Neuraminidase
Neuraminidase - Related Videos
09:31
Fluorescence-based Neuraminidase Inhibition Assay to Assess the Susceptibility of Influenza Viruses to The Neuraminidase Inhibitor Class of Antivirals
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Cited by 56 •
2017
We describe the use of a phenotypic fluorescence-based neuraminidase inhibition assay to assess the susceptibility of influenza A and B viruses to the neuraminidase inhibitor class of antivirals.
08:11
Measuring Influenza Neuraminidase Inhibition Antibody Titers by Enzyme-linked Lectin Assay
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Cited by 54 •
2016
We describe the enzyme-linked lectin assay (ELLA) for measuring influenza neuraminidase (NA)-inhibition antibody titers in sera. The assay uses peanut agglutinin to quantify galactose residues that become accessible when NA removes sialic acid from fetuin-coated, 96-well plates.
03:19
An Assay to Measure Influenza Neuraminidase Inhibition Antibody Titers
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2025
This video demonstrates an assay measuring influenza neuraminidase (NA) inhibiting antibody titers in a serum sample. A serum sample containing antibodies against NA is added to a fetuin-coated microwell plate. Upon adding the virus, the antibodies prevent viral NA from cleaving fetuin and exposing its galactose moiety. A peroxidase-conjugated lectin is then added, which binds to the exposed galactose. The NA-inhibiting antibody titer is determined using a colorimetric test, where a peroxidase...
12:18
Expression of Functional Recombinant Hemagglutinin and Neuraminidase Proteins from the Novel H7N9 Influenza Virus Using the Baculovirus Expression System
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Cited by 182 •
2013
Here we describe a way to express correctly folded and functional influenza virus surface antigens derived from the novel Chinese H7N9 virus in insect cells. The technique can be adapted to express ectodomains of any viral or cellular surface proteins.
13:12
Quantitative Analyses of all Influenza Type A Viral Hemagglutinins and Neuraminidases using Universal Antibodies in Simple Slot Blot Assays
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Cited by 19 •
2011
A simple slot blot method was developed for the quantification of influenza viral hemagglutinin and neuraminidase using universal antibodies targeting their most conserved sequences identified through bioinformatics analyses. This innovative approach may provide a useful alternative to quantitative determination of all viral hemagglutinin and neuraminidase.
FAQs
Neuraminidase hydrolyzes the α-ketosidic bond joining a terminal sialic acid residue to an underlying sugar. Because the residue lies at the exposed end of glycoprotein or glycolipid carbohydrate chains, removing it can alter how those glycoconjugates participate in cell-surface recognition, turnover, and microbial interactions.
By removing terminal sialic acids, the enzyme changes the carbohydrate features presented at the cell surface. Those altered features can influence recognition between cells or between microbes and host cells, making neuraminidase relevant to both normal biological interactions and host-pathogen studies. The outcome depends on which glycoconjugates are modified.
Influenza neuraminidase cleaves sialic acids from cell-surface glycoconjugates during the release of newly formed virions. This activity helps separate progeny virus particles from the infected cell, linking carbohydrate modification to viral replication and spread. Consequently, neuraminidase function provides an important focus for studying influenza host-pathogen interactions.
These compounds are neuraminidase inhibitors with clinical importance because they can limit influenza virus spread. They provide a focused way to consider how reducing sialic-acid cleavage affects the relationship between viral replication, virion release, and infection. Their relevance connects carbohydrate-processing mechanisms with clinically significant antiviral intervention.
Examining where sialic acid is removed from glycoproteins or glycolipids helps connect enzyme activity with changes in glycoconjugate structure and function. That information supports analysis of cell-surface recognition and glycoprotein turnover, while also showing how carbohydrate-processing enzymes shape interactions between microorganisms and their hosts.
Researchers can compare the biological consequences of neuraminidase function with situations in which its activity is limited by oseltamivir or zanamivir. In this context, reduced viral release helps relate carbohydrate cleavage to influenza replication and provides a basis for evaluating clinically relevant inhibition of a process required for efficient viral spread.