Abstract

Neuraminidase (NA) is a glycoprotein of the influenza virus membrane and is involved in releasing newly made virus from infected cells, and thus it is the main target of the current influenza chemotherapy. Novel inhibitors of NA which is easily mutated are urgently required to be developed because of the recent emergence of oseltamivir‐resistant strains and highly pathogenic avian influenza viruses. Yeast cell surface engineering is one of the useful technologies for screening binding proteins with specific affinity to target molecules. In this study, we attempted to construct the efficient system for developing inhibitors of NA using this technology. The head domain of wild‐type or oseltamivir‐resistant (H275Y) H5N1 NA was displayed on yeast cell surface and their activities were evaluated. These results suggested that the displayed head domain of NAs retained the innate characteristics of NAs and was useful for evaluating inhibition activity[1].

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