Abstract
Animal viruses are parasites of animal cells that have characteristics such as heredity and replication. Viruses can be divided into non-enveloped and enveloped viruses if a lipid bilayer membrane surrounds them or not. All the membrane proteins of enveloped viruses that function in attachment to target cells or membrane fusion are modified by glycosylation. Glycosylation is one of the most common post-translational modifications of proteins and plays an important role in many biological behaviors, such as protein folding and stabilization, virus attachment to target cell receptors and inhibition of antibody neutralization. Glycans of the host receptors can also regulate the attachment of the viruses and then influence the virus entry. With the development of glycosylation research technology, the research and development of novel virus vaccines and antiviral drugs based on glycan have received increasing attention. Here, we review the effects of host glycans and viral proteins on biological behaviors of viruses, and the opportunities for prevention and treatment of viral infectious diseases.
Highlights
Animal viruses are parasites of animal cells that have characteristics such as heredity and replication, and are mainly composed of DNA or RNA, proteins and in some, a lipid membrane with glycoproteins [1]
Increasing evidence shows that the alterations in the N-glycan profile and sugar recognition pattern in host cells can reflect the progress of viral infection to some extent and are expected to be a new target for the diagnosis and treatment of viral infection [116]
We have summarized the progress in studying the effects of glycan on viral behavior in recent decades, which will provide new insights for the development of viral vaccines and help to develop new targets to protect against these viruses
Summary
Animal viruses are parasites of animal cells that have characteristics such as heredity and replication, and are mainly composed of DNA or RNA, proteins and in some, a lipid membrane with glycoproteins [1]. In Vero cells, removing the N-glycan near the highly conserved receptor binding domain on the envelope glycoprotein (GP) of the Ebola virus (EBOV) increased GP-mediated virus entry efficiency [30]. Their envelope is derived from the host cell membrane, and the glycan on viral proteins can affect the release of progeny virions.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
