{"id":72544,"date":"2025-05-07T09:25:00","date_gmt":"2025-05-07T13:25:00","guid":{"rendered":"https:\/\/research.uga.edu\/news\/?p=72544"},"modified":"2025-05-07T09:57:44","modified_gmt":"2025-05-07T13:57:44","slug":"uga-biochemists-create-new-tool-to-study-biological-process-in-parasites","status":"publish","type":"post","link":"https:\/\/research.uga.edu\/news\/uga-biochemists-create-new-tool-to-study-biological-process-in-parasites\/","title":{"rendered":"UGA biochemists create new tool to study biological process in parasites"},"content":{"rendered":"

[vc_row][vc_column][vc_column_text css=””]Researchers in the University of Georgia\u2019s West Laboratory are interested in how unicellular parasites thrive in their environments. Focusing on post-translational modifications of proteins, particularly a crucial process called glycosylation<\/a>, researchers are gaining insights into how this basic life process in parasites can lead to better treatments for diseases.<\/p>\n

Led by Distinguished Research Professor Christopher West, the team focuses on Toxoplasma gondii<\/em>, a parasite that causes a chronic infection known as toxoplasmosis, and Dictyostelium discoideum<\/em>, a soil-dwelling social amoeba commonly known as a cellular slime mold. Dictyostelium<\/em> is an unrelated non-pathogenic model organism with a relatively simple life cycle, making it ideal for laboratory research.<\/p>\n

Their colleagues at Boston University, Giulia Bandini and John Samuelson, discovered that dozens of nuclear and cytoplasmic proteins in Toxoplasma<\/em> are unusually modified by a single sugar called fucose. There were potential parallels with a similar modification of host cell proteins with the key difference being the sugar involved-called GlcNAc, which is important for mediating host cell stress responses.<\/p>\n

\u201cThis unprecedented finding raised new questions after we found that a similar process occurred in Dictyostelium<\/em>,\u201d said West<\/a>, Distinguished Research Professor in Franklin College of Arts and Science\u2019s Department of Biochemistry and Molecular Biology<\/a>.<\/p>\n

When the West lab identified the gene responsible for attaching O-fucose, the door was opened to study its function when it was knocked out in Toxoplasma<\/em> and Dictyostelium<\/em>.<\/p>\n

\u201cThough the cells still lived, both grew more slowly,\u201d said West, a member of the Center for Tropical and Emerging Global Diseases<\/a>. \u201cThe evidence indicated that several important proteins were less abundant, which consequently compromised their activity in cells.\u201d<\/p>\n

O-fucose is difficult to detect through traditional methods, which impedes learning more about its roles. To address this need, Megna Tiwari, a recently graduated biochemistry Ph.D. student in the West Lab, got together with Ron Orlando<\/a> at the Complex Carbohydrate Research Center<\/a> and GlycoScientific LLC to generate antibodies that only bind O-fucose on proteins. Her recent study published in mSphere<\/em><\/a> illustrates the power of these antibodies to find and isolate O-fucose in the cell.<\/p>\n

\u201cRemarkably, dozens of new proteins were found to bear O-fucose and the images indicate that majority of them appear to be enriched at the nuclear periphery, inviting new ideas for O-fucose at this location,\u201d West said.[\/vc_column_text][\/vc_column][\/vc_row]<\/p>\n<\/div>","protected":false},"excerpt":{"rendered":"

[vc_row][vc_column][vc_column_text css=””]Researchers in the University of Georgia\u2019s West Laboratory are interested in how unicellular parasites thrive in their environments. Focusing on post-translational modifications of proteins, particularly a crucial process called glycosylation, researchers are gaining insights into how this basic life process in parasites can lead to better treatments for diseases. Led by Distinguished Research Professor … <\/p>\n

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