Differential Binding of Host Complement Inhibitor Factor H by Borrelia burgdorferi Erp Surface Proteins: a Possible Mechanism Underlying the Expansive Host Range of Lyme Disease Spirochetes
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| Published in: | Infection and Immunity Vol. 70; no. 2; pp. 491 - 497 |
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| AbstractList | The Lyme disease spirochete, Borrelia burgdorferi, is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi possesses the ability to contravene the immune defenses of many potential hosts. B. burgdorferi produces multiple different Erp proteins on its outer membrane during mammalian infection. It was reported previously that one Erp protein can bind human factor H (J. Hellwage, T. Meri, T. Heikkilä, A. Alitalo, J. Panelius, P. Lahdenne, I. J. T. Seppälä, and S. Meri, J. Biol. Chem. 276:8427-8435, 2001). In this paper we report that the ability to bind the complement inhibitor factor H is a general characteristic of Erp proteins. Furthermore, each Erp protein exhibits different relative affinities for the complement inhibitors of various potential animal hosts. The data suggest that the presence of multiple Erp proteins on the surface can allow a single B. burgdorferi bacterium to resist complement-mediated killing in any of the wide range of potential hosts that it might infect. Thus, Erp proteins likely contribute to the persistence of B. burgdorferi in nature and to the ability of this bacterium to cause Lyme disease in humans and other animals. The Lyme disease spirochete, Borrelia burgdorferi, is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi possesses the ability to contravene the immune defenses of many potential hosts. B. burgdorferi produces multiple different Erp proteins on its outer membrane during mammalian infection. It was reported previously that one Erp protein can bind human factor H (J. Hellwage, T. Meri, T. Heikkilae, A. Alitalo, J. Panelius, P. Lahdenne, I. J. T. Seppaelae, and S. Meri, J. Biol. Chem. 276:8427 8435, 2001). In this paper we report that the ability to bind the complement inhibitor factor H is a general characteristic of Erp proteins. Furthermore, each Erp protein exhibits different relative affinities for the complement inhibitors of various potential animal hosts. The data suggest that the presence of multiple Erp proteins on the surface can allow a single B. burgdorferi bacterium to resist complement-mediated killing in any of the wide range of potential hosts that it might infect. Thus, Erp proteins likely contribute to the persistence of B. burgdorferi in nature and to the ability of this bacterium to cause Lyme disease in humans and other animals. The Lyme disease spirochete, Borrelia burgdorferi , is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi possesses the ability to contravene the immune defenses of many potential hosts. B. burgdorferi produces multiple different Erp proteins on its outer membrane during mammalian infection. It was reported previously that one Erp protein can bind human factor H (J. Hellwage, T. Meri, T. Heikkilä, A. Alitalo, J. Panelius, P. Lahdenne, I. J. T. Seppälä, and S. Meri, J. Biol. Chem. 276:8427–8435, 2001). In this paper we report that the ability to bind the complement inhibitor factor H is a general characteristic of Erp proteins. Furthermore, each Erp protein exhibits different relative affinities for the complement inhibitors of various potential animal hosts. The data suggest that the presence of multiple Erp proteins on the surface can allow a single B. burgdorferi bacterium to resist complement-mediated killing in any of the wide range of potential hosts that it might infect. Thus, Erp proteins likely contribute to the persistence of B. burgdorferi in nature and to the ability of this bacterium to cause Lyme disease in humans and other animals. The Lyme disease spirochete, Borrelia burgdorferi , is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi possesses the ability to contravene the immune defenses of many potential hosts. B. burgdorferi produces multiple different Erp proteins on its outer membrane during mammalian infection. It was reported previously that one Erp protein can bind human factor H (J. Hellwage, T. Meri, T. Heikkilä, A. Alitalo, J. Panelius, P. Lahdenne, I. J. T. Seppälä, and S. Meri, J. Biol. Chem. 276:8427–8435, 2001). In this paper we report that the ability to bind the complement inhibitor factor H is a general characteristic of Erp proteins. Furthermore, each Erp protein exhibits different relative affinities for the complement inhibitors of various potential animal hosts. The data suggest that the presence of multiple Erp proteins on the surface can allow a single B. burgdorferi bacterium to resist complement-mediated killing in any of the wide range of potential hosts that it might infect. Thus, Erp proteins likely contribute to the persistence of B. burgdorferi in nature and to the ability of this bacterium to cause Lyme disease in humans and other animals. Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue IAI About IAI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy Connect to IAI IAI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0019-9567 Online ISSN: 1098-5522 Copyright © 2014 by the American Society for Microbiology. For an alternate route to IAI .asm.org, visit: IAI |
| Author | Jennifer C. Miller Kelly Babb Nazira El-Hage Melissa A. Hines Brian Stevenson |
| AuthorAffiliation | Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298 |
| AuthorAffiliation_xml | – name: Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298 |
| Author_xml | – sequence: 1 givenname: Brian surname: STEVENSON fullname: STEVENSON, Brian organization: Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298, United States – sequence: 2 givenname: Nazira surname: EL-HAGE fullname: EL-HAGE, Nazira organization: Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298, United States – sequence: 3 givenname: Melissa A surname: HINES fullname: HINES, Melissa A organization: Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298, United States – sequence: 4 givenname: Jennifer C surname: MILLER fullname: MILLER, Jennifer C organization: Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298, United States – sequence: 5 givenname: Kelly surname: BABB fullname: BABB, Kelly organization: Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298, United States |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13452269$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/11796574$$D View this record in MEDLINE/PubMed |
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| Keywords | Human Lyme disease Borrelia burgdorferi Membrane protein Spirochaetaceae Spirochaetales Borrelia infection Host agent relation Complement External membrane Infection Vertebrata Mammalia Spirochaetosis Bacteriosis Bacteria |
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| Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Department of Microbiology and Immunology, University of Kentucky College of Medicine, MS 415 Chandler Medical Center, Lexington, KY 40536-0298. Phone: (859) 257-9358. Fax: (859) 257-8994. E-mail: bstev0@uky.edu. Editor: D. L. Burns |
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| PublicationTitle | Infection and Immunity |
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Reddit... The Lyme disease spirochete, Borrelia burgdorferi, is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi... The Lyme disease spirochete, Borrelia burgdorferi , is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi... |
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| SubjectTerms | Animals Antigens, Bacterial Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins Bacteriology Biological and medical sciences Borrelia burgdorferi Borrelia burgdorferi - metabolism Cats Cattle Complement Factor H - metabolism Dogs Erp protein Fundamental and applied biological sciences. Psychology Humans Lipoproteins Lyme Disease - microbiology Mice Microbiology Molecular Pathogenesis Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Protein Binding Rabbits Rats Rats, Inbred F344 Ticks - microbiology |
| Title | Differential Binding of Host Complement Inhibitor Factor H by Borrelia burgdorferi Erp Surface Proteins: a Possible Mechanism Underlying the Expansive Host Range of Lyme Disease Spirochetes |
| URI | http://iai.asm.org/content/70/2/491.abstract https://www.ncbi.nlm.nih.gov/pubmed/11796574 https://search.proquest.com/docview/18230423 https://search.proquest.com/docview/71404992 https://pubmed.ncbi.nlm.nih.gov/PMC127719 |
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