Nonetheless,

sequencing of the PG545 resistant virus and

Nonetheless,

sequencing of the PG545 resistant virus and its comparison with the original and mock-passaged RSV revealed presence of the F168S and the P180S amino acid substitutions in the G protein in all three virus variants examined, and the V516I amino acid alteration in the F protein in variant A (Table 4). Because alteration in the F protein RGFP966 chemical structure was not found in all variants tested and the resistance of this variant was not substantially different from variants lacking this alteration, this mutation in contrast to alterations in the G protein is likely to be irrelevant for the resistant phenotype. RSV variants generated by selective pressure from muparfostat in 10 passages in HEp-2 cells were readily selected and appeared to be ∼7–9 times more resistant to this compound than original virus. All three plaque variants of resistant virus comprised the N191T amino acid change in the viral attachment protein G (Table 4). In addition to this mutation, variant A also contained the D126E amino acid substitution and the t642c (silent) nucleotide alteration in the G component. Because the drug resistance of variant A was similar to

variants B and C, the N191T amino Tyrosine Kinase Inhibitor Library in vitro acid change in the G protein seemed to confer RSV resistance to muparfostat. In repetition of this experiment, the RSV was subjected to 6 passages in HEp-2 cells in the presence of muparfostat and two viral variants were plaque purified and analyzed. Both variants were resistant to muparfostat and in contrast to initial or mock-passaged virus comprised the N191T amino acid substitution in the G protein (data not shown). One of these plaques also contained the K197T alteration in the G protein. These data confirm that the N191T alteration in the G protein is responsible for resistance Carbohydrate of RSV to muparfostat. Data presented

in Table 2 indicate that, unlike the sulfated oligosaccharides of muparfostat, inhibition of RSV infectivity by PG545 is associated with virucidal activity of this compound. The term “virucidal activity” is usually applied to agents that are capable of neutralizing, inactivating or destroying a virus permanently. We tested the virucidal potency of PG545 in a dose dependent manner. To this end, PG545 at the indicated concentrations and ∼105 PFU of RSV A2 strain were mixed in medium comprising 2% heat-inactivated FCS or in serum-free medium and incubated for 15 min at 37 °C. Subsequently, the virus-compound mixture was serially diluted and the residual virus infectivity determined at the non-inhibitory concentrations of PG545. In contrast to muparfostat, PG545 exhibited virucidal activity (Table 3). This activity of PG545 was most pronounced in the serum-free medium where 10 μg/ml of compound completely inactivated infectivity of ∼105 PFU of RSV. These results indicate that some components of FCS decreased anti-RSV activity of PG545.

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