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*Contributed equally to this work Published: May 19, 2020 DOI: 10.21769/BioProtoc.5007 Views: 2756
Abstract
The Severe Acute Respiratory Syndrome Coronavirus 2 or SARS-COV-2 has been the cause of a global pandemic in 2020. With the numbers infected rising well above a 1.9 million and confirmed deaths above 122,000 as of 15th April 2020, it has become the paramount health concern for the global community at present. The SARS-COV-2 genome has since been sequenced and its predicted proteome identified. In this study, we looked at the expected SARS-COV-2 proteins and compare them to its close relative, the Severe Acute Respiratory Syndrome-Related Coronavirus. In particular we focussed on the M protein which is known to play a significant role in the virion structure of Coronaviruses. The rationale here was that since the major risk factor associated with SARS-COV-2 was its ease of spread, we wished to focus on the viral structure and architecture to look for clues that may indicate structural stability, thus prolonging the time span for which it can survive free of a host. As a result of the study, we found some rather interesting differences between the M protein for SARS-COV-2 and the SARS-CoV virus M protein. This included amino acid changes from non-polar to polar residues in regions important for anchoring the protein in the envelope membrane.
Keywords: ProteomicsBackground
The SARS-COV-2 Novel Corona virus or Severe Acute Respiratory Syndrome Coronavirus 2 has been the cause of a worldwide pandemic in 2020. The novel strain, originating from Wuhan, China has as of 25th April World Health Organization report, infected over 2.7 million people and led to the deaths of over 187,000 individuals worldwide (Coronavirus disease (COVID-2019) situation report-96, 2020). It has led to considerable disruptions in the economic and psychological welfare of populations, on top of the continuously increasing loss of life (Chen et al., 2020). Efforts at identifying possible solutions to combating the virus have thus far ranged from basic precautionary awareness campaigns to the suggestions of nucleotide based drugs currently being tested for other diseases as possible therapeutic agents (Martinez, 2020). The genome of the SARS-COV-2 novel coronavirus has been decoded and its expected proteome already established (RefSeq ID: NC_045512.2). However up until this point, to the best of our knowledge not much progress has been made in terms of identifying unique molecular features that are exclusive to this strain of the Coronavirus. Hence, in this study we made an attempt at studying the protein sequences of a relevant SARS-COV-2 architectural protein in order to identify unique advantageous features. We chose to focus our efforts on the M Protein as it is the most abundant protein in the viral nucleocapsid and is believed to be responsible for maintaining the virion in its characteristic shape (Nal, 2005). This coincides with our investigative rationale; is there any particular feature that aids the spread of this strain. The percentage of infected patients who have died from this virus has been estimated to be approximately 6.9% percent as of this writing (WHO, 2020b). Furthermore the primary susceptible groups are the immunocompromised. This leads us to believe that the primary focus needs to be on the mechanism of spreading, as the rapid rates at which this strain has infected communities across the world has arguably been its most dangerous aspect. The coronaviruses are known to contain four main structural proteins, the S, M, E, and N proteins (Fehr and Perlman, 2015). All of whom have been identified in the predicted proteome of SARS-COV-2. The S protein is the spike protein, responsible for gaining entry into the ER following infection (Delmas and Hurst, 2009; Beniac et al., 2006). The N protein resides inside the nucleocapsid and is an RNA binding protein (Chang et al., 2005; Hurst et al., 2009). The M and E proteins are both transmembrane proteins. The M protein, a 3 pass transmembrane protein is particularly significant as it is believed to be responsible for maintaining and giving the virion its shape (Armstrong et al., 1984).
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