Publications and Research
Document Type
Poster
Publication Date
Fall 2025
Abstract
Mannosidases are a type of glycoside hydrolase (glycosidase) that facilitate the hydrolysis of glycosidic bonds in mannose-containing polysaccharides and glycans, including those found in glycoproteins. Their main role is to cleave specific linkages involving D-mannose residues, effectively trimming or degrading mannose-rich oligosaccharides. These enzymes are crucial in N-glycosylation pathways, which are essential for proper protein folding, glycoprotein maturation, and the regulation of carbohydrate metabolism in eukaryotic cells.
There are two main types of mannosidases: alpha-mannosidases and beta-mannosidases. In humans, several of these enzymes exist, including those found in the endoplasmic reticulum (alpha-mannosidase I), those in the Golgi apparatus (alpha-mannosidase II), and those in lysosomes (alpha-mannosidase B). Some of these enzymes have been shown to be involved in oxidative stress pathways, which are associated with DNA damage, apoptosis, inflammation, and various diseases. Studies have show that these proteins are vital to many functions in cells including cell development and survival, catabolism and protein quality control. However, very little information is available regarding their precise roles in oxidative stress.
Tetrahymena thermophila has been used as a model organism for studying many biological processes including cell cycle, genetics, and DNA repair. They are also well utilized for toxicity studies because of their stress resistant levels. T. thermophila is a unicellular eukaryotic protozoan that possesses a dual nuclei system, consisting of a germline micronucleus and a somatic macronucleus. The entire genome has been sequenced but annotation of its genes is lacking. One area is yet to be examined is mannosidases. Therefore, this study aims to explore the structural and functional roles of mannosidase in Tetrahymena thermophila by comparing its mannosidases with those in humans and other organisms.
Comments
This poster was presented at the 42nd Semi-Annual Dr. Janet Liou-Mark Honors & Undergraduate Research Poster Presentation, December 4, 2025.
Mentor: Dr. Ralph Alcendor (Biological Sciences Department).