Summary auto-generated
This study examined how synthetic peptides derived from the measles virus (MV) fusion protein could inhibit viral infection and cell-cell fusion. Researchers tested peptides corresponding to different alpha-helical regions of the F protein in infected cells. A peptide representing the leucine zipper region (amino acids 455-490) effectively inhibited MV fusion at concentrations as low as 3 micromolar, while a peptide from the amphipathic alpha-helix region (amino acids 148-177) showed no inhibition. The F455-490 peptide blocked both virus-to-cell and cell-to-cell fusion, reduced red blood cell lysis by over 90%, and prevented viral entry into cells. Notably, the peptide did not affect the synthesis or cell membrane transport of the F protein itself, nor did it prevent viral attachment. The inhibitory effect was specific to measles and the related canine distemper virus but not mumps virus. Under one-step growth conditions with high multiplicity of infection, viral yield remained unaffected, but plaque formation was reduced by over 90%, indicating the peptide's primary target is the fusion mechanism rather than viral replication machinery.
Key findings
- Synthetic peptide F455-490 corresponding to the leucine zipper region of measles virus fusion protein potently inhibits viral fusion at nanomolar to micromolar concentrations
- The inhibitory peptide blocks both virus-cell and cell-cell fusion without affecting F protein synthesis, transport to cell membrane, or viral attachment
- The F455-490 peptide demonstrates fusion inhibition activity specific to measles virus and canine distemper virus but not mumps virus
- Viral plaque formation and red blood cell lysis are inhibited over 90% by the peptide, while viral replication under one-step growth is unaffected
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Abstract
Measles virus (MV) infections are characterized by the induction of syncytia, i.e. the fusion of infected cells. Two MV proteins, the haemagglutinin (HA) and fusion (F) proteins, are involved in this process. Synthetic peptides representing two alpha-helical regions of the MV F protein were studied for their ability to inhibit MV fusion. A peptide corresponding to the leucine zipper region (amino acids 455- 490) inhibited MV fusion, whereas a peptide to amino acids 148-177, corresponding to the amphipathic alpha-helix region, did not. Fusion inhibition was also obtained with vaccinia virus-expressed HA and F, a recent wild-type MV isolate and the closely related canine distemper virus, but not with mumps virus. The F455-490 peptide did not affect the synthesis of MV F or its transport to the cell membrane. Virus-cell attachment was unaffected, but haemolysis and virus entry into the cell were inhibited. In one-step growth curves the virus yield was unaffected.