Article ; Online: Unique fibrinogen-binding motifs in the nucleocapsid phosphoprotein of SARS CoV-2: Potential implications in host-pathogen interactions.
2020 Volume 144, Page(s) 110030
Abstract: Novel Coronavirus (SARS CoV-2), the etiological agent for the highly contagious Corona virus disease-2019 (COVID-19) pandemic has threatened global health and economy infecting around 5.8 million people and causing over 359,200 deaths (as of 28th May ... ...
| Abstract | Novel Coronavirus (SARS CoV-2), the etiological agent for the highly contagious Corona virus disease-2019 (COVID-19) pandemic has threatened global health and economy infecting around 5.8 million people and causing over 359,200 deaths (as of 28th May 2020, https://www.worldometers.info/coronavirus/). The clinical manifestations of infected patients generally range from asymptomatic or mild to severe illness, or even death. The ability of the virus to evade the host immune response have been major reasons for high morbidity and mortality. One of the important clinical observations under conditions of critical illness show increased risk of developing disseminated intravascular coagulation. Molecular mechanisms of how SARS CoV-2 induces such conditions still remain unclear. This report describes the presence of two unique motifs in the SARS CoV-2 nucleocapsid phosphoprotein (N-protein) that can potentially interact with fibrinogen and possibly prothrombin. This is based on an established function of secretory proteins in Staphylococcus aureus (S. aureus)-coagulase, Efb (Extracellular fibrinogen binding) and vWBP (von Willebrand factor Binding Protein), which are known to regulate the blood clotting cascade and the functions of host immune response. It is hypothesized that having protein interaction motifs that are homologous to these S. aureus proteins, the N-protein of this virus can mimic their functions, which may in turn play a crucial role in formation of blood clots in the host and help the virus evade host immune response. However, this hypothesis needs to be tested in vitro. Considering the overwhelming increase in the incidence of SARS CoV-2 infection globally, this information may be useful for further investigation and could help in deducing new therapeutic strategies to combat advanced stages of this disease. |
|---|---|
| MeSH term(s) | Amino Acid Motifs ; Bacterial Proteins/chemistry ; COVID-19/metabolism ; COVID-19/virology ; Coronavirus Nucleocapsid Proteins/chemistry ; Fibrinogen/chemistry ; Host-Pathogen Interactions/immunology ; Humans ; Immune System ; Models, Theoretical ; Peptides/chemistry ; Phosphoproteins/chemistry ; Protein Binding ; Protein Domains ; SARS-CoV-2 ; Staphylococcus aureus/enzymology ; von Willebrand Factor/chemistry |
| Chemical Substances | Bacterial Proteins ; Coronavirus Nucleocapsid Proteins ; Efb protein, Staphylococcus aureus ; Peptides ; Phosphoproteins ; nucleocapsid phosphoprotein, SARS-CoV-2 ; von Willebrand Factor ; Fibrinogen (9001-32-5) |
| Keywords | covid19 |
| Language | English |
| Publishing date | 2020-06-24 |
| Publishing country | United States |
| Document type | Journal Article |
| ZDB-ID | 193145-3 |
| ISSN | 1532-2777 ; 0306-9877 |
| ISSN (online) | 1532-2777 |
| ISSN | 0306-9877 |
| DOI | 10.1016/j.mehy.2020.110030 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
| Zs.A 1132: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG) |
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.