by\":1,\"title\":\"Figure 1\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":63267,\"visible\":true,\"origin\":\"\",\"legend\":\"3D model visualizing coronavirus and its structural proteins.\",\"description\":\"\",\"filename\":\"Figure1.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/04efa252ebdae80f91ff3d1b.JPG\"},{\"id\":3776288,\"identity\":\"b5269c72-b029-4860-bbce-d92e90c543e4\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:17\",\"extension\":\"jpg\",\"order_by\":2,\"title\":\"Figure 2\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":123192,\"visible\":true,\"origin\":\"\",\"legend\":\"A representation of a Multiple Sequence Alignment (MSA) of COVID-19 E\\nprotein. The MSA is showing the alignment of COVID-19 E protein with Bat, SARS,\\nMERS Viruses. The alignment is colored based on the hydrophobicity. The blue-colored\\nare hydrophilic, and the red ones are hydrophobic residues.\",\"description\":\"\",\"filename\":\"Figure2.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/5a6a504650177428f8017d6c.JPG\"},{\"id\":3776289,\"identity\":\"e7bf80b9-cb1d-4f97-b590-477670e37552\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:17\",\"extension\":\"jpg\",\"order_by\":3,\"title\":\"Figure 3\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":40351,\"visible\":true,\"origin\":\"\",\"legend\":\"Modeled structure of the E protein for COVID-19 (a), Bat (b), SARS (c), and\\nMERS (d) viruses using Swiss-Model Server. The models were visualized using Discovery\\nstudio visualizer\",\"description\":\"\",\"filename\":\"Figure3.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/1569fa412593996a612ad685.JPG\"},{\"id\":3776290,\"identity\":\"7d0d3f68-1c61-44fc-8626-f037ec9e83c0\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:18\",\"extension\":\"jpg\",\"order_by\":4,\"title\":\"Figure 4\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":51936,\"visible\":true,\"origin\":\"\",\"legend\":\"A comparison between E protein regions for COVID-19 and MERS viruses. (a)\\nA structure of COVID-19 E protein showing interaction regions. The region that could be\\ninvolved in spike protein interaction is shown in cyan, while the one involved in forming\\na homopentameric channel is shown in magenta. The sequence also highlighted in the\\nsame manner. (b) A structure of the MERS virus showing interaction regions. The region\\nwhich is involved in forming a homopentameric channel is shown in magenta.\",\"description\":\"\",\"filename\":\"Figure4.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/005165a65c592f427d45422c.JPG\"},{\"id\":3776291,\"identity\":\"3f786ffa-60fd-4a03-a6a7-88fd42cab5cd\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:18\",\"extension\":\"jpg\",\"order_by\":5,\"title\":\"Figure 5\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":120778,\"visible\":true,\"origin\":\"\",\"legend\":\"A Multiple Sequence Alignment of COVID-19 M protein. The MSA is showing\\nthe alignment of COVID-19 M protein with Bat, SARS, MERS Virus. The alignment is\\ncolored based on the hydrophobicity. The blue-colored are hydrophilic, and the red ones\\nare hydrophobic residues.\",\"description\":\"\",\"filename\":\"Figure5.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/1080ffb08a7b0e4f95cb5898.JPG\"},{\"id\":3776292,\"identity\":\"6c942dac-ca65-4b2d-a0ed-2bf0ef7dd00e\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:18\",\"extension\":\"jpg\",\"order_by\":6,\"title\":\"Figure 6\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":69213,\"visible\":true,\"origin\":\"\",\"legend\":\"Modeled structure of the M protein for COVID-19 (a), Bat (b), SARS (c),\\nand MERS (d) viruses using I-Tasser Server. The models were visualized using Discovery\\nstudio visualizer.\",\"description\":\"\",\"filename\":\"Figure6.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/86a7582550174d240b18327d.JPG\"},{\"id\":3776293,\"identity\":\"4b19b477-c073-408f-ab5f-be3087e16bf5\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:18\",\"extension\":\"jpg\",\"order_by\":7,\"title\":\"Figure 7\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":74062,\"visible\":true,\"origin\":\"\",\"legend\":\"A comparison between M protein regions for COVID-19 and MERS viruses.