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Background
SARS-CoV-2 has caused a sustained epidemic of novel coronavirus infections worldwide. SARS-CoV-2 belongs to the group of β-coronaviruses with typical β-coronavirus genome organization. The viral genome consists of an approximately 30kb of positive-signature single-stranded RNA encoding 29 proteins, including 16 non-structural and 4 structural proteins and 9 accessory proteins. Among the structural proteins are spike proteins (S), envelope proteins (N), membrane proteins (M), and nucleocapsid proteins (N), which are required for viral assembly and the production of structurally intact viral particles.
N protein is one of the most abundant structural proteins in SARS-CoV-2 and contains three intrinsically disordered regions (N-arm, central linkage region and C-tail) and two structural domains: the N-terminal domain (NTD) and the C-terminal domain (CTD). CTD is hydrophobic and rich in α-helical structures that mediate dimerisation and oligomerisation of N proteins. The intrinsically disordered region (IDR) in the middle of the NTD and CTD contains a serine/arginine-rich region (SR), the phosphorylation of which inhibits the dimerisation and translational repression activity of N proteins. Tyrosine residue 109 in the NTD is critical for RNA binding, and mutation of this site greatly attenuates the ability of the N protein to bind RNA.
Figure 1. Genome organization of SARS-CoV-2 and N protein (Source: Peng Y, et al. 2020)
Coronavirus N proteins are highly basic and multiactive RNA-binding proteins in coronaviruses, which play an essential role in viral infection and replication as the most abundant proteins that help viruses to infect cells. The SARS-CoV-2 N protein plays a key role in the viral life cycle, and it is mainly responsible for wrapping the ssRNA viral genome to form a ribonucleoprotein complex, thus protecting the viral RNA from degradation by host factors. In addition, N proteins are involved in regulating the transcription and replication of viral RNA and the assembly of viral particles. The N protein stimulates the body's immune response when the host is infected. Over-replication of the virus in the body stimulates an abnormal, uncontrolled 'cytokine storm' that can lead to lung dysfunction, heart damage, and even multiple organ failure. It was found that the N protein promotes the activation of NLRP3 inflammatory bodies, thereby causing a 'cytokine storm'. In addition, N proteins are relatively stable, immunogenic and less likely to mutate during infection than other proteins, and are therefore considered a key diagnostic molecular marker and prophylactic target.
Alternative Names
Anti-SARS-CoV-2 N
References
1. Bai C, et al. Overview of SARS-CoV-2 genome-encoded proteins. Sci China Life Sci. 2022 Feb;65(2):280-294.
2. Peng Y, et al. Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design. EMBO J. 2020 Oct 15;39(20):e105938.
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References
False-positive SARS-CoV-2 serology in 3 children with Kawasaki disease
DIAGNOSTIC MICROBIOLOGY AND INFECTIOUS DISEASE
Authors: To, Kelvin K. W.; Chua, Gilbert T.; Kwok, Ka Li; Wong, Joshua S. C.; Au, Dennis Chi Yu; Lam, Yuen Yu; Wong, Wilfred H. S.; Ho, Marco H. K.; Chan, Godfrey C. F.; Chui, Celine S. L.; Li, Xue; Tung, Keith T. S.; Wong, Rosa S.; Tso, Winnie W. Y.; Wong, Ian C. K.; Wong, Christina S. M.; Fong, Carol H. Y.; Chan, Kwok Hung; Yuen, Kwok Yung; Ip, Patrick; Kwan, Mike Y. W.
Background: Kawasaki disease (KD) is an acute febrile and eruptive disease with systemic vasculitis predominantly affecting young East Asian children. Recent reports showed that children with KD-like disease from KD low prevalence regions had positive SARS-CoV-2 serology despite a negative SARS-CoV-2 polymerase chain reaction (PCR) in respiratory samples. Objectives: To describe 3 pediatric Kawasaki Disease patients with false positive SARS-CoV-2 serology. Study design: We retrospectively recruited children with KD diagnosed during the COVID-19 outbreak in Hong Kong. Clinical characteristics and laboratory test results including SARS-CoV-2 PCR results were retrieved. We performed a microparticle-based immunoassay for the detection of IgG against nucleoprotein (NP) and spike protein receptor binding domain (RBD), and a microneutralization assay for the detection of neutralizing antibodies. Results: Three Chinese children with typical KD were identified. They had no epidemiological links with COVID-19 patients and tested negative for SARS-CoV-2 NPA PCR. Theywere treated with IVIG and aspirin, and were discharged without complications. Subsequently 2 of them were tested positive against anti-RBD and anti-NP antibodies and 1 was tested positive against anti- RBD antibodies. However, microneutralization assay showed that neutralizing antibodies were absent, suggesting a false-positive IgG result. Conclusion: Detection of neutralizing antibodies is recommended to confirm previous SARS-CoV-2 infection in IgGpositive but PCR-negative patients. (C) 2020 The Author(s). Published by Elsevier Inc.
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
COA
Publication 
Figure 1. Genome organization of SARS-CoV-2 and N protein
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