Journal ArticleDOI
Influenza virus neuraminidase with hemagglutinin activity.
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TLDR
Viruses possessing N9 NA have two different HA activities and antibody to either HA or NA alone was incapable of inhibiting hemagglutinin by the virus, but antibody to the HA of an H1N9 virus neutralized its infectivity as effectively as it neutralized H 1N1 or H1n2 viruses whose neuraminidases have no HA activity.About:
This article is published in Virology.The article was published on 1984-09-01. It has received 145 citations till now. The article focuses on the topics: Orthomyxoviridae & Neuraminidase.read more
Citations
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Journal ArticleDOI
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 anti-influenza activity.
C U Kim,W. Lew,M.A. Williams,Hua-Kun Liu,Lijun Zhang,S Swaminathan,N Bischofberger,Min Chen,D. B. Mendel,C. Y. Tai,W. G. Laver,Raymond C. Stevens +11 more
TL;DR: 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.
Journal ArticleDOI
Three-dimensional structure of a complex of antibody with influenza virus neuraminidase.
Peter M. Colman,W. G. Laver,Joseph N. Varghese,A. T. Baker,P.A. Tulloch,Gillian M. Air,R. G. Webster +6 more
TL;DR: The structure of a complex between influenza virus neuraminidase and an antibody displays features inconsistent with the inflexible 'lock and key' model of antigen‐antibody binding.
BookDOI
Biology of the sialic acids
TL;DR: Sialic Acid as Receptor Determinant of Ortho and Paramyxoviruses and the role of Gangliosides in Transmembrane Signaling and Cell Recognition is investigated.
Journal ArticleDOI
Is the gene pool of influenza viruses in shorebirds and gulls different from that in wild ducks
TL;DR: Evidence is presented for a second major gene pool of influenza A viruses in nature in nature and the hemagglutinin subtypes that are prevalent in wild ducks were rare or absent in shorebirds and gulls.
Journal ArticleDOI
Structure−Activity Relationship Studies of Novel Carbocyclic Influenza Neuraminidase Inhibitors
Choung U. Kim,W. Lew,M.A. Williams,Huiwei Wu,Lijun Zhang,Xiaowu Chen,Paul A. Escarpe,D. B. Mendel,W. G. Laver,Raymond C. Stevens +9 more
TL;DR: From the extensive structure-activity relationship investigation reported in this article, GS 4071 emerged as one of the most potent influenza neuraminidase inhibitors against both influenza A and B strains.
References
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Journal ArticleDOI
Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus.
TL;DR: The results indicate that the small glycoprotein of paramyxoviruses is biologically active and is involved in virus-induced hemolysis, cell fusion, and the initiation of infection, and provides a biochemical basis for previously observed host-dependent variation in infectivity, and in hemolyzing and cell-fusion induced by paramyxviruses.
Journal ArticleDOI
Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
TL;DR: 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.
Journal ArticleDOI
Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.
TL;DR: The results suggest that the lack of hemagglutinating activity of mutant virus grown at 39.5° is a consequence of the formation of aggregates of virus particles carrying neuraminic acid on their surface, and that the ts defect is in the neuraminidase but not the hemagGLutinin molecule.
Journal ArticleDOI
Structure of the catalytic and antigenic sites in influenza virus neuraminidase
TL;DR: 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, and determinants form a nearly-continuous surface across the top of the monomer encircling the catalytic site.
Journal ArticleDOI
Disquisitions on original antigenic sin : i. evidence in man
TL;DR: The basic difference between primary and secondary reactivity rests on the presence of a trapping mechanism that allows anamnestic production of antibody against lower doses of the homologous antigen, thus preventing a standard primary response and allowing manifestations of Original Antigenic Sin.
Related Papers (5)
Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.
Structure of the catalytic and antigenic sites in influenza virus neuraminidase
Rational design of potent sialidase-based inhibitors of influenza virus replication.
Mark von Itzstein,Wen-Yang Wu,Gaik B. Kok,Michael S. Pegg,Jeffrey Clifford Dyason,Betty Jin,Tho Van Phan,Mark L. Smythe,Hume Forrest White,Hume Forrest White,Stuart W. Oliver,Peter M. Colman,Joseph N. Varghese,D. Michael Ryan,Jacqueline M. Woods,Richard C. Bethell,Vanessa J. Hotham,Janet M. Cameron,Charles R. Penn +18 more