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Related Concept Videos

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...
Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
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,...
Antifungal Agents01:15

Antifungal Agents

Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to cholesterol contributes to...
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.
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Automated Measurement of Cryptococcal Species Polysaccharide Capsule and Cell Body
08:08

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Published on: January 11, 2018

Allergen1 regulates polysaccharide structure in Cryptococcus neoformans.

Neena Jain1, Radames J B Cordero, Arturo Casadevall

  • 1Department of Microbiology and Immunology, Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Molecular Microbiology
|April 10, 2013
PubMed
Summary

The Allergen 1 (ALL1) gene influences Cryptococcus neoformans virulence by altering fungal polysaccharide structure and iron regulation. Deleting ALL1 results in shorter, less branched polysaccharides with anti-phagocytic properties.

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Area of Science:

  • Mycology
  • Immunology
  • Biochemistry

Background:

  • Cryptococcus neoformans is a fungal pathogen that releases polysaccharide (exo-PS) into host tissues, contributing to adverse effects like increased intracranial pressure (ICP).
  • Downregulation of the Allergen 1 (ALL1) gene correlates with high ICP, but its role in exo-PS regulation is unclear.

Purpose of the Study:

  • To investigate the relationship between ALL1 gene expression and the structural characteristics of C. neoformans exo-PS.
  • To elucidate the role of ALL1 in fungal iron homeostasis and its impact on virulence.

Main Methods:

  • Biophysical techniques were employed to analyze exo-PS structure in wild-type and Δall1 mutant strains.
  • Comparative transcriptome analysis under iron-deprived conditions was performed.
  • Phagocytosis resistance assays were conducted.

Main Results:

  • Δall1 mutants produced shorter, less branched, and structurally simpler exo-PS with higher intrinsic viscosity compared to parental strains.
  • Mutant strains exhibited altered epitope expression and significant resistance to phagocytosis.
  • ALL1 plays a role in iron homeostasis, regulating genes involved in iron reduction and transport.

Conclusions:

  • ALL1 regulates the conformational structure of C. neoformans polysaccharide and influences iron homeostasis.
  • Structural modifications and polymer length of exo-PS are epigenetically regulated, providing a mechanism for ALL1's influence on virulence.