Severe acute respiratory syndrome (SARS), caused by SARS coronavirus (SARS-CoV), is a kind of respiratory viral diseases. It was first reported in 2003. Currently, there is no reported SARS transmission in the world. However, another kind of coronavirus, SARS-CoV-2 caused COVID-19 has become a pandemic since last December, 2019. COVID-19 showed many similarities to the previous SARS outbreak. Now worldwide scientists are dedicated to exploring mechanisms of SARS-CoV-2 and developing novel therapies to control this pandemic.

Illustration of a SARS-CoV virion Fig.1 Illustration of a SARS-CoV virion.

Transmission electron micrograph of SARS-CoV virions. Fig.2 Transmission electron micrograph of SARS-CoV virions.

Virus Classification of SARS-CoV

SARS-CoV is an enveloped, positive-sense single-stranded RNA virus, and it’s a strain of severe acute respiratory syndrome-related coronavirus (SARSr-CoV). Coronaviruses consist of four genus: α, β, γ, and δ. The coronaviruses that infect mammals are mainly α and β genus. Among the viruses capable of infecting humans, HCoV-229E and HCoV-NL63 belong to the α coronavirus, and HCoV-OC43, SARS-CoV, HCoV-HKU1, MERS-CoV, and SARS-CoV-2 belong to the β coronavirus. It has been demonstrated that SARS-CoV can infect epithelial cells within the lungs through binding to the ACE2 receptor.

Virus family Coronaviridae
Virus genus Betacoronavirus
Virus species Severe acute respiratory syndrome-related coronavirus
Virus strain Severe acute respiratory syndrome coronavirus

Table 1. SARS-CoV classification.

Structure of SARS-CoV

The RNA genome size of SARS-CoV is 27.8 kb, which code for at least 28 proteins (Fig.4). The spike (S) protein is responsible for angiotensin-converting enzyme 2 (ACE2) receptor binding and host cell entry. Nucleocapsid (N) protein is an important structural protein, and it encapsulates the genomic RNA, affecting the RNA replication and transcription. Membrane (M) protein and envelope (E) glycoprotein are also structural proteins which complete the SARS-CoV. In addition, SARS-CoV can encode non-structural proteins including papain-like protease(s) (PLpro), chymotrypsin-likeprotease (3CLpro), RNA-dependent RNA polymerase (RdRp) and helicase (Hel). As the most important protein, S consists of two subunits: S1 and S2. S1 subunit contains a receptor-binding domain (RBD) which plays a key role in ACE2 binding. S2 subunit is critical for membrane fusion when interacting with host cells. S protein mediates critical activities in immune responses during SARS infection.

Structure of the coronavirus virion. Fig.3 Structure of the coronavirus virion. (Holmes, 2003)

Structure of the RNA genome of SARS-CoV. Fig.4 Structure of the RNA genome of SARS-CoV. (Hilgenfeld, 2013)

SARS-CoV Antibodies

Creative Biolabs now provides a variety of SARS-CoV antibodies targeting various proteins (such as SARS-CoV spike protein, SARS-CoV nucleocapsid protein etc.) to meet our clients’ requirements. Please submit your specific SARS-CoV-2 antibody inquiry to us, and we will reply within several hours. For some targets, ready-to-use catalogue is not available. Please reach out to our scientists for antibody discovery services and customized services. For antibody related virology assays, please contact us for a specific assay service. We also provide a full comprehensive suite of secondary antibodies and isotype controls to meet your needs.

Target Proposed function ViroAntibodies
S Spike protein, binding to cell receptor and mediate virus-cell fusion Learn more ViroAntibodies
N Nucleocapsid protein, forms complexes with genomic RNA, interact with M protein for viral assembly Learn more ViroAntibodies
M Membrane protein, virus assembly Learn more ViroAntibodies
E Envelope protein, virus assembly and morphogenesis Learn more ViroAntibodies
NSP8 Non-structural protein Learn more ViroAntibodies
ORF7a Accessory protein Learn more ViroAntibodies
RdRp Viral replication Learn more ViroAntibodies

The current provided SARS-CoV antibody products are for research use only and are not approved for use in humans or in clinical diagnosis and therapeutics. If you are interested in SARS-CoV-2 antibody discovery and development services for in vitro diagnosis or therapeutic applications, please contact us for more details.


  1. van Doremalen, Neeltje, et al. "Aerosol and surface stability of SARS-CoV-2 as compared with SARS-CoV-1." New England Journal of Medicine (2020).
  2. Fehr, Anthony R., and Stanley Perlman. "Coronaviruses: an overview of their replication and pathogenesis." Coronaviruses. Humana Press, New York, NY, 2015. 1-23.
  3. Ge, Xing-Yi, et al. "Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor." Nature 503.7477 (2013): 535-538.
  4. Holmes, Kathryn V. "SARS-associated coronavirus." New England Journal of Medicine 348.20 (2003): 1948-1951.
  5. Hilgenfeld, Rolf, and Malik Peiris. "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses." Antiviral research 100.1 (2013): 286-295.
All products and services are intended for Research Use Only, and NOT to be used in diagnostic or therapeutic procedures.

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