3106269196

3106269196



RESULTS

Seąuence analysis of VSV G mutants.

In order to characterize the potential of VSV G protein mutants as novel oncolytic agents, we took advantage of previously isolated mutants derived from the HR variant of the San Juan isolate of VSV (Indiana serotype) (Francoeur et al., 1987). Mutants, G5Gsr, Gć and Gór were isolated, without prior mutagenesis, by virtue of their smali plaque-size phenotype on interferon (IFN)-inducible cells, but normal plaque-size on Vero cells. Furthermore, Gs and Gó were shown to be thermo-sensitive as their growth in a plaque assay on Vero cells was equal to that of HR at 34°C, but slightly reduced at 37°C (Francoeur et al., 1987). Revertants Gsr and Gćr were isolated by plating Gs and at 39-41°C on Vero cells (Francoeur et al., 1987). The Mmsir (Tl026) mutant was isolated in a different set of experiments from a mutagemzed stock of HR (Schincariol and Howatson, 1970). It is known to harbor an M51R amino acid replacement in the M protein (Desforges et al., 2001), but the remainder of its genome had not been sequenced previously. We therefore set out to sequence the entire genome of all four G protein mutants and compared it to the parental HR virus and the Mmsir mutant. Sequence analysis revealed that amino acid changes in these mutants were restricted to the G glycoprotein (Table 1 and data not shown). Even though the Mmsir mutant shows the same D216G substitution in its G protein as mutants Gs and Gó (Table 1), previous studies using viral recombinants containing the mutant M protein on a wild-type background or M protein transfection showed that the M protein on its own confers the attenuated phenotype suggesting that this mutation does not afifect viral replication (Ahmed et al., 2003; Black et al., 1993; Ferran and Lucas-Lenard, 1997).



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