SARS-CoV-2; coronavirus; SARS-CoV-2 NP; SARS-CoV-2 Nucleocapsid Protein
Purity
>90% by SDS-PAGE
Format
Liquid
Concentration
lot specific
Buffer
PBS
Preservative
None
Storage
Store at -20°C to -80°C
Introduction
The 2019 novel coronavirus (SARS-CoV-2), also known as the Wuhan coronavirus, is a contagious virus that causes respiratory infection and has shown evidence of human-to-human transmission, first identified by authorities in Wuhan, Hubei, China, as the cause of the ongoing COVID-19 outbreak. Genomic sequencing has shown that it is a positive-sense, single-stranded RNA coronavirus.
Keywords
SARS-CoV-2; coronavirus; SARS-CoV-2 NP; SARS-CoV-2 Nucleocapsid Protein
Citations
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Background
COVID-19, which has caused global economic disruption and significant health risks, is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). SARS-CoV-2 is an enveloped positive-sense single-stranded RNA virus belonging to the β-coronavirus family, along with middle east respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV. The viral genome produces four structural proteins, the envelope (E), membrane (M), nucleocapsid (N) and S protein. The N protein is highly conserved and is the most abundant structural protein in virus-infected cells, and its main role is to integrate viral genomic RNA into the ribonucleoprotein complex and to facilitate the initiation of viral assembly by M and E proteins.
Coronavirus N protein consists of 419 amino acids, which can be classified into intrinsically disordered region (IDR) and conserved structural region based on sequence features. The IDR consists of three modules: the N-arm, the Ser/Arg-rich central flexible linkage region (LKR), and the C-tail, whereas the conserved structural region consists of two modules: the N-terminal structural domain (NTD) and the C-terminal structural domain (CTD). Each NTD molecule is in the shape of a right-handed fist, and the core subdomain consists of a five-stranded, U-shaped, antiparallel β-sheet with the topology β4-β2-β3-β1-β5, sandwiched between two short α-helices. In the NTD domain, the prominent β hairpin (β2'-β3') consists mainly of basic amino acid residues. Arginine residues that bind directly to the RNA are located in the positively charged canyon between the basic hairpin and the core structure. For the SARS-CoV-2 N-CTD, the positively charged groove consists of residues K256, K257, K261, and R262.
Figure 1. Structural overview of the SARS-CoV-2 N protein (Source: Bai Z, et al. 2021)
N proteins have been shown to be involved in host cellular mechanisms such as interferon inhibition, RNA interference, and apoptosis, and play a regulatory role in the viral life cycle. In addition, N proteins are immunodominant antigens in the host immune response and can be used as diagnostic antigens and immunogens. N proteins are major immunogens that induce a strong antibody response in the host, so N proteins can be used in serologic tests or a combination of N and S proteins can be used as capture antigens to increase test sensitivity. The N protein is also a promising target for drug discovery based on its conserved nature and critical role in viral replication.
Alternative Names
SARS-CoV-2 N Protein
References
1. Bai Z, et al. The SARS-CoV-2 Nucleocapsid Protein and Its Role in Viral Structure, Biological Functions, and a Potential Target for Drug or Vaccine Mitigation. Viruses. 2021 Jun 10;13(6):1115.
2. Yu H, et al. The role of SARS-CoV-2 nucleocapsid protein in antiviral immunity and vaccine development. Emerg Microbes Infect. 2023 Dec;12(1):e2164219.
