Outer surface proteins E and F of Borrelia burgdorferi, the agent of Lyme disease

• DOI: 10.1128/iai.62.1.290-298.1994
• Publication Date: 2020-01-03T13:30:46Z
• Authors: T T Lam; T P Nguyen; R R Montgomery; F S Kantor; E Fikrig; R A Flavell
• Keywords: 0301 basic medicine; Antigens, Bacterial; Lyme Disease; Base Sequence; Lipoproteins; Blotting, Western; Molecular Sequence Data; Restriction Mapping; Fluorescent Antibody Technique; Regulatory Sequences, Nucleic Acid; Molecular Weight; 03 medical and health sciences; Bacterial Proteins; Borrelia burgdorferi Group; Genes, Bacterial; Operon; Humans; Amino Acid Sequence; Cloning, Molecular; Codon; Sequence Alignment; Bacterial Outer Membrane Proteins

We report the cloning and characterization of two outer surface proteins (Osps), designated OspE OspF, from strain N40 Borrelia burgdorferi, spirochetal agent Lyme disease. The ospE ospF genes are structurally arranged in tandem as one transcriptional unit under control a common promoter. gene, located at 5' end operon, is 513 nucleotides length encodes 171-amino-acid protein with calculated molecular mass 19.2 kDa. 27 bp downstream stop codon consists 690 230 amino acids 26.1 Pulsed-field gel electrophoresis showed that on 45-kb plasmid. Comparison leader sequences OspF those four known B. burgdorferi Osps (OspA, OspB, OspC, OspD) reveals hydrophobic domain consensus cleavage sequence (L-X-Y-C) recognized by signal peptidase II, [3H]palmitate labeling shows lipoproteins. Immunofluorescence studies demonstrated both exposed. These features consistent finding