A COVID-19 vaccine candidate composed of SARS-CoV-2 RBD dimer and Neisseria meningitidis outer membrane vesicles

SARS-CoV-2 infection is mediated by the interaction of the spike glycoprotein trimer via its receptor-binding domain (RBD) with the host’s cellular receptor. Vaccines seek to block this interaction by eliciting...

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Self-adjuvant and immune-stimulating activity of the anti-meningococcus B vaccine candidate Neisseria Meningitidis adhesin A as a soluble recombinant antigen (NadAΔ351–405) or as part of bacterial outer membrane vesicles

New Biotechnology ◽

10.1016/j.nbt.2009.06.017 ◽

2009 ◽

Vol 25 ◽

pp. S6 ◽

Cited By ~ 1

Author(s):

R. Tavano ◽

S. Franzoso ◽

P. Cecchini ◽

E. Cartocci ◽

F. Oriente ◽

...

Keyword(s):

Neisseria Meningitidis ◽

Outer Membrane ◽

Vaccine Candidate ◽

Membrane Vesicles ◽

Recombinant Antigen ◽

Outer Membrane Vesicles ◽

Bacterial Outer Membrane

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Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein

Infectious Disorders - Drug Targets ◽

10.2174/1871526520666200804161650 ◽

2020 ◽

Vol 20 ◽

Author(s):

Bipin Singh

Keyword(s):

Receptor Binding ◽

Point Mutations ◽

Binding Domain ◽

Receptor Binding Domain ◽

Spike Glycoprotein ◽

Angiotensin Converting Enzyme 2 ◽

Recent Outbreak ◽

Novel Coronavirus ◽

Genomic Similarity

: The recent outbreak of novel coronavirus (SARS-CoV-2 or 2019-nCoV) and its worldwide spread is posing one of the major threats to human health and the world economy. It has been suggested that SARS-CoV-2 is similar to SARSCoV based on the comparison of the genome sequence. Despite the genomic similarity between SARS-CoV-2 and SARSCoV, the spike glycoprotein and receptor binding domain in SARS-CoV-2 shows the considerable difference compared to SARS-CoV, due to the presence of several point mutations. The analysis of receptor binding domain (RBD) from recently published 3D structures of spike glycoprotein of SARS-CoV-2 (Yan, R., et al. (2020); Wrapp, D., et al. (2020); Walls, A. C., et al. (2020)) highlights the contribution of a few key point mutations in RBD of spike glycoprotein and molecular basis of its efficient binding with human angiotensin-converting enzyme 2 (ACE2).

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COVID-eVax, an electroporated plasmid DNA vaccine candidate encoding the SARS-CoV-2 Receptor Binding Domain, elicits protective immune responses in animal models of COVID-19

Molecular Therapy ◽

10.1016/j.ymthe.2021.09.011 ◽

2021 ◽

Cited By ~ 1

Author(s):

Antonella Conforti ◽

Emanuele Marra ◽

Fabio Palombo ◽

Giuseppe Roscilli ◽

Micol Ravà ◽

...

Keyword(s):

Animal Models ◽

Immune Responses ◽

Dna Vaccine ◽

Receptor Binding ◽

Plasmid Dna ◽

Vaccine Candidate ◽

Binding Domain ◽

Receptor Binding Domain ◽

Plasmid Dna Vaccine

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Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein

Cell Reports ◽

10.1016/j.celrep.2018.06.041 ◽

2018 ◽

Vol 24 (2) ◽

pp. 441-452 ◽

Cited By ~ 30

Author(s):

Senyan Zhang ◽

Panpan Zhou ◽

Pengfei Wang ◽

Yangyang Li ◽

Liwei Jiang ◽

...

Keyword(s):

Receptor Binding ◽

Binding Domain ◽

Receptor Binding Domain ◽

Spike Glycoprotein ◽

Neutralization Epitope ◽

Definition Of ◽

Structural Definition

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Discovery of potential inhibitors of the receptor-binding domain (RBD) of pandemic disease-causing SARS-CoV-2 Spike Glycoprotein from Triphala through molecular docking

Current Chinese Chemistry ◽

10.2174/2666001601666210322121802 ◽

2021 ◽

Vol 01 ◽

Author(s):

Sharuk L. Khan ◽

Falak A. Siddiqui ◽

Mohd Sayeed Shaikh ◽

Nitin V. Nema ◽

Aijaz A. Shaikh

Keyword(s):

Molecular Docking ◽

Hydrogen Bonds ◽

Receptor Binding ◽

Chemical Constituents ◽

Antioxidant Properties ◽

Binding Domain ◽

Quality Data ◽

Receptor Binding Domain ◽

Spike Glycoprotein

Background: COVID-19 (SARS-CoV-2 infection) has affected almost every region of the world. Presently, there is no defined line of treatment available for it. Triphala is already proven to have a safe biological window and well known for its antioxidant and immunomodulatory properties. Objective: Present work has been carried out to study Triphala's effectiveness for the treatment of COVID-19. Methods: The Receptor-binding domain (RBD) of SARS-CoV-2 Spike Glycoprotein responsible for the invasion into the host cell, which leads to further infection. The molecular docking (MD) was performed to explore the binding affinities (kcal/mol) of Triphala's chemical constituents and compared them with the existing drugs under investigation for the treatment of COVID-19 epidemiology. Results: Chebulinic acid binding affinity -8.5 kcal/mol with the formation of 10 hydrogen bonds. Almost all the major chemical constituents have formed two or more hydrogen bonds with RBD of SARS-CoV-2 Spike Glycoprotein. Conclusion: The present study showed that Triphala might perform vital roles in the treatment of COVID-19 and expand its usefulness to physicians to treat this illness. There is a need to complete the in-vitro, in-vivo biological testing of Triphala on SARS-CoV-2 disease to create more quality data. The binding mode of Chebulinic acid in the allosteric cavity allows a better understanding of RBD of SARS-CoV-2 Spike Glycoprotein target and provides insight for the design of new inhibitors. Triphala is already proven to have a safe biological window, which indicates we can skip the pre-clinical trials. Apart from this, Triphala is well known for its antioxidant properties, which ultimately improves the immunity of the COVID-19 patient.

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