TERKAIT DENGAN MASA MASA PANDEMI COVID-19 DILAKUKANNYA KESIMBANGAN DENGAN PENCEGAHAN DAN MENINGKATKAN KESELAMATAN PASIEN RAWAT INAP

2020 ◽  
Author(s):  
Agnes Jessica Lubis

Coronavirus adalah virus RNA dengan ukuran partikel 120-160 nm. Virus ini utamanya menginfeksi hewan, di antaranya adalah kelelawar dan unta. Sebelum terjadinya wabah COVID-19, ada 6 jenis coronavirus yang dapat menginfeksi manusia, yaitu alphacoronavirus 229E, alphacoronavirus NL63, betacoronavirus OC43, betacoronavirus HKU1, Severe Acute Respiratory Illness Coronavirus (SARS-CoV), dan Middle East Respiratory Syndrome Coronavirus (MERS-CoV).Coronavirus yang menjadi etiologi COVID-19 termasuk dalam genus betacoronavirus. Hasil analisis filogenetik menunjukkan bahwa virus ini masuk dalam subgenus yang sama dengan coronavirus yang menyebabkan wabah Severe Acute Respiratory Illness (SARS) pada 2002-2004 silam, yaitu Sarbecovirus. Atas dasar ini, International Committee on Taxonomy of Viruses mengajukan nama SARS-CoV-2.

2019 ◽  
Vol 12 (6) ◽  
pp. 900-903
Author(s):  
Sumit D. Bhardwaj ◽  
Varsha A. Potdar ◽  
Pragya D. Yadav ◽  
Manohar L. Chaudhary ◽  
Mandeep S. Chadha ◽  
...  

2019 ◽  
Vol 75 (1) ◽  
pp. 8-15 ◽  
Author(s):  
Thi Hong Van Nguyen ◽  
Julie Lichière ◽  
Bruno Canard ◽  
Nicolas Papageorgiou ◽  
Sarah Attoumani ◽  
...  

Middle East respiratory syndrome coronavirus (MERS-CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C-terminal domain of N from MERS-CoV obtained using single-crystal X-ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small-angle X-ray scattering measurements. Comparisons with the structures of the C-terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.


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