title: Digestion of glycogen by a glucosidase released by Trichomonas vaginalis.
abstract: Trichomonas vaginalis is a protozoan parasite that is the causative agent of trichomoniasis, a widespread sexually transmitted disease. In vitro culture of T. vaginalis typically employs a medium supplemented with either maltose or glucose and carbohydrates are considered essential for growth. Although the nature of the carbohydrates utilized by T. vaginalis in vivo is undefined, the vaginal epithelium is rich in glycogen, which appears to provide a source of carbon for the vaginal microbiota. Here, we show that T. vaginalis grows equally well in growth media supplemented with simple sugars or with glycogen. Analysis of conditioned growth medium by thin layer chromatography indicates that growth on glycogen is accompanied by glycogen breakdown to a mixture of products including maltose, glucose, and oligosaccharides. Enzymatic assays with conditioned growth medium show that glycogen breakdown is accomplished via the release of a glucosidase activity having the properties of an α-amylase into the growth medium. Furthermore, we find that released glucosidase activity increases upon removal of carbohydrate from the growth medium, indicating regulation of synthesis and/or secretion in response to environmental cues. Lastly, we show that addition of T. vaginalis glucosidase activity to a growth medium containing glycogen generates sufficient simple sugar to support the growth of lactobacilli which, themselves, are unable to degrade glycogen. Thus, not only does the glucosidase activity likely play an important role in allowing T. vaginalis to secure simple sugars for its own use, it has the potential to impact the growth of other members of the vaginal microbiome.
authors.affiliation: Department of Microbiology and Immunology, Des Moines University, 3200 Grand Avenue, Des Moines, IA 50312, USA.
authors.forename: Ryan D
authors.initials: RD
authors.lastname: Huffman
authors.affiliation: Department of Microbiology and Immunology, Des Moines University, 3200 Grand Avenue, Des Moines, IA 50312, USA.
authors.forename: Lauren D
authors.initials: LD
authors.lastname: Nawrocki
authors.affiliation: Department of Biochemistry and Nutrition, Des Moines University, 3200 Grand Avenue, Des Moines, IA 50312, USA.
authors.forename: Wayne A
authors.initials: WA
authors.lastname: Wilson
authors.affiliation: Department of Microbiology and Immunology, Des Moines University, 3200 Grand Avenue, Des Moines, IA 50312, USA. Electronic address: andrew.brittingham@dmu.edu.
authors.forename: Andrew
authors.initials: A
authors.lastname: Brittingham
mesh_terms: D000818:Animals; D003470:Culture Media; D005260:Female; D005959:Glucosidases / Q000378:metabolism*; D006003:Glycogen / Q000378:metabolism*; D006736:Horses; D006801:Humans; D007778:Lactobacillus / Q000254:growth & development; D008320:Maltose / Q000378:metabolism; D044967:Serum / Q000201:enzymology; D014246:Trichomonas vaginalis / Q000201:enzymology* / Q000254:growth & development; D014621:Vagina / Q000382:microbiology / Q000469:parasitology; D000516:alpha-Amylases / Q000378:metabolism; D000520:alpha-Glucosidases / Q000378:metabolism
chemical_list: D003470:Culture Media; D008320:Maltose; D006003:Glycogen; D005959:Glucosidases; D000516:alpha-Amylases; D000520:alpha-Glucosidases
keywords: Amylase; Lactobacilli; Polysaccharide