\\n(a) A structure of COVID-19 M protein showing interaction regions. The region involved\\nin M-M interaction is shown in magenta, and the one which is a phosphorylation site is\\nshown in orange. (b) A structure of MERS M protein showing interaction regions. The\\nregion involved in M-M interaction is shown in magenta, and the carboxy-terminal motif\\ninvolved in many interactions is shown in orange.\",\"description\":\"\",\"filename\":\"Figure7.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/ae9f1b4c62861baef366067f.JPG\"},{\"id\":3776294,\"identity\":\"fbec17e6-42ca-4bbd-8db4-70b57ba24ef4\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:18\",\"extension\":\"jpg\",\"order_by\":8,\"title\":\"Figure 8\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":90884,\"visible\":true,\"origin\":\"\",\"legend\":\"The interaction between M and E protein of COVID-19. (a) The interacting\\nregions are represented in the ball and stick model with the M protein highlighted in yellow\\nand the E protein shown in purple. (b) A 2D-plot showing the interaction between M and\\nE chains of COVID-19 and the interacting residues. The H2 bonds are shown in dotted\\nlines.\",\"description\":\"\",\"filename\":\"Figure8.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/9a0f8e827b4d80d622501b30.JPG\"},{\"id\":3776295,\"identity\":\"c8ffef32-473f-4114-a953-0d73c8c9922a\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:35:18\",\"extension\":\"jpg\",\"order_by\":9,\"title\":\"Figure 9\",\"display\":\"\",\"copyAsset\":false,\"role\":\"figure\",\"size\":72834,\"visible\":true,\"origin\":\"\",\"legend\":\"The interaction between M and E protein of MERS virus. (a) The interacting\\nregions are represented in the ball and stick model. The E protein is shown in purple. The\\ninteracting residues are highlighted in yellow. (b) A 2D-plot of the interaction between\\nM and E chains of MERS virus. The interacting residues are shown. The H2 bonds are\\nshown in dotted lines.\",\"description\":\"\",\"filename\":\"Figure9.JPG\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1/77b7228f445825278902c32e.JPG\"},{\"id\":13557830,\"identity\":\"1bad1c7a-af71-4a4c-9de7-78c3ac701706\",\"added_by\":\"auto\",\"created_at\":\"2021-09-17 02:54:04\",\"extension\":\"pdf\",\"order_by\":1,\"title\":\"\",\"display\":\"\",\"copyAsset\":false,\"role\":\"manuscript-pdf\",\"size\":2768887,\"visible\":true,\"origin\":\"\",\"legend\":\"\",\"description\":\"\",\"filename\":\"COVID19EMp.pdf\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1_covered.pdf\"},{\"id\":3776360,\"identity\":\"3a87dd14-1c4e-4286-820b-7165083b39f5\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:37:49\",\"extension\":\"pdf\",\"order_by\":1,\"title\":\"\",\"display\":\"\",\"copyAsset\":false,\"role\":\"manuscript-pdf\",\"size\":2235588,\"visible\":true,\"origin\":\"\",\"legend\":\"\",\"description\":\"\",\"filename\":\"COVID19EMp.pdf\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1_stamped.pdf\"},{\"id\":3776359,\"identity\":\"bf2f2714-947e-4da1-be21-5b4d36682574\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:37:48\",\"extension\":\"pdf\",\"order_by\":1,\"title\":\"\",\"display\":\"\",\"copyAsset\":false,\"role\":\"manuscript-pdf\",\"size\":2235588,\"visible\":true,\"origin\":\"\",\"legend\":\"\",\"description\":\"\",\"filename\":\"COVID19EMp.pdf\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1_stamped.pdf\"},{\"id\":3776358,\"identity\":\"418b26c3-fd6f-4d5a-bc61-09d17500c62b\",\"added_by\":\"auto\",\"created_at\":\"2020-11-23 21:37:48\",\"extension\":\"pdf\",\"order_by\":1,\"title\":\"\",\"display\":\"\",\"copyAsset\":false,\"role\":\"manuscript-pdf\",\"size\":2235588,\"visible\":true,\"origin\":\"\",\"legend\":\"\",\"description\":\"\",\"filename\":\"COVID19EMp.pdf\",\"url\":\"https://assets-eu.researchsquare.com/files/rs-108454/v1_stamped.pdf\"}],\"financialInterests\":\"\",\"formattedTitle\":\"\\u003cp\\u003eSequence and Structural Analysis of COVID-19 E and M Protein With MERS Virus E and M Protein – A Comparative Study\\u003c/p\\u003e\",\"fulltext\":[{\"header\":\"Full Text\",\"content\":\"\\u003cp\\u003eThis preprint is available for \\u003ca href='/article/rs-108454/latest.pdf' target='_blank'\\u003edownload as a PDF\\u003c/a\\u003e.