Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 438233
Title Mechanism-Based Covalent Neuraminidase Inhibitors with Broad Spectrum Influenza Antiviral Activity
Author(s) Kim, J.H.; Resende, R.; Wennekes, T.; Chen, N.; Bance, N.; Buchini, S.; Watts, A.G.; Pilling, P.; Streltsov, V.A.; Petric, M.; Liggins, R.; Barrett, S.; McKimm-Breschkin, J.L.; Niikura, M.; Withers, S.G.
Source Science 340 (2013)6128. - ISSN 0036-8075 - p. 71 - 75.
DOI https://doi.org/10.1126/science.1232552
Department(s) Laboratory for Organic Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2013
Keyword(s) virus neuraminidase - drug design - h1n1 virus - resistant - sialidase - 4-guanidino-neu5ac2en - sensitivity - oseltamivir - mutations - variant
Abstract Influenza antiviral agents play important roles in modulating disease severity and in controlling pandemics while vaccines are prepared, but the development of resistance to agents like the commonly used neuraminidase inhibitor oseltamivir may limit their future utility. We report here a new class of specific, mechanism-based anti-influenza drugs that function via the formation of a stabilized covalent intermediate in the influenza neuraminidase enzyme, and confirm this mode of action via structural and mechanistic studies. These compounds function in cell-based assays and in animal models, with efficacies comparable to that of the neuraminidase inhibitor zanamivir and with broad spectrum activity against drug-resistant strains in vitro. The similarity of their structure to that of the natural substrate and their mechanism-based design make these attractive antiviral candidates
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