Why are viral proteins glycosylated?

The envelope proteins of these viruses are heavily glycosylated, and these glycans can hide an antigenic epitope to thereby avoiding recognition by neutralizing antibodies (nAbs) against that site and providing a convenient way for viruses to infect host cells and to promote immune escape.

What is vesicular stomatitis virus glycoprotein?

The fusion glycoprotein (G protein) of vesicular stomatitis virus (VSV) and related rhabdoviruses (e.g., rabies virus) is the sole surface-expressed protein on the bullet-shaped virions. It mediates both attachment and low-pH-induced fusion (8).

What is glycosylation of a virus?

Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication.

What type of virus is vesicular stomatitis?

VSV is a zoonotic arbovirus that belongs to the family, Rhabdoviridae, the same family as the rabies viruses. VSV has an 11 kb genome that consists of a single strand of negative-sense RNA.

Why are proteins glycosylated?

Protein glycosylation, a general posttranslational modification of proteins involved in cell membrane formation, is crucial to dictate proper conformation of many membrane proteins, retain stability on some secreted glycoproteins, and play a role in cell–cell adhesion.

Why are some proteins glycosylated?

Protein glycosylation has multiple functions in the cell. In the ER, glycosylation is used to monitor the status of protein folding, acting as a quality control mechanism to ensure that only properly folded proteins are trafficked to the Golgi.

What is a vesicular stomatitis?

Vesicular stomatitis is a viral disease which primarily affects horses, cattle, and swine. The agent that causes vesicular stomatitis, VSV, has a wide host range and can occasionally infect sheep and goats.

What is glycosylation in protein?

Glycosylation, the attachment of sugar moieties to proteins, is a post-translational modification (PTM) that provides greater proteomic diversity than other PTMs.

Where does protein glycosylation start?

N-linked protein glycosylation begins with the synthesis of the oligosaccharide precursor in the cytoplasmic, which is then translocated to the endoplasmic reticulum (ER) lumen. After the oligosaccharide precursor undergoes several modifications, it is transferred to an asparagine residue of a nascent protein.