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Review
. 2021 Jul 15:16:4813-4830.
doi: 10.2147/IJN.S302516. eCollection 2021.

Glycan Nanostructures of Human Coronaviruses

Wanru Guo  1 , Harini Lakshminarayanan  2 , Alex Rodriguez-Palacios  3   4   5   6 , Robert A Salata  7 , Kaijin Xu  1 , Mohamed S Draz  7
Affiliations
Review

Glycan Nanostructures of Human Coronaviruses

Wanru Guo et al. Int J Nanomedicine. .

Abstract

Human coronaviruses present a substantial global disease burden, causing damage to populations' health, economy, and social well-being. Glycans are one of the main structural components of all microbes and organismic structures, including viruses-playing multiple essential roles in virus infection and immunity. Studying and understanding virus glycans at the nanoscale provide new insights into the diagnosis and treatment of viruses. Glycan nanostructures are considered potential targets for molecular diagnosis, antiviral therapeutics, and the development of vaccines. This review article describes glycan nanostructures (eg, glycoproteins and glycolipids) that exist in cells, subcellular structures, and microbes. We detail the structure, characterization, synthesis, and functions of virus glycans. Furthermore, we describe the glycan nanostructures of different human coronaviruses, such as human coronavirus 229E (HCoV-229E), human coronavirus OC43 (HCoV-OC43), severe acute respiratory syndrome-associated coronavirus (SARS-CoV), human coronavirus NL63 (HCoV-NL63), human coronavirus HKU1 (HCoV-HKU1), the Middle East respiratory syndrome-associated coronavirus (MERS-CoV), and how glycan nanotechnology can be useful to prevent and combat human coronaviruses infections, along with possibilities that are not yet explored.

Keywords: SARS-CoV-2; coronaviruses; diagnostics; glycan; glycolipids; glycoproteins; nanotechnology; vaccine.

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Conflict of interest statement

The authors declare no conflicts of interest for this work.

Figures

Figure 1
Figure 1
Structure of glycoproteins. Glycoproteins are mainly glycosylated with N-linked and O-linked glycans. N-glycans are attached to the asparagine residues, and they are processed in the Golgi apparatus to yield oligomannose, hybrid, and complex-type N-glycan structures. The mucin-type O-linked glycosylation mainly contains four common O-linked glycan cores. Non-mucin-type O-glycosylations are produced by attaching GlcNAc, mannose, fucose, glucose, galactose, or xylose to the amino acid.
Figure 2
Figure 2
N-linked glycosylation of proteins in the ER and Golgi apparatus.
Figure 3
Figure 3
The symptoms of coronaviruses infection.
Figure 4
Figure 4
Comparison of different genome structures of coronaviruses.
Figure 5
Figure 5
The difference in the glycans on the virus particles of coronaviruses.
Figure 6
Figure 6
N-linked glycans on the middle east respiratory syndrome-associated coronavirus (MERS) and severe acute respiratory syndrome (SARS)-associated coronavirus S proteins. Reprinted with permission from Watanabe, Y et al Vulnerabilities in coronavirus glycan shields despite extensive glycosylation. Nat Commun. 2020;11(1): 2688. Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/).
Figure 7
Figure 7
SARS-CoV-2 S N-linked glycans.
Figure 8
Figure 8
Glycan structure of the spike protein of SARS-CoV-2.
Figure 9
Figure 9
Mutations in the S protein N-glycosylation sites of N234A and N165A show increased instability of RBD-A in the “up” state (A–D).
Figure 10
Figure 10
Applications of glycans in the diagnosis and treatment of viral infections.
Figure 11
Figure 11
Idealistic versus realistic view of active targeting nanomedicines.
See this image and copyright information in PMC

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