Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins

• Published in: Microbiology (Society for General Microbiology) 2001-04, Vol.147 (4), p.821-830
• Main Authors: El-Hage, Nazira, Babb, Kelly, Carroll, James A, Lindstrom, Nicole, Fischer, Elizabeth R, Miller, Jennifer C, Gilmore, Robert D., Jr, Mbow, M. Lamine, Stevenson, Brian
• Format: Article
• Language: English
• Subjects: Animals; Antigens, Bacterial - metabolism; Bacterial Outer Membrane Proteins - metabolism; Bacterial Proteins - immunology; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; Borrelia burgdorferi; Borrelia burgdorferi Group - growth & development; Borrelia burgdorferi Group - metabolism; Electrophoresis, Polyacrylamide Gel; Endopeptidase K - metabolism; Erp protein; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Immune Sera - biosynthesis; Immune Sera - pharmacology; Immunoblotting; Immunohistochemistry; Lipoproteins - metabolism; Membrane Proteins - immunology; Membrane Proteins - metabolism; Mice; Mice, Inbred BALB C; Microbiology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/00221287-147-4-821

Department of Microbiology and Immunology, University of Kentucky College of Medicine, MS 415 Chandler Medical Center, Lexington, KY 40536-0298, USA 1 Microscopy Branch, Rocky Mountain Laboratories, NIAID, National Institutes of Health, 903 South 4th St, Hamilton, MT 59840, USA 2 Division of Vector-Borne Infectious Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, PO Box 2087, Foothills Campus, Fort Collins, CO 80522, USA 3 Department of Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523-1671, USA 4 Author for correspondence: Brian Stevenson. Tel: [phone]. Fax: [phone]. e-mail: bstev0{at}pop.uky.edu Borrelia burgdorferi can encode numerous lipoproteins of the Erp family. Although initially described as outer surface proteins, the technique used in that earlier study has since been demonstrated to disrupt bacterial membranes and allow labelling of subsurface proteins. Data are now presented from additional analyses indicating that Erp proteins are indeed surface exposed in the outer membrane. Surface localization of these infection-associated proteins indicates the potential for interactions of Erp proteins with vertebrate tissues. Some Erp proteins were resistant to in situ digestion by certain proteases, suggesting that those proteins fold in manners which hide protease cleavage sites, or that they interact with other protective membrane components. Additionally, cultivation of B. burgdorferi in the presence of antibodies directed against Erp proteins inhibited bacterial growth. Keywords: spirochaete, immunofluourescence, Erp proteins, bacterial surface proteins, protease resistance, Lyme disease Abbreviations: IFA, immunofluorescent antibody a Present address: Dept. of Molecular Biology, University of Wyoming, Laramie, WY 82071, USA. b Present address: Centocor Inc., 200 Great Valley Parkway, Malvern, PA 19355, USA.