Neuraminidase Inhibitors
Neuraminidase Inhibitors - 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.
01:52
Eukaryotic Transcription Inhibitors
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2020
Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells. Eukaryotic transcription inhibitors usually contain two distinct domains, a DNA...
FAQs
The active site is the critical binding region where neuraminidase normally acts on sialic acid residues attached to cell-surface glycoproteins. When an inhibitor occupies this site, cleavage is blocked. This prevents newly formed viral particles from being released efficiently from infected cells, interrupting a key stage of viral replication and reducing the opportunity for infection to spread.
Blocking cleavage changes what happens after new influenza particles form inside an infected cell. Without neuraminidase activity, those particles cannot be released normally from the cell surface. As a result, viral dissemination is restricted, limiting the progression of infection from already infected cells toward neighboring cells and showing why this enzyme is an important biological target.
Oseltamivir and zanamivir are named examples of neuraminidase inhibitors used in influenza treatment and prevention. Their activity provides practical evidence that interfering with the enzyme can affect viral spread. Studying these drugs also supports investigation of how inhibitor binding, dosing, and antiviral effectiveness relate to influenza biology and the development of improved therapies.
Neuraminidase links a viral enzyme mechanism to a measurable infection outcome: the release of newly formed influenza particles. Inhibiting that activity allows researchers to examine how one molecular process influences viral dissemination. This makes the enzyme useful for connecting molecular biology, antiviral drug action, drug resistance, and efforts to address emerging influenza strains.
These inhibitors are used for two broad purposes identified in the source material: treating influenza and preventing it. In both contexts, their relevance comes from reducing the viral release step that supports spread. The treatment and prevention roles make the compounds useful not only as medicines but also as tools for examining how antiviral intervention changes infection biology.
Research with these compounds can clarify several connected questions, including how neuraminidase activity supports viral replication, how drug resistance affects antiviral performance, and how dosing relates to treatment or prevention. Such studies also inform the development of improved therapies, particularly when researchers are addressing emerging influenza strains with potentially different biological characteristics.