Related Experiment Videos
Neutralized vesicular stomatitis virus binds to host cells by a different "receptor"
Biochemical and Biophysical Research Communications
|July 29, 1983
Summary
Neutralizing antibodies bind to vesicular stomatitis virus (VSV), forming complexes that still attach to and enter host cells. This suggests antibodies alter VSV’s cell binding, potentially affecting G protein fusion.
Area of Science:
- Virology
- Immunology
- Cell Biology
Background:
- Vesicular stomatitis virus (VSV) is a model virus used to study viral entry.
- Immune serum contains antibodies that can neutralize viral infectivity.
- Viral attachment and entry are critical steps in the viral life cycle.
Purpose of the Study:
- To investigate the cell binding and internalization mechanisms of VSV-antibody complexes.
- To compare the entry pathway of neutralized VSV with that of infectious VSV.
- To identify potential alterations in VSV-host cell interactions due to antibody binding.
Main Methods:
- Formation of VSV/antibody complexes using immune serum.
- Measurement of VSV and VSV/antibody complex binding to host cells.
- Assessment of viral internalization rates.
- Inhibition assays using phosphatidylserine and trypsin treatment.
Main Results:
- VSV/antibody complexes are non-infectious but bind and internalize into host cells similarly to infectious VSV.
- Binding and uptake of neutralized VSV are not inhibited by phosphatidylserine.
- Internalization of neutralized VSV shows partial sensitivity to trypsin treatment.
- These findings indicate that neutralized VSV utilizes different or additional cell binding sites.
Conclusions:
- Neutralizing antibodies do not completely abolish VSV cell binding and internalization.
- Antibody binding to VSV alters its interaction with host cells, suggesting a modified binding site.
- This alteration may interfere with the fusogenic activity of the VSV G protein, impacting viral entry.