Viral Glycoproteins
Viral Glycoproteins - Related Videos
08:29
Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo
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Cited by 23 •
2014
An approach is presented for determining structures of viral membrane glycoprotein complexes using a combination of electron cryo-tomography and sub-tomogram averaging with the computational package Jsubtomo.
05:42
Using a Sandwich ELISA to Determine the Immunogenic Glycoprotein Content in a Vaccine
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2025
This video showcases an indirect enzyme-linked immunosorbent assay or ELISA sandwich immunocapture assay designed to assess immunogenic glycoprotein levels in vaccines. The assay plate, containing glycoprotein-specific antibodies, is incubated with serially diluted vaccine samples, including reference and test vaccines, followed by immunoassay to quantify glycoprotein content in the test vaccine.
02:47
A Viral Attachment Assay for Screening of Antiviral Compounds
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2025
This video demonstrates a viral attachment assay for screening antiviral compounds. Using genetically modified hepatitis C virus and luciferase, it assesses inhibitory effects on viral attachment, as indicated by lower light intensity in co-treated wells compared to wells treated with the virus alone.
03:59
Isolation and Purification of Recombinant Myelin Oligodendrocyte Glycoproteins
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2025
Source: Jain, R. W., et al. Simple and Efficient Production and Purification of Mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis Studies. J. Vis. Exp. (2016)This video demonstrates the isolation and purification of MOGtag, a recombinant Myelin Oligodendrocyte Glycoprotein (MOG) used in Experimental Autoimmune Encephalomyelitis (EAE) studies. The protocol involves bacterial lysis, sonication, centrifugation, and nickel affinity chromatography to obtain...
01:21
Matrix Proteoglycans and Glycoproteins
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2023
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
FAQs
Surface glycans can alter viral attachment and entry by changing how a glycoprotein engages a host-cell receptor and participates in membrane fusion. They also affect immune recognition, so the same protein architecture may present different antigenic features as carbohydrate patterns change. This makes glycan arrangement relevant to both infectivity-related interactions and the design of molecules that block them.
Host-cell biosynthetic pathways provide the compartments where viral glycoproteins fold and mature before functioning at the viral surface. The endoplasmic reticulum and Golgi apparatus therefore influence the final biochemical state of these proteins, including features that affect receptor binding, fusion activity, and immune recognition. Studying this maturation helps connect cellular processing with viral entry mechanisms.
Changes in surface carbohydrate patterns can modify which regions of a viral glycoprotein are accessible to immune recognition. As a result, glycan variation may influence the antigenic features presented to the host without requiring a completely different protein framework. This relationship is important when examining how viral surface molecules interact with neutralizing antibodies and when developing vaccine strategies.
Structural studies can reveal how viral glycoproteins present sites involved in receptor binding, membrane fusion, and recognition by neutralizing antibodies. They also help researchers examine how carbohydrate modification contributes to antigenic variation. This information provides a molecular basis for investigating host-pathogen interactions and for identifying protein features suitable for diagnostic or inhibitory approaches.
Their roles in receptor binding, membrane fusion, and immune recognition make viral glycoproteins important targets for vaccine and antiviral development. Researchers can focus on structural features that are recognized by neutralizing antibodies or that support viral entry. Such work connects molecular analysis of the viral surface with efforts to prevent infection or interfere with essential virus-host interactions.
Viral glycoprotein structures can serve as targets in diagnostic assays, allowing research tools to focus on characteristic viral surface features. They can also be incorporated into engineered protein-based systems for investigating host-pathogen interactions. These applications extend biochemical analysis beyond viral entry, supporting controlled studies of recognition, antigenicity, and the molecular contacts that shape infection-related processes.