\\u003c/p\\u003e\"}],\"fulltextSource\":\"\",\"fullText\":\"\",\"funders\":[],\"hasAdminPriorityOnWorkflow\":false,\"hasManuscriptDocX\":false,\"hasOptedInToPreprint\":true,\"hasPassedJournalQc\":\"\",\"hasAnyPriority\":false,\"hideJournal\":true,\"highlight\":\"\",\"institution\":\"\",\"isAcceptedByJournal\":false,\"isAuthorSuppliedPdf\":true,\"isDeskRejected\":\"\",\"isHiddenFromSearch\":false,\"isInQc\":false,\"isInWorkflow\":false,\"isPdf\":false,\"isPdfUpToDate\":true,\"isWithdrawnOrRetracted\":false,\"journal\":{\"display\":true,\"email\":\"info@researchsquare.com\",\"identity\":\"researchsquare\",\"isNatureJournal\":false,\"hasQc\":true,\"allowDirectSubmit\":true,\"externalIdentity\":\"\",\"sideBox\":\"\",\"snPcode\":\"\",\"submissionUrl\":\"/submission\",\"title\":\"Research Square\",\"twitterHandle\":\"researchsquare\",\"acdcEnabled\":true,\"dfaEnabled\":false,\"editorialSystem\":\"\",\"reportingPortfolio\":\"\",\"inReviewEnabled\":false,\"inReviewRevisionsEnabled\":true},\"keywords\":\"COVID-19, Beta coronaviruses, E protein, M protein, sequence and structural analysis\",\"lastPublishedDoi\":\"10.21203/rs.3.rs-108454/v1\",\"lastPublishedDoiUrl\":\"https://doi.org/10.21203/rs.3.rs-108454/v1\",\"license\":{\"name\":\"CC BY 4.0\",\"url\":\"https://creativecommons.org/licenses/by/4.0/\"},\"manuscriptAbstract\":\"The outbreak of SARS in 2003, MERS in 2012, and now COVID-19 in 2019 have demonstrated that Coronaviruses are capable of causing primary lethal infections in humans, and the pandemic is now a global concern. The COVID-19 belongs to the beta coronavirus family encoding 29 proteins, of which 4 are structural, the Spike, Membrane, Envelope, and Nucleocapsid proteins. Here we have analyzed and compared the Membrane (M) and Envelope (E) proteins of COVID-19 and MERS with SARS and Bat viruses. The sequence analysis of conserved regions of both E and M protein revealed that many regions of COVID-19 are similar to Bat and SARS viruses while the MERS virus showed variations. The essential binding motifs found in SARS-CoV appeared in COVID-19. Besides, the M protein of COVID- 19 showed a distinct serine phosphorylation site in the C-terminal domain, which looked like a catalytic triad seen in serine proteases. A Dileucine motif occurred many times in the sequence of the M protein of all the four viruses compared. Concerning the structural part, the COVID-19 E protein showed more similarity to Bat while MERS shared similarity with the SARS virus. The M protein of both COVID-19 and MERS displayed variations in the structure. The interaction between M and E protein was also studied to know the additional binding regions. Our study highlights the critical motifs and structural regions to be considered for further research to design better inhibitors for the infection caused by these viruses.\",\"manuscriptTitle\":\"Sequence and Structural Analysis of COVID-19 E and M Protein With MERS Virus E and M Protein – A Comparative Study\",\"msid\":\"\",\"msnumber\":\"\",\"nonDraftVersions\":[{\"code\":1,\"date\":\"2020-11-23 21:35:15\",\"doi\":\"10.21203/rs.3.rs-108454/v1\",\"editorialEvents\":[{\"type\":\"communityComments\",\"content\":0}],\"status\":\"published\",\"journal\":{\"display\":true,\"email\":\"info@researchsquare.com\",\"identity\":\"researchsquare\",\"isNatureJournal\":false,\"hasQc\":true,\"allowDirectSubmit\":true,\"externalIdentity\":\"\",\"sideBox\":\"\",\"snPcode\":\"\",\"submissionUrl\":\"/submission\",\"title\":\"Research Square\",\"twitterHandle\":\"researchsquare\",\"acdcEnabled\":true,\"dfaEnabled\":false,\"editorialSystem\":\"\",\"reportingPortfolio\":\"\",\"inReviewEnabled\":false,\"inReviewRevisionsEnabled\":true}}],\"origin\":\"\",\"ownerIdentity\":\"28f5f570-e811-403c-ad95-231d2d08572d\",\"owner\":[],\"postedDate\":\"November 23rd, 2020\",\"published\":true,\"recentEditorialEvents\":[],\"rejectedJournal\":[],\"revision\":\"\",\"amendment\":\"\",\"status\":\"posted\",\"subjectAreas\":[{\"id\":1173702,\"name\":\"Molecular Biology\"},{\"id\":1173703,\"name\":\"General Cell Biology \\u0026 Physiology\"}],\"tags\":[],\"updatedAt\":\"2021-01-14T11:43:03+00:00\",\"versionOfRecord\":[],\"versionCreatedAt\":\"2020-11-23 21:35:15\",\"video\":\"\",\"vorDoi\":\"\",\"vorDoiUrl\":\"\",\"workflowStages\":[]},\"version\":\"v1\",\"identity\":\"rs-108454\",\"journalConfig\":\"researchsquare\"},\"__N_SSP\":true},\"page\":\"/article/[identity]/[[...version]]\",\"query\":{\"redirect\":\"/article/rs-108454\",\"identity\":\"rs-108454\",\"version\":[\"v1\"]},\"buildId\":\"rHA-KDH7Qsr4HCuvH75dn\",\"isFallback\":false,\"isExperimentalCompile\":false,\"dynamicIds\":[84888],\"gssp\":true,\"scriptLoader\":[]}","source_license":"CC-BY-4.0","license_restricted":false}