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SARS-CoV 2 in Cellular Level: Do we dominate the whole picture and how can we intervene?

Yıl 2021, , 248 - 253, 25.03.2021
https://doi.org/10.16899/jcm.839810

Öz

Coronaviruses are a family of viruses present in various animals, and alpha and beta types can infect humans. Human coronavirus varieties settle in different regions of the respiratory tract epithelium, causing disease with varying severity. We conducted a comprehensive academic search to aggregate data and added our own ideas to create a good research article. As a result of many studies carried out in a short time, detailed information was obtained about the entry of the virus into the cell and its cellular cycle.
Although vaccination studies are about to come to an end, we do not yet have an agent that provides a definitive treatment that will facilitate millions of people's lives. At this point, humanity needs detailed genetic research, especially on cellular interactions.
Because although we think that we are in control of the subject, science is a field that changes daily, and new data are added to it. It is evident that we need marginal ideas for a virus that has affected the whole world, can easily be transmitted by respiratory and droplets, and has destroyed everyday life. This research aims to examine the data we have so far in detail on all of the topics we have mentioned and try to make some suggestions within our knowledge.

Kaynakça

  • Referans1. Paules CI, Marston HD, Fauci AS. Coronavirus infections-more than just the common cold. JAMA. 2020 Feb;323(8):707–8.
  • Referans2. Walsh EE, Shin JH, Falsey AR. Clinical impact of human coronaviruses 229E and OC43 infection in diverse adult populations. J Infect Dis. 2013 Nov;208(10):1634–42.
  • Referans3. Zhou P, Yang XL, Wang XG, Hu B, Zhang L, Zhang W, et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020 Mar;579(7798):270–3.
  • Referans4. Mousavizadeh L, Ghasemi S. Genotype and phenotype of COVID-19: their roles in pathogenesis. J Microbiol Immunol Infect. 2020 Mar; S1684-1182(20)30082-7. https://doi.org/10.1016/j.jmii.2020.03.022.
  • Referans5. Gorbalenya AE, Baker SC, Baric R.S.; Coronaviridae Study Group of the International Committee on Taxonomy of Viruses. The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2. Nat Microbiol. 2020 Apr;5(4):536–44.
  • Referans6. Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020 Apr;181(2):271–280.e8.
  • Referans7. Matsuyama S, Nagata N, Shirato K, Kawase M, Takeda M, Taguchi F. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J Virol. 2010 Dec;84(24):12658–64.
  • Referans8. Shang J, Wan Y, Luo C, Ye G, Geng Q, Auerbach A, et al. Cell entry mechanisms of SARS-CoV-2. Proc Natl Acad Sci USA. 2020 May;117(21):11727–34.
  • Referans9. Ou X, Liu Y, Lei X, Li P, Mi D, Ren L, et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV. Nat Commun. 2020 Mar;11(1):1620.
  • Referans10. Millet, J. K. & Whittaker, G. R. Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells. Virology 517, 3–8 (2018). Return to ref 17 in the article.
  • Referans11. de Haan CA, Haijema BJ, Schellen P, Wichgers Schreur P, te Lintelo E, Vennema H, et al. Cleavage of group 1 coronavirus spike proteins: how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation. J Virol. 2008 Jun;82(12):6078–83.
  • Referans12. Cagno V, Tseligka ED, Jones ST, Tapparel C. Heparan sulfate proteoglycans, and viral attachment: proper receptors or adaptation Bias? Viruses. 2020;11(7):596.
  • Referans13. Milewska A, Zarebski M, Nowak P, Stozek K, Potempa J, Pyrc K. Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells. J Virol. 2014 Nov;88(22):13221–30.
  • Referans14. Peng Q, Peng R, Yuan B, Zhao J, Wang M, Wang X, et al. Structural and biochemical Characterization of nsp12-nsp7-nsp8 core polymerase complex from COVID-19 virus. Cell Rep. 2020 Jun;31(11):107774.
  • Referans15. Wei C, Wan L, Yan Q, Wang X, Zhang J, Yang X, et al. HDL-scavenger receptor B type 1 facilitates SARS-CoV-2 entry. Nat Metab. 2020 Nov; https://doi.org/10.1038/s42255-020-00324-0.
  • Referans16. Letko M, Marzi A, Munster V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B beta coronaviruses. Nat Microbiol. 2020 Apr;5(4):562–9.
  • Referans17. Tai W, He L, Zhang X, Pu J, Voronin D, Jiang S, et al. Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for the development of RBD protein as a viral attachment inhibitor and vaccine. Cell Mol Immunol. 2020 Jun;17(6):613–20.
  • Referans18. Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. 2020 Apr;181(2):281–292.e6.
  • Referans19. Wang K, Chen W, Zhou YS, Lian JQ, Zhang Z, Du P, et al. SARS-CoV-2 invades host cells via a novel route: CD147-spike protein. Microbiology. 2020.
  • Referans20. Baranov PV, Henderson CM, Anderson CB, Gesteland RF, Atkins JF, Howard MT. Programmed ribosomal frameshifting in decoding the SARS-CoV genome. Virology. 2005 Feb;332(2):498–510.
  • Referans21. Guo YR, Cao QD, Hong ZS, Tan YY, Chen SD, Jin HJ, et al. The origin, transmission and clinical therapies on coronavirus disease 2019 (COVID-19) outbreak - an update on the status. Mil Med Res. 2020 Mar;7(1):11.
  • Referans22. Fehr AR, Perlman S. Coronaviruses: an overview of their replication and pathogenesis. Methods Mol Biol. 2015;1282:1–23.
  • Referans23. Heurich A, Hofmann-Winkler H, Gierer S, Liepold T, Jahn O, Pöhlmann S. TMPRSS2, and ADAM17 cleave ACE2 differentially, and the only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein. J Virol. 2014 Jan;88(2):1293–307.
  • Referans24. Chen J, Jiang Q, Xia X, Liu K, Yu Z, Tao W, et al. Individual variation of the SARS-CoV-2 receptor ACE2 gene expression and regulation. Aging Cell. 2020 Jul;19(7):192020030191.
  • Referans25. Milken Institute. COVID-19 treatment and vaccine tracker. Glossary. https://covid-19tracker.milkeninstitute.org/glossary
  • Referans26. Milken Institute. COVID-19 vaccine tracker. Last updated: November 30, 2020, 2:33 PM PST. https://www.covid-19vaccinetracker.org/
  • Referans27. World Health Organization. Guidance framework for testing of genetically modified mosquitoes. 2014a. Available at http://apps.who.int/iris/bitstream/10665/127889/1/9789241507486_eng.pdf?ua=1 Accessed December 16, 2019. Google Scholar.