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References
Targeting virus-host interaction by novel pyrimidine derivative: anin silicoapproach towards discovery of potential drug against COVID-19
The entire human population over the globe is currently facing appalling conditions due to the spread of infection from coronavirus disease-2019 (COVID-19). The spike glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) present on the surface of the virion mediates the virus entry into the host cells and therefore is targeted by several scientific groups as a novel drug target site. The spike glycoprotein binds to the human angiotensin-converting enzyme-2 (hACE2) cell surface receptor abundantly expressed in lung tissues, and this binding phenomenon is a primary determinant of cell tropism and pathogenesis. The binding and internalization of the virus is the primary and most crucial step in the process of infection, and therefore the molecules targeting the inhibition of this process certainly hold a significant therapeutic value. Thus, we systematically applied the computational techniques to identify the plausible inhibitor from a chosen set of well characterized diaryl pyrimidine analogues which may disrupt interfacial interaction of spike glycoprotein (S) at the surface of hACE2. Using molecular docking, molecular dynamics (MD) simulation and binding free energy calculation, we have identified AP-NP (2-(2-amino-5-(naphthalen-2-yl)pyrimidin-4-yl)phenol), AP-3-OMe-Ph (2-(2-amino-5-(3-methoxyphenyl)pyrimidin-4-yl)phenol) and AP-4-Me-Ph (2-(2-amino-5-(p-tolyl) pyrimidin-4-yl)phenol) from a group of diaryl pyrimidine derivatives which appears to bind at the interface of the hACE2-S complex with low binding free energy. Thus, pyrimidine derivative AP-NP may be explored as an effective inhibitor for hACE2-S complex. Furthermore,in vitroandin vivostudies will strengthen the use of these inhibitors as suitable drug candidates against SARS-COV-2. Communicated by Ramaswamy H. Sarma
A comprehensive, longitudinal analysis of humoral responses specific to four recombinant antigens of SARS-CoV-2 in severe and non-severe COVID-19 patients
Author summary The world is facing an unprecedented challenge with communities and economies affected by the growing pandemic of coronavirus disease 2019 (COVID-19). Currently, there is no vaccine or effective drugs have been approved to treat or prevent COVID-19. The development of antibody response to SARS-CoV-2, the virus that causes COVID-19, started to be reported but remained largely elusive. Understanding the adaptive responses where the body makes antibodies that specifically bind to the SARS-CoV-2 among COVID-19 patients provides fundamental information for developing effective treatment and preventive vaccine. In this study, we not only successively analyzed the specificity and magnitude of antibody responses using four SARS-CoV-2 related antigens, but also monitored the neutralization potency of the convalescent sera from COVID-19 patients at the time point of hospital discharge and follow-up visit. Our results indicated that most patients generated humoral responses against nucleoprotein and three spike protein-related antigens with their distinct kinetics profiles. Additionally, most convalescent sera had the varying extents of neutralization activities against SARS-CoV-2. Of note, we identified that IgA antibody responses specific to S1 and ECD were strongly correlated with neutralization activities in non-severe patients, but not in severe patients. Furthermore, we identified a significant reduction of neutralizing activities of the convalescent sera within one month. Our data provide a collective basis of serological testing, antibody-based intervention, and vaccine design of COVID-19. There is an urgent need for effective treatment and preventive vaccine to contain this devastating global pandemic, which requires a comprehensive understanding of humoral responses specific to SARS-CoV-2 during the disease progression and convalescent phase of COVID-19 patients. We continuously monitored the serum IgM and IgG responses specific to four SARS-CoV-2 related antigens, including the nucleoprotein (NP), receptor binding domain (RBD), S1 protein, and ectodomain (ECD) of the spike protein among non-severe and severe COVID-19 patients for seven weeks since disease onset. Most patients generated humoral responses against NP and spike protein-related antigens but with their distinct kinetics profiles. Combined detection of NP and ECD antigens as detecting antigen synergistically improved the sensitivity of the serological assay, compared to that of using NP or RBD as detection antigen. 80.7% of convalescent sera from COVID-19 patients revealed that the varying extents of neutralization activities against SARS-CoV-2. S1-specific and ECD-specific IgA responses were strongly correlated with the neutralization activities in non-severe patients, but not in severe patients. Moreover, the neutralizing activities of the convalescent sera were shown to significantly decline during the period between 21 days to 28 days after hospital discharge, accompanied by a substantial drop in RBD-specific IgA response. Our data provide evidence that are crucial for serological testing, antibody-based intervention, and vaccine design of COVID-19.
COA
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Figure 1. Structural overview of the SARS-CoV-2 N protein
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