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ABSTRACT
Glycans are among the most important cell molecular components. However, given their structural diversity, their functions have not been fully explored. Glycosylation is a vital post-translational modification for various proteins. Many bacteria and viruses rely on N-linked and O-linked glycosylation to perform critical biological functions. The diverse functions of glycosylation on viral proteins during viral infections, including Dengue, Zika, influenza, and human immunodeficiency viruses as well as coronaviruses have been reported. N-linked glycosylation is the most common form of protein modification, and it modulates folding, transportation and receptor binding. Compared to N-linked glycosylation, the functions of O-linked viral protein glycosylation have not been comprehensively evaluated. In this review, we summarize findings on viral protein glycosylation, with particular attention to studies on N-linked glycosylation in viral life cycles. This review informs the development of virus-specific vaccines or inhibitors.
Acknowledgments
We thank Ms. Qianqian Zhang, Fujian Agriculture and Forestry University, for the critical reading of the manuscript and valuable discussions.
Disclosure statement
No potential conflict of interest was reported by the author(s).
Data availability statement
Data sharing not applicable to this article as no data sets were generated or analyzed during the current study. Data cited in this review are published and available online or upon request from the authors of the respective publications.