James Crowe
Faculty Member
Last active: 3/31/2020

RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation.

Pastey MK, Crowe JE, Graham BS
J Virol. 1999 73 (9): 7262-70

PMID: 10438814 · PMCID: PMC104251 · DOI:10.1128/JVI.73.9.7262-7270.1999

The fusion glycoprotein (F) of respiratory syncytial virus (RSV), which mediates membrane fusion and virus entry, was shown to bind RhoA, a small GTPase, in yeast two-hybrid interaction studies. The interaction was confirmed in vivo by mammalian two-hybrid assay and in RSV-infected HEp-2 cells by coimmunoprecipitation. Furthermore, the interaction of F with RhoA was confirmed in vitro by enzyme-linked immunosorbent assay and biomolecular interaction analysis. Yeast two-hybrid interaction studies with various deletion mutants of F and with RhoA indicate that the key binding domains of these proteins are contained within, or overlap, amino acids 146 to 155 and 67 to 110, respectively. The biological significance of this interaction was studied in RSV-infected HEp-2 cells that were stably transfected to overexpress RhoA. There was a positive correlation between RhoA expression and RSV syncytium formation, indicating that RhoA can facilitate RSV-induced syncytium formation.

MeSH Terms (20)

Amino Acid Sequence Binding Sites Chromosome Mapping Cloning, Molecular DNA, Complementary Enzyme-Linked Immunosorbent Assay Giant Cells GTP-Binding Proteins GTP Phosphohydrolases HeLa Cells HN Protein Humans Molecular Sequence Data Precipitin Tests Respiratory Syncytial Virus, Human rhoA GTP-Binding Protein Saccharomyces cerevisiae Tumor Cells, Cultured Viral Envelope Proteins Viral Proteins

Connections (1)

This publication is referenced by other Labnodes entities: