Spike glycoprotein Proteins

Spike protein is one of the major structural proteins of severe acute respiratory syndrome-coronavirus. It is essential for the interaction of the virons with host cell receptors and subsequent fusion of the viral envelop with host cell membrane to allow infection. Some spike proteins of coronavirus are proteolytically cleaved into two subunits, S1 and S2.[1] The spike protein (S protein) has pivotal roles in viral infection and pathogenesis.

With the outbreak of Novel Coronavirus 2019(SARS-CoV-2, 2019-nCoV), the spike protein gets more and more attention. CUSABIO is one of the companies that research and manufacture spike protein related reagents for SARS-CoV-2 research in the world.

Now CUSABIO provides spike protein products of multiple species, including BCoV, HCoV-OC43, SARS-CoV and SARS-CoV-2 etc. Among of them, there are 18 recombinant spike proteins for SARS-CoV-2 research. They are featured with high purity (most of them greater than 90%), and low endotoxin. The bioactivity of some SARS-CoV-2 Spike proteins has been validated. Except for SARS-CoV-2 (2019-nCoV) Spike proteins, you can also find Spike proteins for other species in the following catalog. Quality is guaranteed. And our technical team will be here to support you.

Spike glycoprotein Proteins Catalog

Spike glycoprotein Proteins for Bovine coronavirus (strain vaccine) (BCoV) (BCV)

Spike glycoprotein Proteins for Human coronavirus OC43 (HCoV-OC43)

Spike glycoprotein Proteins for Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)

Spike glycoprotein Proteins for Human coronavirus HKU1 (isolate N5) (HCoV-HKU1)

Spike glycoprotein Proteins for Human coronavirus NL63 (HCoV-NL63)

Spike glycoprotein Proteins for Human coronavirus 229E (HCoV-229E)

Spike glycoprotein Proteins for Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)

Spike glycoprotein Proteins for Homo sapiens (Human)

Spike glycoprotein Background

SARS-CoV-2 (Severe acute respiratory syndrome coronavirus 2), a novel coronavirus found in late 2019, tremendously attracted the attention of global scientific researchers [2]. This newly definite coronavirus is an enveloped RNA virus, and it is zoonotic and can cause severe and atypical pneumonia [2]. One type of spike-like shaped protein on the envelope of the coronavirus is spike glycoproteins. People commonly call it S protein. The S-protein of the coronavirus is the structural protein responsible for the crown-like shape of the CoV viral particles, and "coronavirus" was originally named for this reason. S proteins belong to transmembrane proteins and mediate the viral attachment to host cell, host-virus interaction, and virus entry into the host cell [3][4]. There are two functional subunits in the S protein: S1 subunit responsible for binding to the host cell receptor and S2 subunit for the fusion of the viral and cellular membranes [5][6]. The S2 protein contains the fusion peptide (FP), a second proteolytic site (S2′), followed by an internal fusion peptide (IFP) and two heptad-repeat domains preceding the transmembrane domain (TM). Coronavirus enters cells by viral S glycoprotein-mediated binding to host cells and subsequent fusion of virus and host cell membranes [4]. During infection, the trimetric S-protein of coronavirus is processed at the S1/S2 cleavage site by host cell proteases [7]. S protein is divided into an N-terminal S1-ectodomain that recognizes a cognate cell surface receptor and a C-terminal S2-membrane-anchored protein involved in viral entry after the cleavage or priming [7]. The SARS-CoV S1-protein recognizes the angiotensin-converting enzyme 2 (ACE2) through a conserved Receptor Binding Domain (RBD) [8]. Wan et al. found that several residues among the 14 amino acids in the S1 of SARS-CoV are strictly conserved in 2019-nCoV, suggesting that ACE2 is also the receptor of the newly emerged nCoV [2][9]. The internal fusion peptides (IFPs) of the 2019-nCoV are the same as that of the SARS-CoV, showing characteristics of viral fusion peptides [9]. Alexandra C. Walls et al. identified a peculiar furin-like cleavage site in the spike protein of the SARS-CoV-2, lacking in the other SARS-like CoVs, despite a high similarity with the genome sequence of SARS-CoV and SARS-like CoVs [6]. Berend-Jan Bosch, a coronavirus specialist at Utrecht University in the Netherlands, said that all viral proteins will elicit antibody responses to some extent. Since spike protein is the sole protein on the viral surface responsible for entry into the host cell, it is the main antigen that elicits neutralizing antibodies. Some SARS-CoV-2 S1 protein IgG antibody ELISA kits, therefore, are developed to detect this virus. Spike S2 subunit is more conserved among CoVs and thus plays a role in the cross-reactivity seen when the whole S was used as an antigen. While S1 is more specific than S as an antigen for SARS-CoV-2 serological diagnosis.

[1] Wu XD1, Shang B, et al. The spike protein of severe acute respiratory syndrome (SARS) is cleaved in virus infected Vero-E6 cells [J]. Cell Res. 2004 Oct;14(5):400-6.
[2] Na Zhu, Ph.D., et al. A Novel Coronavirus from Patients with Pneumonia in China, 2019 [J]. N Engl J Med 2020; 382:727-733.
[3] M.A. Tortorici, D. Veesler. Structural insights into coronavirus entry [J]. Adv. Virus Res., 105 (2019), pp. 93-116.
[4] Shulla A, Gallagher T. Role of spike protein endodomains in regulating coronavirus entry [J]. J Biol Chem. 2009 Nov 20;284(47):32725-34.
[5] Xiuyuan Ou, Yan Liu, et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV [J]. Nature Communications volume 11, Article number: 1620 (2020).
[6] Alexandra C.Walls, Young-JunPark, et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein [J]. Cell. Volume 181, Issue 2, 16 April 2020, Pages 281-292.
[7] B.Coutard, C.Valle, et al. The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade [J]. Antiviral Research Volume 176, April 2020, 104742.
[8] W. Li, M.J. Moore, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus [J]. Nature, 426 (2003), pp. 450-454.
[9] Y. Wan, J. Shang, et al. Receptor recognition by novel coronavirus from Wuhan: an analysis based on decade-long structural studies of SARS [J]. J. Virol. (2020).


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