VSIV G does not follow the same path as most vesicles because transport of the G protein from the ER to the plasma membrane is interrupted by incubation at 15 °C.

The material in the lipid-rich vesicle fraction appears to be a post-ER intermediate in the transport process to the plasma membrane (PM).

After infection, the VSIV G gene is expressed and is commonly studied as a model for N-linked glycosylation in the endoplasmic reticulum (ER).

It is translated into the rough ER where the Glc3-Man9-GlcNac2 oligosaccharide is added by a dolichol-containing protein, to an NXS motif on VSIV G. Sugars are removed gradually as the protein travels to the Golgi apparatus, and it becomes resistant to endoglycosidase H.[7] When synthesized in polarized epithelial cells, the envelope glycoprotein VSV G is targeted to the basolateral PM.

[citation needed] The VSIV L protein is encoded by half the genome, and combines with the phosphoprotein to catalyze replication of the mRNA.

[8][9] The main sign in animals is oral disease appearing as mucosal vesicles and ulcers in the mouth, but also on the udder and around the coronary band.

In most cases, VSV infection has resulted in a short 3 to 5 day illness characterized by fever, headache, myalgia, weakness and occasionally vesicular lesions of the mouth.

[10] Serological testing is most commonly performed with an ELISA or complement fixation, and viral isolation can also be attempted.

[2] Control relies on biosecurity protocols, quarantine, isolation and disinfection to ensure the viral disease does not enter a country or herd.

[17] The VSIV G protein is routinely used in biomedical research to pseudotype retroviral and lentiviral vectors, conferring the ability to transduce a broad range of mammalian cell types with genes of interest.

[8][20] Such studies help build a better understanding of viral behavior in the presence and absence of innate immune response.