Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D [PDF]
Respiratory Research, 2008 Surfactant protein D (SP-D) plays an important role in innate defense against influenza A viruses (IAVs) and other pathogens.We tested antiviral activities of recombinant human SP-D against a panel of IAV strains that vary in glycosylation sites on their hemagglutinin (HA).
Hartshorn, Kevan L +8 more
openaire +13 more sources
High-complexity extracellular barcoding using a viral hemagglutinin [PDF]
Proceedings of the National Academy of Sciences, 2020 While single-cell sequencing technologies have revealed tissue heterogeneity, resolving mixed cellular libraries into cellular clones is essential for many pooled screens and clonal lineage tracing. Fluorescent proteins are limited in number, while DNA barcodes can only be read after cell lysis.
Gavriel Mullokandov +7 more
openaire +4 more sources
A simple procedure for purification of viral hemagglutinin [PDF]
Virology, 1962 Peer Reviewed ; http://deepblue.lib.umich.edu/bitstream/2027.42/32311/1/0000379 ...
Mizutani, H. +3 more
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Insight into highly conserved H1 subtype-specific epitopes in influenza virus hemagglutinin [PDF]
, 2014 Influenza viruses continuously undergo antigenic changes with gradual accumulation of mutations in hemagglutinin (HA) that is a major determinant in subtype specificity.
Cho, Ki Joon +7 more
core +8 more sources
Formation of influenza virus particles lacking hemagglutinin on the viral envelope [PDF]
Journal of Virology, 1986 We investigated the intracellular block in the transport of hemagglutinin (HA) and the role of HA in virus particle formation by using temperature-sensitive (ts) mutants (ts134 and ts61S) of influenza virus A/WSN/33. We found that at the nonpermissive temperature (39.5 degrees C), the exit of ts HA from the rough endoplasmic reticulum to the Golgi ...
Pattnaik, Asit K. +2 more
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Polymer-stabilized sialylated nanoparticles : synthesis, optimization, and differential binding to influenza hemagglutinins [PDF]
, 2020 During influenza infection, hemagglutinins (HAs) on the viral surface bind to sialic acids on the host cell's surface. While all HAs bind sialic acids, human influenza targets terminal α2,6 sialic acids and avian influenza targets α2,3 sialic acids.
Baker, Alexander +3 more
core +2 more sources
Structural Basis for Influence of Viral Glycans on Ligand Binding by Influenza Hemagglutinin [PDF]
Biophysical Journal, 2008 Binding of cell surface glycans by influenza hemagglutinin controls viral attachment and infection of host cells. This binding is a three-way interaction between viral proteins, host glycans, and viral glycans; many structural details of this interaction have been difficult to resolve.
Peter M. Kasson, Vijay S. Pande
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Recognition of viral hemagglutinins by NKp44 but not by NKp30
European Journal of Immunology, 2001 Natural killer (NK) cells destroy virus-infected and tumor cells without prior antigen stimulation. The NK cell cytotoxicity is regulated in large part by the expression of NK cell receptors that are able to bind major histocompatibility complex (MHC) class I glycoproteins.
Arnon, T +5 more
openaire +4 more sources
Hemagglutinin Spatial Distribution Shifts in Response to Cholesterol in the Influenza Viral Envelope [PDF]
Biophysical Journal, 2015 Influenza virus delivers its genome to the host cytoplasm via a process of membrane fusion mediated by the viral hemagglutinin protein. Optimal fusion likely requires multiple hemagglutinin trimers, so the spatial distribution of hemagglutinin on the viral envelope may influence fusion mechanism.
Mark Yeager +5 more
openaire +3 more sources
Mechanism of glycan receptor recognition and specificity switch for avian, swine, and human adapted influenza virus hemagglutinins: a molecular dynamics perspective. [PDF]
, 2009 Hemagglutinins (HA's) from duck, swine, and human influenza viruses have previously been shown to prefer avian and human glycan receptor analogues with distinct topological profiles, pentasaccharides LSTa (alpha-2,3 linkage) and LSTc (alpha-2,6 linkage),
Alam, Maqsudul +8 more
core +2 more sources