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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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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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Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
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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.
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The human body contains a monogastric digestive system. In a monogastric digestive system, the stomach only contains one chamber in which it digests food. Several other animal species also have monogastric digestive systems, including pigs, horses, dogs, and birds. This chapter, however, focuses on the human digestive system.
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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...
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Glycan processing in gut microbiomes.

Sabina Leanti La Rosa1, Matthew P Ostrowski2, Arturo Vera-Ponce de León3

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Area of Science:

  • Microbiology and Host-Animal Interactions
  • Nutrient Metabolism
  • Gastrointestinal Ecosystems

Background:

  • Microbiomes and their enzymes are vital for processing nutrients in the gastrointestinal tract, impacting host health and nutrition.
  • Gut microbes utilize dietary and host-derived glycans, forming complex interactions within their ecosystems.
  • Recent multi-omic studies offer new perspectives on glycan-dependent microbial interactions.

Purpose of the Study:

  • To review recent insights into nutrient processing by microbiomes in contrasting gastrointestinal ecosystems (humans, ruminants, insects).
  • To focus on bacterial mechanisms for utilizing common, atypical dietary glycans, and host-derived mucus glycans.
  • To highlight how understanding glycan processing can advance microbiome reprogramming for improved host health and growth.

Main Methods:

  • Review of current literature on gut microbiome nutrient processing.
  • Analysis of bacterial mechanisms for glycan utilization.
  • Integration of findings from multi-omic studies.

Main Results:

  • Detailed examination of glycan processing in human, ruminant, and insect gut microbiomes.
  • Elucidation of bacterial strategies for degrading diverse glycan structures.
  • Demonstration of glycan-dependent interactions shaping microbial communities.

Conclusions:

  • Understanding glycan processing by gut microbiomes is key to deciphering host-microbe nutrient exchange.
  • This knowledge is critical for the emerging field of microbiome reprogramming.
  • Leveraging diet to modulate gut microbiomes offers a promising avenue for enhancing animal growth and host well-being.