Surface exposure and protease insensitivity of Borrelia burgdorferi Erp (OspEF-related) lipoproteins.
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.
Department of Microbiology and Immunology, University of Kentucky College of Medicine, MS 415 Chandler Medical Center, Lexington, KY 40536-0298, USA1.
Nazira
N
El-Hage
Department of Microbiology and Immunology, University of Kentucky College of Medicine, MS 415 Chandler Medical Center, Lexington, KY 40536-0298, USA1.
Kelly
K
Babb
Microscopy Branch, Rocky Mountain Laboratories, NIAID, National Institutes of Health, 903 South 4th St, Hamilton, MT 59840, USA2.
James A
JA
Carroll
Microscopy Branch, Rocky Mountain Laboratories, NIAID, National Institutes of Health, 903 South 4th St, Hamilton, MT 59840, USA2.
Nicole
N
Lindstrom
Microscopy Branch, Rocky Mountain Laboratories, NIAID, National Institutes of Health, 903 South 4th St, Hamilton, MT 59840, USA2.
Elizabeth R
ER
Fischer
Department of Microbiology and Immunology, University of Kentucky College of Medicine, MS 415 Chandler Medical Center, Lexington, KY 40536-0298, USA1.
Jennifer C
JC
Miller
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, USA3.
Robert D
RD
Gilmore
Department of Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523-1671, USA4.
M Lamine
ML
Mbow
Department of Microbiology and Immunology, University of Kentucky College of Medicine, MS 415 Chandler Medical Center, Lexington, KY 40536-0298, USA1.
Brian
B
Stevenson
D000818:Animals; D000942:Antigens, Bacterial / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001426:Bacterial Proteins / Q000276:immunology / Q000378:metabolism*; D015748:Borrelia burgdorferi Group / Q000254:growth & development / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D007106:Immune Sera / Q000096:biosynthesis / Q000494:pharmacology; D015151:Immunoblotting; D007150:Immunohistochemistry; D008074:Lipoproteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; C096737:ERP protein, Mycobacterium tuberculosis; D007106:Immune Sera; D008074:Lipoproteins; D008565:Membrane Proteins; C084998:OspE protein, Borrelia burgdorferi; C084999:OspF protein, Borrelia burgdorferi; D019286:Endopeptidase K