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Home > Coronavirus

LSBio offers many products related to coronaviruses, including antibodies, proteins, detection kits and expression-ready ORF clones.



Coronavirus And COVID-19 Inhibitors


Cytokine Release Syndrome


Coronaviruses (CoVs) are enveloped viruses with positive-sense, single-stranded RNA genomes that range in size from 26 to 32 kilobases, the largest among RNA viruses. They are pathogens known to infect humans and numerous other animal species. Based on genetic and antigenic criteria, CoVs have been organized into four groups: alpha, beta, gamma, and delta coronaviruses (Dhama, 2014; Coleman, 2014).

Common human coronaviruses include the 229E and NL63 alpha coronaviruses and the OC43 and HKU-1 beta coronaviruses. In infected humans, they are associated with a range of cold-like symptoms as well as severe respiratory tract infections (Fielding, 2011). Other more symptomatically severe human coronaviruses that have been transmitted from animals include MERS-CoV, a beta coronavirus that causes Middle East Respiratory Syndrome (MERS); SARS-CoV, a beta coronavirus that causes severe acute respiratory syndrome (SARS); and SARS-CoV-2, a beta coronavirus that causes coronavirus disease 2019 (COVID-19).

Proteins that contribute to the overall structure and function of all coronaviruses are the spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins, as well as the non-structural proteins cleaved from the orf1a/b polyprotein. Important non-structural proteins include the RNA-dependent RNA polymerase, protease, and endoRNAse (Fehr, 2016).

The spike (S) protein is responsible for attachment to and fusion with the host cell. For both SARS-CoV and SARS-CoV-2, the host receptor is known to be angiotensin converting enzyme 2 (ACE2) (Hoffman, 2020). The nucleocapsid (N) protein binds to the CoV genome and is responsible for packaging it into the ribonucleoprotein complex (capsid). The membrane (M) protein determines the shape of the viral envelope and organizes viral assembly through interaction with each additional structural protein. The envelope (E) protein is the smallest of the structural proteins and is incorporated into the virion envelope, but this represents only a small amount of total expressed envelope protein. A high proportion is also expressed inside the infected cell, where it is involved in viral assembly, budding, maturation and propagation (Schoeman, 2019; Chang, 2020).

The SARS-CoV-2 (COVID-19) coronavirus genome has 89% sequence similarity with the bat SARS-like CoVZXC21 coronavirus, and 82% similarity with human SARS-CoV coronavirus. The orf1a/b, S, E, M, and N proteins also share a high degree of phylogenetic similarity with bat, civet, and human SARS coronaviruses. Notable differences in sequence are found in the SARS-CoV-2 spike protein’s receptor binding domain, which has only 40% amino acid overlap with other related viruses. Furthermore, the SARS-CoV-2 orf3b protein represents a completely novel short protein (Rehman, 2020; Chan, 2020).

Coronavirus Genome

Coronavirus Phylogenetic Tree

Coronavirus Family Homology Heatmap

FELINE (ASU62488.1) 100.00 49.53 42.42 28.64 28.48 28.66 26.54 29.11 29.2
CANINE (AKA65829.1) 49.53 100.00 41.95 25.5 25.76 25.76 25.72 25.2 25.11
PORCINE (AIA61001.1) 42.42 41.95 100.00 26.37 26.46 26.35 26.85 27.17 27.48
SARS-CoV (NP_828851.1) 28.64 25.5 26.37 100.00 77.77 78.23 32.16 32.73 32.56
SARS-CoV-2 (YP_009724390.1) 28.48 25.76 26.46 77.77 100.00 97.71 31.79 32.13 32.13
BAT (QHR63300.2) 28.66 25.76 26.35 78.23 97.71 100.00 31.79 32.08 32.25
MERS (YP_009047204.1) 26.54 25.72 26.85 32.16 31.79 31.79 100.00 34.21 34.54
BOVINE (NP_150077.1) 29.11 25.20 27.17 32.73 32.13 32.08 34.21 100.00 94.28
CAMEL (AHN64774.1) 29.20 25.11 27.48 32.56 32.13 32.25 34.54 94.28 100.00


  • Chan, J. F., Kok, K. H., Zhu, Z., Chu, H., To, K. K., Yuan, S., & Yuen, K. Y. (2020). Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerging Microbes & Infections, 9(1), 221–236.
  • Chang, C. K., Hou, M. H., Chang, C. F., Hsiao, C. D., & Huang, T. H. (2014). The SARS coronavirus nucleocapsid protein--forms and functions. Antiviral Research, 103, 39–50.
  • Coleman, C. M., & Frieman, M. B. (2014). Coronaviruses: important emerging human pathogens. Journal of Virology, 88(10), 5209–5212.
  • Dhama, K., Pawaiya, R.V.S., Chakraborty, R., Tiwari, S. M., & Verma, A.K., (2014). Coronavirus Infection in Equines: A Review. Asian Journal of Animal and Veterinary Advances, 9, 164-176.
  • Fehr, A. R., & Perlman, S. (2015). Coronaviruses: an overview of their replication and pathogenesis. Methods in Molecular Biology (Clifton, N.J.), 1282, 1–23.
  • Fielding B. C. (2011). Human coronavirus NL63: a clinically important virus?. Future Microbiology, 6(2), 153–159.
  • Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N. H., Nitsche, A., Müller, M. A., Drosten, C., & Pöhlmann, S. (2020). SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell, 181(2), 271–280.e8.
  • Rehman, S. U., Shafique, L., Ihsan, A., & Liu, Q. (2020). Evolutionary Trajectory for the Emergence of Novel Coronavirus SARS-CoV-2. Pathogens (Basel, Switzerland), 9(3).
  • Schoeman, D., & Fielding, B. C. (2019). Coronavirus envelope protein: current knowledge. Virology Journal, 16(1), 69.