Antiviral Activities of Peptides with Sequences Related to the Cytoplasmic Domain of the Respiratory Syncytial Virus Glycoproteins

Abstract

A set of peptides from 6–10 amino acids in length with sequences corresponding to the respiratory syncytial virus (RSV) attachment glycoprotein, G, has been found to inhibit secretion of virus particles from two human cell lines infected with RSV. Peptides of similar lengths with sequences related to the fusion (F) protein were not effective. A modified assay for syncytia formation was used to measure infectious particles and we found that cell-free infectious RSV was inhibited by those same peptides that blocked particle release. However, only about 5–20% of the total infectious virus formed in the cultured cells was released from the cells – the remaining was assayable only after lysis of the infected cells. Formation of this major fraction of infectious, cell-associated RSV was not affected by the peptides. The inhibitory peptides were ineffective in blocking release of infectious virus from cells infected with influenza, vesicular stomatitis and Semliki Forest viruses. Only a set of specific amino acids in these peptides were inhibitory and they consisted of a very hydrophobic sequence that also required a cysteine residue.