- Future Students
- Current Students
- Faculty & Staff
A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3.
|Title||A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3.|
|Publication Type||Journal Article|
|Year of Publication||2000|
|Authors||Pastey M, Gower TL, Spearman PW, Crowe JE, Graham BS|
|Date Published||2000 Jan|
|Keywords||Amino Acid Sequence, Animals, Cell Fusion, Cells, Cultured, Enzyme-Linked Immunosorbent Assay, Giant Cells, Humans, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Parainfluenza Virus 3, Human, Peptide Fragments, Respiratory Syncytial Virus Infections, Respiratory Syncytial Virus, Human, rhoA GTP-Binding Protein, Vaccinia virus|
The fusion glycoproteins of human respiratory syncytial virus (RSV) and human parainfluenza virus type-3 (PIV-3) mediate virus entry and syncytium formation. Interaction between the fusion protein of RSV and RhoA, a small GTPase, facilitates virus-induced syncytium formation. We show here a RhoA-derived peptide inhibits RSV and syncytium formation induced by RSV and PIV-3, both in vitro by inhibition of cell-to-cell fusion and in vivo by reduction of peak titer by 2 log10 in RSV-infected mice. These findings indicate that the interaction between these two paramyxovirus fusion proteins and RhoA is an important target for new antiviral strategies.
|Alternate Journal||Nat. Med.|