Volume 6, Issue 2, June 2020, Page: 46-48
Covid-19 Pandemic, Glycobiology, Glycan Shields, Vaccine Strategies, Heparin Sulfate: A Mini Review
Steven Oppenheimer, Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, United States
Received: May 27, 2020;       Accepted: Jun. 11, 2020;       Published: Jun. 20, 2020
DOI: 10.11648/j.ajasr.20200602.14      View  289      Downloads  379
The area of sugar biology (glycobiology) is an under-reported component of the Covid-19 pandemic. This mini-review will provide non-experts with a brief overview of some aspects of glycobiology with emphasis on metabolic pathways and enzymes that are involved in the main topic of this review, the virus glycan shields of HIV and SARS-Cov-2 that help protect the viruses from immunological recognition. The HIV glycan shield is more dense than the SARS-Cov-2 shield and is one reason that a successful HIV vaccine has not yet been developed. The glycan shields of both HIV and SARS-Cov-2 consist of mannose chains and other sugars that resemble host molecules, explaining why they are not strongly recognized by the host’s immune system as foreign. But because of the less dense SARS-Cov-2 glycan shield there is more optimism that an effective SARS-Cov-2 vaccine could be developed. This, in addition, to unusual vaccine approaches using, for example, virus messenger RNA instead of whole cells or viral proteins, and potential use of heparin sulfate to block virus attachment to cells are concepts that will be also discussed. This mini-review therefore begins with an overview of glycobiology to introduce the topic of viral glycan shields of HIV compared with SARS-COV-2. This is followed by discussion of novel vaccine approaches for SARS-COV-2 and the interesting issue of the glycan heparin sulfate that binds to the SARS-COV-2 surface and might be engineered to produce an anti-viral drug.
Covid-19, HIV, SARS-COV-2, Glycan Shields, m-RNA Vaccines, Heparin Sulfate
To cite this article
Steven Oppenheimer, Covid-19 Pandemic, Glycobiology, Glycan Shields, Vaccine Strategies, Heparin Sulfate: A Mini Review, American Journal of Applied Scientific Research. Vol. 6, No. 2, 2020, pp. 46-48. doi: 10.11648/j.ajasr.20200602.14
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This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Oppenheimer, S. B., Edidin, M,, Orr, C., Roseman, S. An L-glutamine requirement for intercellular adhesion, Proceedings of the National Academy of Sciences USA, 63 (1969) pp. 1395-1402.
Oppenheimer, S., Humphreys, T. Isolation of specific macromolecules required for adhesion of mouse tumor cells, Nature 232 (1971), pp. 125-127.
Neri, A., Roberson, M., Connolly, D., Oppenheimer, S. Quantitative evaluation of receptor site distributions on the surfaces of specific populations of embryonic cells, Nature 258 (1975), pp. 342-344.
Oppenheimer, S., Meyer, J. Carbohydrate specificity of sea urchin adhesion component, Experimental Cell Research, 139 (1982), pp. 451- 456.
Idoni, B., Ghazarian, H., Metzenberg, S., Hutchins-Carroll, V, Carroll, Jr., E., Oppenheimer, S. Use of specific glycosidases to probe cellular interactions in the sea urchin embryo. Experimental Cell Research, 316 (2010), pp. 2204-2211.
Aleksanyan, H., Liang, j., Metzenberg, S., Oppenheimer, S.. Terminal alpha-D-mannosides are critical during sea urchin gastrulation, Zygote doi: 10.1017/SO967199416000113 (2016).
Liang, J., Aleksanyan, H., Metzenberg, S., Oppenheimer, S. Involvement of L-rhamnose in sea urchin gastrulation. Part II: alpha rhamnosidase, Zygote (2016) pp. 37—377.
Ghazarian, H., Idoni, B., Oppenheimer, S. B. A Glycobiology review, Acta Histochemica 113 (2011), pp. 236-247.
Lairson, L. L., Henrissat, B., Davies, G. L. Withers, S. G. Glycosyl transferases: structures, functions, and mechanisms Annu Rev Biochem. 77 (2008) pp. 521-555.
Watanabe, Y., Bowden, T. A., Wilson, I. A., Crispin, M. Exploitation of glycosylation in enveloped virus pathobiology, Biochim Biophys. Acta Gen Subj 1863 (2019), pp. 480-497.
Crispin, M., Doores, K. J., Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design Curr. Opin. Virol. 11 (2015) pp. 63-69.
Seabright, G. E., Doores, K. J., Burton, Crispin, M. Protein and glycan mimicry in HIV vaccine design J. Mol Biol 431 (2019) pp. 2223-2247.
Watanabe, Y., Allen, J. D., Wrapp, D., McLellan, Crispin, M. Site-specific glycan analysis of the SARS-Cov-2 spike Science 04 May (2020) DOI: 10.1126/science.abb9983.
Mann, A. Spike protein for a potential vaccine https://news.uga.edu/searching-for-the covid-spike protein for a potential vaccine https:// phys.org.news/2020-04 (2020).
Crispin, M., Ward, A. B., Wilson, I. A. Structure and immune recognition of the HIV glycan shield Annu. Rev. Biophys. 47 (2020), pp. 499-523.
Chamary, J. V. Unlike HIV, coronavirus has a weak shield https://www.forbes.com/sites/jvchamary/2020/05/04/coronavirud-v (2020).
Thachil, J. The versatile heparin in Covid-19. Journal of Thrombosis and Haemostasis 18 (2020) https://doi.org/10.1111/jth. 14821. (2020).
Liu, L., Chopra, P., Wolfert, M. A., Tompkins, S. M. SARS-Cov-2 spike protein binds heparin sulfate in a length and sequence-dependent manner, doi: https: www.biorxiv.org/content (2020).
Moderna News Release, Moderna’s work on a Covid-19 vaccine candidate (m-RNA-1273), May (2020).
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