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Related Concept Videos

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.
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Related Experiment Video

Updated: Sep 21, 2025

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity
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Structural Insight into Terminal Galactose Recognition by Two Non-HBGA Binding GI.3 Noroviruses.

Chenlong Wang1,2,3, Huiling Kang1,2,4, Ming Tan5,6

  • 1National Laboratory of Biomacromolecules, Institute of Biophysicsgrid.418856.6, Chinese Academy of Sciences, Beijing, China.

Journal of Virology
|June 6, 2022
PubMed
Summary
This summary is machine-generated.

Human noroviruses (huNoVs) that don't bind histo-blood group antigens (HBGAs) instead recognize terminal galactose glycans. This discovery explains their infection mechanism and aids in developing antiviral strategies.

Keywords:
ELISAHBGAMSTP proteincapsidcomplexcrystallographynorovirus

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Area of Science:

  • Virology and Glycobiology
  • Structural Biology
  • Infectious Diseases

Background:

  • Human noroviruses (huNoVs) are a leading cause of epidemic acute gastroenteritis globally.
  • Most huNoVs utilize histo-blood group antigens (HBGAs) as host receptors, but some strains, like GI.3 DSV and VA115, do not.
  • The receptor-binding mechanism for HBGA-negative huNoVs has remained unclear, limiting understanding of their pathogenesis and spread.

Purpose of the Study:

  • To elucidate the molecular mechanism of host receptor recognition for HBGA-negative human norovirus strains GI.3 DSV and VA115.
  • To identify the specific glycan ligands bound by these norovirus strains.
  • To provide structural insights into the interaction between norovirus proteins and their identified glycan receptors.

Main Methods:

  • Glycan array analysis to screen for binding interactions between norovirus P domain proteins and various oligosaccharides.
  • X-ray crystallography to determine the high-resolution structures of DSV/VA115 P proteins in complex with specific glycan ligands.
  • Identification of key amino acids involved in the glycan-binding interface through structural analysis.

Main Results:

  • Both GI.3 DSV and VA115 norovirus P domain proteins demonstrated specific binding to oligosaccharides containing terminal galactoses.
  • Crystal structures revealed that the terminal galactose moiety is the primary recognized saccharide by these viral proteins.
  • The findings highlight a conserved galactose-binding site within GI noroviruses, enabling interaction with non-HBGA glycans.

Conclusions:

  • Human norovirus strains GI.3 DSV and VA115 infect hosts by recognizing non-histo-blood group antigen glycans with terminal galactoses.
  • This interaction mechanism explains the inability of these strains to bind HBGAs and sheds light on norovirus host adaptation.
  • The identified glycan-binding mechanism provides a basis for developing novel strategies for norovirus control, prevention, and antiviral therapies.