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In vitro selection and characterisation of influenza B/Beijing/1/87 isolates with altered susceptibility to zanamivir.

Abstract：

:We describe the in vitro selection and characterisation of virus derived from B/Beijing/1/87 passaged in the presence of zanamivir. During zanamivir passage, the phenotype of virus isolates was either drug dependent or drug resistant in plaque reduction assays. The susceptibility of the neuraminidase of the drug-dependent isolates was unchanged from that of the wild-type enzyme. The drug-dependent isolates contained two mutations in the viral haemagglutinin: V90A, close to the proposed secondary sialic acid-binding site, and L240Q, close to the primary sialic acid-binding site. Virus isolates that were drug resistant contained the same mutations in the haemagglutinin but also contained the mutation E116G in the neuraminidase. For the drug-dependent viruses, zanamivir susceptibility could not be measured because plaque numbers increased with increasing drug concentration. The in vitro zanamivir susceptibility of drug-resistant viruses was lower than that of the wild-type virus by a factor of 275- to >2532-fold. Neuraminidase containing the E116G mutation has a 33-fold lower affinity for zanamivir than the wild-type enzyme. The finding that the same haemagglutinin mutations are found in both drug-dependent and drug-resistant viruses confirms that the same changes to the receptor binding function can contribute to both phenotypes. This observation demonstrates the interplay between the influenza virus haemagglutinin and neuraminidase in escape from zanamivir inhibition in vitro.

journal_name

Virology

journal_title

Virology

authors

Barnett JM,Cadman A,Burrell FM,Madar SH,Lewis AP,Tisdale M,Bethell R

doi

10.1006/viro.1999.0058

subject

Has Abstract

pub_date

1999-12-20 00:00:00

pages

286-95

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(99)90058-2

journal_volume

265

pub_type

杂志文章

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