Human cell surface proteins selectively assembled into vesicular stomatitis virus virions

Area of Science:

• Virology
• Cell Biology
• Immunology

Background:

• Vesicular stomatitis virus (VSV) is known to assemble proteins from host cells into progeny virions.
• Understanding the selective incorporation of host proteins by VSV can provide insights into viral assembly mechanisms and host-cell interactions.

Purpose of the Study:

• To identify and characterize human cell proteins selectively assembled by VSV into progeny virions.
• To investigate the association of these host-derived viral proteins with specific human tumor types.

Main Methods:

• Purification and analysis of VSV virions produced in human cell lines (HeLa, T47D, HMB2) using SDS-polyacrylamide gel electrophoresis.
• Production of antisera against VSV-assembled host proteins using a VSV mutant (tsO45).
• Antigenic characterization of selected proteins using antibody reactivity and association studies with tumor tissues.

Main Results:

• VSV selectively assembled two to three host proteins (around 100K Mr) into virions.
• At least three distinct antigenic specificities were detected among the assembled host proteins.
• Proteins selected from gynecological tumor cell lines (HeLa, T47D) showed relatedness and were associated with epithelial-derived gynecological tumors, with lower expression in normal ovarian tissues.
• A distinct antigen assembled from melanoma cells (HMB2) was associated with cell growth.

Conclusions:

• VSV selectively incorporates specific host cell proteins, with distinct patterns observed depending on the cell of origin.
• The identified host-derived viral proteins exhibit differential associations with tumor types, suggesting potential as biomarkers, particularly for gynecological cancers.
• The precise mechanisms for VSV's selective protein assembly remain unclear but may involve shared structural properties with viral glycoproteins or endogenous retroviral elements.