Resistance of a measles virus mutant to fusion inhibitory oligopeptides is not associated with mutations in the fusion peptide

Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein.

“…In the case of the tripeptide analogue (116-118), it has been proposed that this prevents fusion by competing with the fusion protein for a cellular receptor (Richardson et al, 1980). However, escape mutants that resist the effect of the tripeptide were found to possess mutations in the cysteine-rich region of MV F (Hull et al, 1987), which we have shown to be the site of interaction with the MV HA (T. F. Wild et al, 1994). This suggests that rather than having a direct effect on fusion, the tripeptide disrupts the F-HA interaction known to be a prerequisite for MV fusion (T. F. Wild et al, 1994).…”

Identification of Several Different Lineages of Measles Virus

“…One group of viruses (A) consists of the Edmonston-related sequences including, not surprisingly, the EdP9 salt-dependent haemagglutinating variant and the identical Moraten vaccine strain, but also strain Hu2, derived from a Schwarz vaccine-related death, and the Hall6 strain of virus isolated from an SSPE case. The M gene of the Hu2 strain shows only a few differences to the Edmonston strain (Curran & Rima, 1988) as does the F gene (Hull et al, 1987). Particularly, some of the differences in the M gene are probably significant in indicating re-adaptation of the vaccine strain to human Table 1 for descriptions of the strains).…”

Mutant Fusion Proteins with Enhanced Fusion Activity Promote Measles Virus Spread in Human Neuronal Cells and Brains of Suckling Hamsters

“…The L354M substitution is located in the cysteine-rich region, which is thought to interact with the H protein (50). Mutant MVs resistant to a fusion-inhibitory peptide contain amino acid substi- (51). The N462K substitution is located in the HR-B domain.…”