Hücresel Düzeyde SARS-CoV 2: Resmin tamamına hakim miyiz ve nasıl müdahale edebiliriz?

Yıl 2021, , 248 - 253, 25.03.2021
https://doi.org/10.16899/jcm.839810

Öz

Koronavirüsler, çeşitli hayvanlarda bulunan bir virüs ailesidir ve alfa ve beta türleri insanları enfekte edebilir. İnsan koronavirüs çeşitleri, solunum yolu epitelinin farklı bölgelerine yerleşerek değişen şiddette hastalığa neden olur. Verileri toplamak için kapsamlı bir akademik araştırma yaptık ve iyi bir araştırma makalesi oluşturmak için kendi fikirlerimizi ekledik. Kısa sürede yapılan birçok çalışma sonucunda virüsün hücreye girişi ve hücresel döngüsü hakkında detaylı bilgiler elde edildi. Aşılama çalışmaları bitmek üzere olsa da henüz milyonlarca insanın hayatını kolaylaştıracak kesin tedavi sağlayacak bir ajana sahip değiliz. Bu noktada insanlığın özellikle hücresel etkileşimler konusunda detaylı genetik araştırmalara ihtiyacı var. Çünkü konunun kontrolünde olduğumuzu düşünsek de bilim her geçen gün değişen bir alan ve ona yeni veriler ekleniyor. Tüm dünyayı etkilemiş, solunum ve damlacıklarla kolaylıkla bulaşabilen ve günlük yaşamı mahvetmiş bir virüs için marjinal fikirlere ihtiyacımız olduğu aşikardır. Bu araştırma, bahsettiğimiz tüm konularda bugüne kadar sahip olduğumuz verileri detaylı bir şekilde incelemeyi ve bilgimiz dahilinde bazı önerilerde bulunmayı amaçlamaktadır.

