1- Department of Biotechnology, College of Science, University of Tehran, Tehran, Iran
2- Department of Biotechnology, College of Science, University of Tehran, Tehran, Iran , Asad@ut.ac.ir
2- Department of Biotechnology, College of Science, University of Tehran, Tehran, Iran , Asad@ut.ac.ir
Abstract: (171 Views)
In the last month of 2019, an unknown virus appeared in Wuhan, China. Sequencing studies have shown that the virus is a new member of the coronavirus family, which mostly causes a respiratory disease with pneumonia-like symptoms. The new coronavirus consists of 25 proteins, including 4 important structural proteins and 15 non-structural proteins. Spike protein is one of the most important structural proteins on the surface of the virus; It is highly glycosylated and plays a key role in the virus binding to the host cells. The binding of glycans to proteins affects their structure and function in two ways; They lead to proper protein folding, and can play an important role in protein interactions, and also, by covering the surface of the protein, it causes the virus to escape from the immune system. So it is obvious that the study of glycan structures becomes more important when either a vaccine is going to be designed or glycan structures have important roles in the folding, activity, and interaction of a protein. Therefore, since the spike protein is a non-functional structural protein, the study of glycan structures is important for two goals of vaccine design and investigating the role of glycans in protein interactions. In this article, we are going to review the most important findings on spike protein glycosylation and compare the amount of glycosylation in different viruses, indicating the importance of glycan structures in designing an effective vaccine.
Article Type: Analytic Review |
Subject:
Molecular biotechnology
Received: 2022/06/9 | Accepted: 2023/04/24
Received: 2022/06/9 | Accepted: 2023/04/24
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