title: Quantitative Proteomics of an Amphibian Pathogen, Batrachochytrium dendrobatidis, following Exposure to Thyroid Hormone.
abstract: Batrachochytrium dendrobatidis (Bd), a chytrid fungus, has increasingly been implicated as a major factor in the worldwide decline of amphibian populations. The fungus causes chytridiomycosis in susceptible species leading to massive die-offs of adult amphibians. Although Bd infects the keratinized mouthparts of tadpoles and negatively affects foraging behavior, these infections are non-lethal. An important morphogen controlling amphibian metamorphosis is thyroid hormone (T3). Tadpoles may be infected with Bd and the fungus may be exposed to T3 during metamorphosis. We hypothesize that exposure of Bd to T3 may induce the expression of factors associated with host colonization and pathogenicity. We utilized a proteomics approach to better understand the dynamics of the Bd-T3 interaction. Using liquid chromatography-mass spectrometry (LC-MS), we generated a data set of a large number of cytoplasmic and membrane proteins following exposure of Bd to T3. From these data, we identified a total of 263 proteins whose expression was significantly changed following T3 exposure. We provide evidence for expression of an array of proteins that may play key roles in both genomic and non-genomic actions of T3 in Bd. Additionally, our proteomics study shows an increase in several proteins including proteases and a class of uncommon crinkler and crinkler-like effector proteins suggesting their importance in Bd pathogenicity as well as those involved in metabolism and energy transfer, protein fate, transport and stress responses. This approach provides insights into the mechanistic basis of the Bd-amphibian interaction following T3 exposure.
authors.affiliation: Department of Internal Medicine, Yale University School of Medicine, New Haven, CT, 06520, United States of America.
authors.forename: Jose
authors.initials: J
authors.lastname: Thekkiniath
authors.affiliation: Center for Biotechnology and Genomics, Texas Tech University, Lubbock, TX, 79402-3132, United States of America.
authors.forename: Masoud
authors.initials: M
authors.lastname: Zabet-Moghaddam
authors.affiliation: Center for Biotechnology and Genomics, Texas Tech University, Lubbock, TX, 79402-3132, United States of America.
authors.forename: Kameswara Rao
authors.initials: KR
authors.lastname: Kottapalli
authors.affiliation: Department of Cell Biology and Pediatrics, Harvard Medical School, Boston, MA, 02115, United States of America, and Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, 02115, United States of America.
authors.forename: Mithun R
authors.initials: MR
authors.lastname: Pasham
authors.affiliation: Center for Biotechnology and Genomics, Texas Tech University, Lubbock, TX, 79402-3132, United States of America; Department of Biological Sciences, Texas Tech University, Lubbock, TX, 79409-3131, United States of America.
authors.forename: Susan
authors.initials: S
authors.lastname: San Francisco
authors.affiliation: Department of Biological Sciences, Texas Tech University, Lubbock, TX, 79409-3131, United States of America.
authors.forename: Michael
authors.initials: M
authors.lastname: San Francisco
mesh_terms: D000818:Animals; D001001:Anura / Q000382:microbiology; D001692:Biological Transport / Q000187:drug effects; D050260:Carbohydrate Metabolism / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D008411:Chytridiomycota / Q000187:drug effects* / Q000302:isolation & purification / Q000378:metabolism; D004586:Electrophoresis; D005656:Fungal Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism; D050356:Lipid Metabolism / Q000187:drug effects; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism; D010455:Peptides / Q000032:analysis; D040901:Proteomics; D053719:Tandem Mass Spectrometry; D014284:Triiodothyronine / Q000494:pharmacology*; D014357:Trypsin / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D010455:Peptides; D014284:Triiodothyronine; D014357:Trypsin