RESEARCH ARTICLES

Volume 9 |Issue 3| May-June 2021                                 First published: 30 June 2021

Glycosylation pattern in the glycoproteins of the Makona variant of Ebola virus

Mahale Kiran1*, Patole Milind1 and Walhe Rajan2*

1National Centre for Cell Science, SP Pune University Campus, Pune 411007, India.

2Department of Microbiology, MES Abasaheb Garware College, Pune 411004, India.

*Correspondence: kkmahale@gmail.com, rawalhe@rediffmail.com

Abstract

Surface glycoprotein of viruses like Ebola virus are very important, since they are the targets of many vaccination strategies. The current study focuses on the glycoprotein sequences of the West African Makona variant (2104-16) of Ebola virus. The protein sequences of the glycoprotein of 1,184 genomes and their glycosylation potential showed that the diversity of the protein sequences in the 2014-16 outbreak was limited and did not disturb the glycosylation potential of these proteins to a great extent.

Keywords:Ebola Virus, Makona, Vaccine, N-glycosylation, O-glycosylation

Editor: Dr.Arvind Chavhan

Cite this article as:
Mahale Kiran, Patole Milind and Walhe Rajan. Glycosylation pattern in the glycoproteins of the Makona variant of Ebola virus, Int. Res. Journal of Science & Engineering, 2021, Volume 9(3): 71-76.

References

1. Martinez O, Ndungo E, Tantral L, Miller EM, Leung LW, Chandran K, Basler CF. A Mutation in the Ebola Virus Envelope Glycoprotein Restricts Viral Entry in a Host Species- and Cell-Type-Specific Manner. Journal of Virology. 2013; 87 (6) :3324 –3334.

2. Kuhn JH, Becker S, Ebihara H, Geisbert TW, Johnson KM, Kawaoka Y, et al. Proposal for a revised taxonomy of the family Filoviridae: classification, names of taxa and viruses, and virus abbreviations. Archives of virology. 2010; 155 (12): 2083-2103.

3. Mahale KN, Patole MS. The crux and crust of ebolavirus: analysis of genome sequences and glycoprotein gene. Biochemical and biophysical research communications. 2015; 463 (4): 756-761.

4. Kuhn JH, Andersen KG, Baize S, Bào Y, Bavari S, et al. Nomenclature-and database-compatible names for the two Ebola virus variants that emerged in Guinea and the Democratic Republic of the Congo in 2014. Viruses. 2014; 6 (11): 4760-4799.

5. Ito H, Watanabe S, Takada A, Kawaoka Y. Ebola Virus Glycoprotein: Proteolytic Processing, Acylation, Cell Tropism, and Detection of Neutralizing Antibodies. Journal of Virology. 2019; 75 (3): 1576–1580.

6. Sanchez A, Kiley MP, Holloway BP, Auperin DD. Sequence analysis of the Ebola virus genome: organization, genetic elements, and comparison with the genome of Marburg virus. Virus research. 1993; 29 (3): 215-240.

7. Manicassamy B, Rong L. Expression of Ebolavirus glycoprotein on the target cells enhances viral entry. Virology Journal. 2009; 6 (75):1-15.

8. Lin G, Simmons G, Po¨hlmann S, Baribaud F, Ni H, Leslie G, Haggarty BS, Bates P, Weissman D, Hoxie JA, Doms RW. Differential N-Linked Glycosylation of Human Immunodeficiency Virus and Ebola Virus Envelope Glycoproteins Modulates Interactions with DC-SIGN and DC-SIGNR. Journal of Virology. 2003;77 (2): 1337–1346.

9. Cook JD, Lee JE. The secret life of viral entry glycoproteins: moonlighting in immune evasion. PLoS pathogens. 2013; 9 (5): e1003258.

10. Bagdonaite L, Wandall HH. Global aspects of viral glycosylation. Glycobiology. 2018;28 (7): 443–467.

11. Watanabe Y. Bowden TA, Wilson IA, Crispina M. Exploitation of glycosylation in enveloped virus pathobiology. BBA - General Subjects. 2019; 1863: 1480–1497.

12. Volchkov VE, Feldmann H, Volchkova VA, Klenk HD. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proceedings of the National Academy of Sciences. 1998; 95 (10): 5762-5767.

13. Apweiler R, Hermjakob H, Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochimica et Biophysica Acta (BBA)-General Subjects. 1999; 1473 (1): 4-8.

14. Krieg J, Hartmann S, Vicentini A, Gläsner W, Hess D, Hofsteenge J. Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-xx-Trp. Molecular biology of the cell. 1998; 9 (2): 301-309.

15. Vigerust D, Shepherd VL. Virus glycosylation: role in virulence and immune interactions. Trends in Microbiology. 2019; 15 (5): 211-218.

16. Iraqi M, Edri A, Greenshpan Y, Kundu K, Bolel P. et al. N-Glycans Mediate the Ebola Virus-GP1 Shielding of Ligands to Immune Receptors and Immune Evasion. Frontiers in cellular and infection Microbiology. 2020; 10 (48): 1-11.