Kaynakça

  • Referans1. Paules CI, Marston HD, Fauci AS. Coronavirus infections-more than just the common cold. JAMA. 2020 Feb;323(8):707–8.
  • Referans2. Walsh EE, Shin JH, Falsey AR. Clinical impact of human coronaviruses 229E and OC43 infection in diverse adult populations. J Infect Dis. 2013 Nov;208(10):1634–42.
  • Referans3. Zhou P, Yang XL, Wang XG, Hu B, Zhang L, Zhang W, et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020 Mar;579(7798):270–3.
  • Referans4. Mousavizadeh L, Ghasemi S. Genotype and phenotype of COVID-19: their roles in pathogenesis. J Microbiol Immunol Infect. 2020 Mar; S1684-1182(20)30082-7. https://doi.org/10.1016/j.jmii.2020.03.022.
  • Referans5. Gorbalenya AE, Baker SC, Baric R.S.; Coronaviridae Study Group of the International Committee on Taxonomy of Viruses. The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2. Nat Microbiol. 2020 Apr;5(4):536–44.
  • Referans6. Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020 Apr;181(2):271–280.e8.
  • Referans7. Matsuyama S, Nagata N, Shirato K, Kawase M, Takeda M, Taguchi F. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J Virol. 2010 Dec;84(24):12658–64.
  • Referans8. Shang J, Wan Y, Luo C, Ye G, Geng Q, Auerbach A, et al. Cell entry mechanisms of SARS-CoV-2. Proc Natl Acad Sci USA. 2020 May;117(21):11727–34.
  • Referans9. Ou X, Liu Y, Lei X, Li P, Mi D, Ren L, et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV. Nat Commun. 2020 Mar;11(1):1620.
  • Referans10. Millet, J. K. & Whittaker, G. R. Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells. Virology 517, 3–8 (2018). Return to ref 17 in the article.
  • Referans11. de Haan CA, Haijema BJ, Schellen P, Wichgers Schreur P, te Lintelo E, Vennema H, et al. Cleavage of group 1 coronavirus spike proteins: how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation. J Virol. 2008 Jun;82(12):6078–83.
  • Referans12. Cagno V, Tseligka ED, Jones ST, Tapparel C. Heparan sulfate proteoglycans, and viral attachment: proper receptors or adaptation Bias? Viruses. 2020;11(7):596.
  • Referans13. Milewska A, Zarebski M, Nowak P, Stozek K, Potempa J, Pyrc K. Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells. J Virol. 2014 Nov;88(22):13221–30.
  • Referans14. Peng Q, Peng R, Yuan B, Zhao J, Wang M, Wang X, et al. Structural and biochemical Characterization of nsp12-nsp7-nsp8 core polymerase complex from COVID-19 virus. Cell Rep. 2020 Jun;31(11):107774.
  • Referans15. Wei C, Wan L, Yan Q, Wang X, Zhang J, Yang X, et al. HDL-scavenger receptor B type 1 facilitates SARS-CoV-2 entry. Nat Metab. 2020 Nov; https://doi.org/10.1038/s42255-020-00324-0.
  • Referans16. Letko M, Marzi A, Munster V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B beta coronaviruses. Nat Microbiol. 2020 Apr;5(4):562–9.
  • Referans17. Tai W, He L, Zhang X, Pu J, Voronin D, Jiang S, et al. Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for the development of RBD protein as a viral attachment inhibitor and vaccine. Cell Mol Immunol. 2020 Jun;17(6):613–20.
  • Referans18. Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. 2020 Apr;181(2):281–292.e6.
  • Referans19. Wang K, Chen W, Zhou YS, Lian JQ, Zhang Z, Du P, et al. SARS-CoV-2 invades host cells via a novel route: CD147-spike protein. Microbiology. 2020.
  • Referans20. Baranov PV, Henderson CM, Anderson CB, Gesteland RF, Atkins JF, Howard MT. Programmed ribosomal frameshifting in decoding the SARS-CoV genome. Virology. 2005 Feb;332(2):498–510.
  • Referans21. Guo YR, Cao QD, Hong ZS, Tan YY, Chen SD, Jin HJ, et al. The origin, transmission and clinical therapies on coronavirus disease 2019 (COVID-19) outbreak - an update on the status. Mil Med Res. 2020 Mar;7(1):11.
  • Referans22. Fehr AR, Perlman S. Coronaviruses: an overview of their replication and pathogenesis. Methods Mol Biol. 2015;1282:1–23.
  • Referans23. Heurich A, Hofmann-Winkler H, Gierer S, Liepold T, Jahn O, Pöhlmann S. TMPRSS2, and ADAM17 cleave ACE2 differentially, and the only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein. J Virol. 2014 Jan;88(2):1293–307.
  • Referans24. Chen J, Jiang Q, Xia X, Liu K, Yu Z, Tao W, et al. Individual variation of the SARS-CoV-2 receptor ACE2 gene expression and regulation. Aging Cell. 2020 Jul;19(7):192020030191.
  • Referans25. Milken Institute. COVID-19 treatment and vaccine tracker. Glossary. https://covid-19tracker.milkeninstitute.org/glossary
  • Referans26. Milken Institute. COVID-19 vaccine tracker. Last updated: November 30, 2020, 2:33 PM PST. https://www.covid-19vaccinetracker.org/
  • Referans27. World Health Organization. Guidance framework for testing of genetically modified mosquitoes. 2014a. Available at http://apps.who.int/iris/bitstream/10665/127889/1/9789241507486_eng.pdf?ua=1 Accessed December 16, 2019. Google Scholar.
Toplam 27 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Sağlık Kurumları Yönetimi
Bölüm Derleme
Yazarlar

Muhammed Emin 0000-0002-1837-6415

Aydın Balcı 0000-0002-6723-2418

Elif Menekşe 0000-0001-7300-5636

Yayımlanma Tarihi 25 Mart 2021
Kabul Tarihi 10 Şubat 2021
Yayımlandığı Sayı Yıl 2021

Kaynak Göster

AMA Emin M, Balcı A, Menekşe E. SARS-CoV 2 in Cellular Level: Do we dominate the whole picture and how can we intervene?. J Contemp Med. Mart 2021;11(2):248-253. doi:10.16899/jcm.839810