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Journal of General Virology, Vol 78, 107-111, Copyright © 1997 by Society for General Microbiology
ARTICLES |
TF Wild and R Buckland
INSERM Unit 404 Immunity and Vaccination, Institut Pasteur de Lyon, France. fwipaly@imaginet.fr
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.
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