Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent…
- C. U. Kim, W. Lew, R. Stevens
- Chemistry, BiologyJournal of the American Chemical Society
- 29 January 1997
The design, synthesis, and in vitro evaluation of the novel carbocycles as transition-state-based inhibitors of influenza neuraminidase (NA) are described and the presence of a large hydrophobic pocket in the region corresponding to the glycerol subsite of sialic acid is revealed.
Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase.
- S. Crennell, E. Garman, W. G. Laver, E. Vimr, G. Taylor
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 November 1993
The three-dimensional structure of a bacterial sialidase, from Salmonella typhimurium LT2, is reported and the structure of its complex with the inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid at 2.2-A resolution is compared.
Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
- J. Varghese, W. G. Laver, P. Colman
- ChemistryNature
- 5 May 1983
The tetrameric enzyme has circular 4-fold symmetry stabilized in part by metal ions bound on the symmetry axis, and sugar residues are attached to four of the five potential glycosylation sequences, and in one case contribute to the interaction between subunits in the tetramer.
Structure of the catalytic and antigenic sites in influenza virus neuraminidase
- P. Colman, J. Varghese, W. G. Laver
- ChemistryNature
- 5 May 1983
The catalytic sites of influenza virus neuraminidase are located on the upper corners of the box-shaped tetramer that forms the head of the molecule. Antigenic determinants form a nearly-continuous…
Molecular mechanisms of variation in influenza viruses
- R. Webster, W. G. Laver, G. Air, G. Schild
- MedicineNature
- 11 March 1982
This review summarizes recent information on the structure of the genes and their products, the way in which these vary and the effects of the changes on the biological activities of the virus.
Molecular basis for the resistance of influenza viruses to 4-guanidino-Neu5Ac2en.
- K. Staschke, J. Colacino, W. G. Laver
- Biology, ChemistryVirology
- 20 December 1995
We report the selection and characterization of influenza A/NWS-G70c and B/HK/8/73 (HG) viruses which are resistant to the potent influenza neuraminidase inhibitor, 4-guanidino-Neu5Ac2en. Viruses…
Morphology of the isolated hemagglutinin and neuraminidase subunits of influenza virus.
- W. G. Laver, R. Valentine
- Biology, MedicineVirology
- 1 May 1969
Determination of the number of nonoverlapping antigenic areas on Hong Kong (H3N2) influenza virus hemagglutinin with monoclonal antibodies and the selection of variants with potential epidemiological…
- R. Webster, W. G. Laver
- BiologyVirology
- 15 July 1980
The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody.
- R. Malby, W. R. Tulip, P. Colman
- BiologyStructure
- 1 August 1994
Antigenic structure and variation in an influenza virus N9 neuraminidase
- R. Webster, G. Air, W. G. Laver
- Biology, ChemistryJournal of Virology
- 1 September 1987
The NAs of several variants with sequence changes in the NC-41 epitope lost hemagglutinin activity without any loss of enzyme activity, suggesting that the two activities are associated with separate sites on the N9 NA head.
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