title: Functional insights into recombinant TROSPA protein from Ixodes ricinus.
abstract: Lyme disease (also called borreliosis) is a prevalent chronic disease transmitted by ticks and caused by Borrelia burgdorferi s. l. spirochete. At least one tick protein, namely TROSPA from I. scapularis, commonly occurring in the USA, was shown to be required for colonization of the vector by bacteria. Located in the tick gut, TROSPA interacts with the spirochete outer surface protein A (OspA) and initiates the tick colonization. Ixodes ricinus is a primary vector involved in B. burgdorferi s. l. transmission in most European countries. In this study, we characterized the capacities of recombinant TROSPA protein from I. ricinus to interact with OspA from different Borrelia species and to induce an immune response in animals. We also showed that the N-terminal part of TROSPA (a putative transmembrane domain) is not involved in the interaction with OspA and that reduction of the total negative charge on the TROSPA protein impaired TROSPA-OspA binding. In general, the data presented in this paper indicate that recombinant TROSPA protein retains the capacity to form a complex with OspA and induces a significant level of IgG in orally immunized rats. Thus, I. ricinus TROSPA may be considered a good candidate component for an animal vaccine against Borrelia.
authors.affiliation: Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland ; Institute of Computing Science, Poznan University of Technology, Poznan, Poland.
authors.forename: Marek
authors.initials: M
authors.lastname: Figlerowicz
authors.forename: Anna
authors.initials: A
authors.lastname: Urbanowicz
authors.forename: Dominik
authors.initials: D
authors.lastname: Lewandowski
authors.forename: Jadwiga
authors.initials: J
authors.lastname: Jodynis-Liebert
authors.forename: Czeslaw
authors.initials: C
authors.lastname: Sadowski
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface / Q000276:immunology / Q000378:metabolism; D060829:Arthropod Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D001179:Arthropod Vectors / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D001425:Bacterial Outer Membrane Proteins / Q000276:immunology / Q000378:metabolism; D001428:Bacterial Vaccines / Q000276:immunology / Q000378:metabolism; D001483:Base Sequence; D001898:Borrelia / Q000378:metabolism / Q000502:physiology; D025065:Borrelia burgdorferi / Q000378:metabolism / Q000502:physiology; D004797:Enzyme-Linked Immunosorbent Assay; D007114:Immunization / Q000379:methods; D007074:Immunoglobulin G / Q000097:blood / Q000276:immunology; D018884:Ixodes / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D008074:Lipoproteins / Q000276:immunology / Q000378:metabolism; D008193:Lyme Disease / Q000276:immunology / Q000382:microbiology / Q000635:transmission; D022123:Lyme Disease Vaccines / Q000008:administration & dosage / Q000276:immunology; D008969:Molecular Sequence Data; D009154:Mutation; D059372:Nucleotide Motifs / Q000235:genetics; D011485:Protein Binding; D051381:Rats; D017208:Rats, Wistar; D011994:Recombinant Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid
chemical_list: D000954:Antigens, Surface; D060829:Arthropod Proteins; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D007074:Immunoglobulin G; D008074:Lipoproteins; D022123:Lyme Disease Vaccines; C072045:OspA protein; D011994:Recombinant Proteins