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Structure and Assembly | Spotlight

Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase

Xiaojin Xu, Xueyong Zhu, Raymond A. Dwek, James Stevens, Ian A. Wilson
Xiaojin Xu
1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
3Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
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Xueyong Zhu
1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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Raymond A. Dwek
3Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
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James Stevens
1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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Ian A. Wilson
1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
2Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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  • For correspondence: wilson@scripps.edu
DOI: 10.1128/JVI.00959-08
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ABSTRACT

Influenza virus neuraminidase (NA) plays a crucial role in facilitating the spread of newly synthesized virus in the host and is an important target for controlling disease progression. The NA crystal structure from the 1918 “Spanish flu” (A/Brevig Mission/1/18 H1N1) and that of its complex with zanamivir (Relenza) at 1.65-Å and 1.45-Å resolutions, respectively, corroborated the successful expression of correctly folded NA tetramers in a baculovirus expression system. An additional cavity adjacent to the substrate-binding site is observed in N1, compared to N2 and N9 NAs, including H5N1. This cavity arises from an open conformation of the 150 loop (Gly147 to Asp151) and appears to be conserved among group 1 NAs (N1, N4, N5, and N8). It closes upon zanamivir binding. Three calcium sites were identified, including a novel site that may be conserved in N1 and N4. Thus, these high-resolution structures, combined with our recombinant expression system, provide new opportunities to augment the limited arsenal of therapeutics against influenza.

  • Copyright © 2008 American Society for Microbiology
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Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase
Xiaojin Xu, Xueyong Zhu, Raymond A. Dwek, James Stevens, Ian A. Wilson
Journal of Virology Oct 2008, 82 (21) 10493-10501; DOI: 10.1128/JVI.00959-08

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Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase
Xiaojin Xu, Xueyong Zhu, Raymond A. Dwek, James Stevens, Ian A. Wilson
Journal of Virology Oct 2008, 82 (21) 10493-10501; DOI: 10.1128/JVI.00959-08
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KEYWORDS

Influenza A Virus, H1N1 Subtype
neuraminidase
Zanamivir

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