The structural and molecular dynamics studies unravel the structure of novel coronavirus

Naveen Vankadari, Jacqueline A Wilce

Overview

#COVID-19 or SARS-CoV-2 differs in its protein sequence with other SARS coronavirus. The study shows how this new virus camouflages in human though its unique glycosylation of spike glycoprotein. The study also finds human CD26 as a new target for this coronavirus for cell adhesion & hijacking.

Summary

The COVID-19 pandemic across is the current public-health emergency around the globe and killed more than 35,000 people and nearly one-million people getting infected. It is important to know how this virus is camouflaged and attacks human cell for infection. Unravelling these molecular issues will abet in finding the bonafide therapeutics.

Author Comments

Dr Vankadari Naveen, MS., MPhil., DCA., PhD,
Dr Vankadari Naveen, MS., MPhil., DCA., PhD,
Monash University
Research Fellow
Biochemistry, Virology, Molecular Biology, Structural Biology, Molecular dynamics, Microbiology
Melbourne, VIC | Australia
The recent outbreak of pneumonia-causing COVID-19 pandemic is an urgent global public health issue with an increase in mortality and morbidity. The structures of COVID-19 spike glycoprotein in both closed (ligand-free) and open (ligand-bound) conformation open the arena of viral infection. While designing antibodies, the glycosylation pattern of virus need to be considered or the antibodies are useless. The structural and molecular dynamic studies show new human target for this virus and abet in finding new therapeutic to block the interaction between the virus and human CD26 a key immunoregulatory factor for cell adhesion and virulence.Dr Vankadari Naveen, MS., MPhil., DCA., PhD,

Resources

Twitter
https://twitter.com/NaveenV37588539/status/1241996585623375872
Scientific Research Journal
https://www.tandfonline.com/doi/full/10.1080/22221751.2020.1739565
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32178593

Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26.

Authors:
Dr Vankadari Naveen, MS., MPhil., DCA., PhD,
Dr Vankadari Naveen, MS., MPhil., DCA., PhD,
Monash University
Research Fellow
Biochemistry, Virology, Molecular Biology, Structural Biology, Molecular dynamics, Microbiology
Melbourne, VIC | Australia

Emerg Microbes Infect 2020 17;9(1):601-604. Epub 2020 Mar 17.

Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.

The recent outbreak of pneumonia-causing COVID-19 in China is an urgent global public health issue with an increase in mortality and morbidity. Here we report our modelled homo-trimer structure of COVID-19 spike glycoprotein in both closed (ligand-free) and open (ligand-bound) conformation, which is involved in host cell adhesion. We also predict the unique N- and O-linked glycosylation sites of spike glycoprotein that distinguish it from the SARS and underlines shielding and camouflage of COVID-19 from the host the defence system. Furthermore, our study also highlights the key finding that the S1 domain of COVID-19 spike glycoprotein potentially interacts with the human CD26, a key immunoregulatory factor for hijacking and virulence. These findings accentuate the unique features of COVID-19 and assist in the development of new therapeutics.

Download full-text PDF

Source
http://dx.doi.org/10.1080/22221751.2020.1739565DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103712PMC
March 2020

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References

(Supplied by CrossRef)

Xiong XL et al.
J Virol 2018

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