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LOCALIZATION and PARTIAL IMMUNOLOGICAL CHARACTERIZATION of Fasciola Hepatica THIOREDOXIN

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LOCALIZATION and PARTIAL IMMUNOLOGICAL CHARACTERIZATION of Fasciola Hepatica THIOREDOXIN LOCALIZATION AND PARTIAL IMMUNOLOGICAL CHARACTERIZATION OF Fasciola hepatica THIOREDOXIN A Dissertation by RICHARD DWAYNE MCKOWN Submitted to the Office of Graduate Studies of Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY December 2004 Major Subject: Veterinary Microbiology LOCALIZATION AND PARTIAL IMMUNOLOGICAL CHARACTERIZATION OF Fasciola hepatica THIOREDOXIN A Dissertation by RICHARD DWAYNE MCKOWN Submitted to Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Approved as to style and content by: ____________________________ ___________________________ Allison Rice-Ficht Thomas M. Craig (Co-Chair of Committee) (Co-Chair of Committee) ____________________________ ___________________________ Karen F. Snowden Pete D. Teel (Member) (Member) ____________________________ Ann B. Kier (Head of Department) December 2004 Major Subject: Veterinary Microbiology iii ABSTRACT Localization and Partial Immunological Characterization of Fasciola hepatica Thioredoxin. (December 2004) Richard Dwayne McKown, B.S., Kansas State University; D.V.M., Kansas State University; M.S., Kansas State University Co-Chairs of Advisory Committee: Dr. Allison C. Rice-Ficht Dr. Thomas M. Craig This study reports the localization and partial characterization of thioredoxin from the parasitic trematode Fasciola hepatica. Snails (Pseudosuccinia columella) were raised in culture and infected with F. hepatica so that Western blotting and immunohistochemical techniques could be utilized to determine the presence of thioredoxin in different stages of the parasite’s development. The results of these experiments showed that thioredoxin was present in the tegument, gut epithelium, excretory canal epithelium and sperm, of the adult parasite as well as in the tegument and gut of the redia and cercaria intermediate stages. In situ hybridization was used to determine the localization and possible differential mRNA expression of two different F. hepatica thioredoxin isotypes (Fh2020.A and Fh2020.SL) in the adult parasite. The in situ hybridization results showed that both isotypes are expressed in the tegument and gut epithelium. Fh2020.A stains with a greater intensity possibly demonstrating a difference in the amount of expression between the two isotypes. Recombinant F. hepatica thioredoxin expressed in bacteria using the pMAL™ Protein Fusion and Expression System was used to test its affects on the production of super oxide anion by murine peritoneal macrophages, bovine monocyte-derived iv macrophages and bovine whole blood neutrophils, and nitric oxide production by mouse peritoneal macrophages and bovine monocyte-derived macrophages. The results of the cellular assays were not definitive due to the fact that the maltose binding protein (MBP) moiety of the recombinant thioredoxin, when tested alone, increased production of nitric oxide by bovine monocyte-derived macrophages. Consequently, since the MBP could not be effectively separated from the thioredoxin portion of the recombinant, allowing the thioredoxin affects to be tested independently, no true conclusions regarding its affects on the host immune cells tested could be drawn. This is the first report of the localization of thioredoxin in both the adult F. hepatica as well as in specific intermediate stages of the parasite. These studies demonstrate the possible affects that a protein tag can have on experimental results and demonstrate how such data may be interpreted when a non-cleaved recombinant protein is used in cellular or other assays when compared to native or cleaved recombinant proteins. v DEDICATION This dissertation and all the work done to get to this point are due entirely to my family, especially my wife Carol and daughter Genny. Without their support and encouragement over the years this never would have been completed. vi ACKNOWLEDGEMENTS I would like to thank the individuals at Texas A & M University who have provided support, guidance and friendship during my tenure there, particularly the administrative and support staff of the Departments of Veterinary Pathobiology and Medical Biochemistry and Genetics. Additionally, I would like to thank the administration and staff of the U.S. Meat Animal Research Center, and the Great Plains Veterinary Education Center, both in Clay Center, Nebraska for the generous use of their facilities. Much of the work described within this dissertation would have been much more difficult to achieve without the assistance of the technical, support, and secretarial staffs at both of these facilities – for their unselfish help and good humor, I am deeply indebted. Finally, I owe immeasurable thanks to Dr. Judy Ball for all of the effort and stress she dedicated to helping a graduate student she basically didn’t know, but fought for anyway. May you be truly blessed! vii TABLE OF CONTENTS Page ABSTRACT.................................................................................................................. iii DEDICATION.............................................................................................................. v ACKNOWLEDGEMENTS ......................................................................................... vi TABLE OF CONTENTS.............................................................................................. vii LIST OF FIGURES ...................................................................................................... xi LIST OF TABLES........................................................................................................ xiv CHAPTER I INTRODUCTION AND LITERATURE REVIEW ............................ 1 History....................................................................................... 3 Description................................................................................ 4 Life Cycle.................................................................................. 4 Tegument .................................................................................. 7 Veterinary Importance .............................................................. 9 Medical Importance .................................................................. 12 Protein Biochemistry ................................................................ 14 II MATERIALS AND METHODS.......................................................... 21 Fasciola hepatica Adult and Intermediate Stage Collection .... 21 Adult Flukes and Eggs.................................................. 21 Miracidia....................................................................... 22 Snail Culture ................................................................. 23 Snail Infection............................................................... 24 Sporocysts..................................................................... 25 Redia ............................................................................. 26 Cercaria......................................................................... 26 Metacercaria.................................................................. 27 Mouse Infection............................................................ 27 Juvenile Flukes.............................................................. 28 Parasite Soluble Protein Preparation and Analysis................... 28 Preparation of Parasite Soluble Protein ........................ 28 Determination of Protein Concentration....................... 29 viii CHAPTER Page Sodium Dodecyl Sulfate – PolyacrylamideGel Electrophoresis (SDS-PAGE)........................... 29 Coomassie® Brilliant Blue Staining of Polyacrylamide Gel................................................................................. 30 Polyacrylamide Gel Drying .......................................... 30 Electrophoretic Transfer of Protein from SDS-PAGE to Nitrocellulose............................................................ 31 Protein Immunodetection.......................................................... 32 Western Blotting ........................................................... 32 Sample Handling for Immunohistochemistry........................... 33 Fixation of Tissues........................................................ 33 Processing and Embedding of Tissues.......................... 33 Sialanization of Glass Slides......................................... 34 Immunohistochemistry ............................................................. 34 Protein Localization...................................................... 34 In situ Hybridization ................................................................. 36 Preparation of Reagents and Glassware........................ 36 Parasite Preparation and Fixation ................................. 36 Processing and Embedding........................................... 36 Design of Oligonucleotide Probes ................................ 36 Digoxigenin Tailing of Probes...................................... 37 Dot Blot......................................................................... 38 Calculation of Hybridization Temperature ................... 38 In situ Hybridization Protocol....................................... 39 Immune Cell Collection and Isolation ...................................... 40 Murine Peritoneal Macrophages................................... 40 Bovine Monocyte-Derived Macrophages..................... 42 Bovine Whole Blood Neutrophils................................. 43 Cytospin Preparation
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