A single site for N-linked glycosylation in the envelope glycoprotein of feline immunodeficiency virus modulates the virus-receptor interaction
2008

How a Mutation in FIV Affects Virus Interaction with Receptors

publication Evidence: moderate

Author Information

Author(s): Willett Brian J, McMonagle Elizabeth L, Logan Nicola, Samman Ayman, Hosie Margaret J

Primary Institution: University of Glasgow

Hypothesis

The study investigates how specific mutations in the feline immunodeficiency virus (FIV) envelope glycoprotein influence its interaction with cellular receptors.

Conclusion

The T271I mutation in FIV significantly alters the virus's interaction with the CD134 receptor, potentially impacting its ability to infect cells.

Supporting Evidence

  • The T271I mutation alters the nature of the virus-CD134 interaction.
  • Primary viruses with the T271I mutation do not require certain receptor determinants for entry.
  • The study suggests that glycosylation sites in the FIV envelope are critical for receptor binding.

Takeaway

The study found that a small change in the virus can change how it attaches to cells, which might help it spread better.

Methodology

The researchers introduced mutations into the FIV envelope glycoprotein and assessed their effects on receptor interactions and viral entry.

Limitations

The study primarily focuses on specific mutations and may not account for other factors influencing FIV receptor interactions.

Digital Object Identifier (DOI)

10.1186/1742-4690-5-77

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication