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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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G Protein-coupled Receptors01:15

G Protein-coupled Receptors

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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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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...
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The SARS-CoV-2 Spike Protein Receptor-Binding Domain Expressed in Rice Callus Features a Homogeneous Mix of

Guillermo Sobrino-Mengual1, Victoria Armario-Nájera1, Juliette Balieu2

  • 1Department of Agricultural and Forest Sciences and Engineering, University of Lleida, Agrotecnio CERCA Center, 25003 Lleida, Spain.

International Journal of Molecular Sciences
|April 27, 2024
PubMed
Summary

Rice callus produces a SARS-CoV-2 spike protein receptor-binding domain (RBD) with specific N-glycan structures. This glycosylation profile differs from other hosts, impacting its potential for vaccines and diagnostics.

Keywords:
SARS-CoV-2biologicsglycan profileplant molecular farmingreceptor-binding domainspike protein

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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Virology

Background:

  • The SARS-CoV-2 spike protein receptor-binding domain (RBD) is crucial for viral entry and a key target for vaccines and diagnostics.
  • Plant-based expression systems are explored for large-scale RBD production due to high demand.
  • Understanding N-glycan structures on RBD is essential for evaluating its efficacy and functionality.

Purpose of the Study:

  • To analyze the N-glycan profile of RBD produced in rice callus.
  • To compare the glycosylation of RBD from rice callus with that from other expression hosts.
  • To identify plant platforms yielding RBDs with optimal N-glycan structures for specific applications.

Main Methods:

  • Expression of SARS-CoV-2 RBD in rice callus.
  • Analysis of N-glycan structures using mass spectrometry.
  • Comparison of glycosylation profiles across different plant expression systems.

Main Results:

  • One of the two potential N-glycan acceptor sites on RBD was not utilized in rice callus.
  • The utilized N-glycan site contained a mixture of complex-type N-glycans.
  • The N-glycan profile in rice callus differed significantly from that observed in other hosts like Nicotiana benthamiana.

Conclusions:

  • Rice callus can produce SARS-CoV-2 RBD with a distinct N-glycan profile.
  • The observed glycosylation pattern in rice callus is less heterogeneous compared to other plant hosts.
  • Comparative analysis of glycosylation facilitates selection of optimal plant platforms for RBD production tailored to vaccine or diagnostic needs.