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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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.
Components of...
Leaky Scanning02:28

Leaky Scanning

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 stands for...
Proteoglycans01:05

Proteoglycans

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,...
Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...

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Glycosylation modulates arenavirus glycoprotein expression and function.

Cyrille J Bonhomme1, Althea A Capul, Elvin J Lauron

  • 1University of California, Irvine, Department of Molecular Biology and Biochemistry & Division of Infectious Disease, 3205 McGaugh Hall, Irvine, CA 92697-3900, USA. cbonhomm@uci.edu

Virology
|November 9, 2010
PubMed
Summary

Investigating N-linked glycosylation of lymphocytic choriomeningitis virus (LCMV) glycoprotein revealed its crucial role in viral fusion and infectivity. Specific N-glycans are essential for glycoprotein expression, cleavage, and cell fusion, impacting viral particle infectivity.

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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
10:32

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

Published on: May 29, 2016

Area of Science:

  • Virology
  • Glycobiology
  • Molecular Biology

Background:

  • The glycoprotein (GP) of lymphocytic choriomeningitis virus (LCMV) plays a critical role in viral entry and pathogenesis.
  • LCMV GP possesses nine potential N-linked glycosylation sites, but their functional significance remains largely unexplored.

Purpose of the Study:

  • To elucidate the functional roles of N-linked glycosylation sites on LCMV GP in viral processes.
  • To determine the impact of specific N-glycans on GP expression, processing, cell fusion, and virus-like particle (VLP) infectivity.

Main Methods:

  • Alanine-scanning mutagenesis was employed to systematically mutate potential N-glycosylation sites on LCMV GP.
  • Expression, cleavage, and cell-surface localization of mutant GPs were assessed.
  • GP-mediated cell-cell fusion assays were performed.
  • Infectivity of VLPs bearing mutant GPs was evaluated.
  • The role of N-glycans in masking neutralizing epitopes was investigated.

Main Results:

  • All available N-linked glycosylation sites on GP1 and two of three on GP2 were occupied.
  • Mutations at GP1 positions 87 and 97 reduced expression, abolished cleavage, and abrogated GP-mediated fusion.
  • Mutants T234A and E379N/A381T impaired cell fusion without affecting expression or processing.
  • Viral infectivity mediated by VLPs necessitated the presence of glycans and a cleaved glycoprotein.
  • An unutilized glycosylation site on GP2 enhanced VLP infectivity.
  • N-linked glycan at position 173 was confirmed to mask the neutralizing epitope GP-1D.

Conclusions:

  • N-linked glycosylation is essential for LCMV glycoprotein function, mediating viral fusion and infectivity.
  • Specific N-glycans on GP1 are critical for proper expression, cleavage, and fusion activity.
  • Glycosylation patterns influence VLP infectivity, with potential for novel therapeutic strategies.
  • N-glycans play a dual role in facilitating viral entry and evading host immune responses.