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Immunogenicity of Borrelia burgdorferi arthritis-related protein.

ABSTRACT: Immunization against arthritis-related protein (Arp) elicits antibody in mice that resolves arthritis but is not protective against challenge with Borrelia burgdorferi. In mice immunized against Arp, an unrelated 37-kDa protein (P37-42), outer surface protein A (OspA), or glutathione S-transferase (GT) and then challenged by syringe or tick, only OspA conferred protection. Passive transfer of Arp antiserum into infected SCID mice induced arthritis resolution, but antisera to P37-42, OspA, GT, or six overlapping Arp peptide fragments did not. Results suggest that the arthritis-resolving immunogenicity is specific to Arp, but the relevant epitopes may be conformational.

SUBMITTER: Feng S

PROVIDER: S-EPMC308918 | biostudies-literature | 2003 Dec

REPOSITORIES: biostudies-literature

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Immunogenicity of Borrelia burgdorferi arthritis-related protein.

Feng Sunlian S Hodzic Emir E Freet Kimberly K Barthold Stephen W SW

Infection and immunity 20031201 12

Immunization against arthritis-related protein (Arp) elicits antibody in mice that resolves arthritis but is not protective against challenge with Borrelia burgdorferi. In mice immunized against Arp, an unrelated 37-kDa protein (P37-42), outer surface protein A (OspA), or glutathione S-transferase (GT) and then challenged by syringe or tick, only OspA conferred protection. Passive transfer of Arp antiserum into infected SCID mice induced arthritis resolution, but antisera to P37-42, OspA, GT, or ...[more]

PMID: 14638819

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Project description:The bacterial spirochete Borrelia burgdorferi is the causative agent of the most commonly reported arthropod-borne illness in the United States, Lyme disease. A family of proteins containing von Willebrand Factor A (VWFA) domains adjacent to a MoxR AAA+ ATPase have been found to be highly conserved in the genus Borrelia. Previously, a VWFA domain containing protein of B. burgdorferi, BB0172, was determined to be an outer membrane protein capable of binding integrin ?3?1. In this study, the characterization of a new VWFA domain containing membrane protein, BB0173, is evaluated in order to define the location and topology of this multi-spanning membrane protein. In addition, functional predictions are made.Our results show that BB0173, in contrast to BB0172, is an inner membrane protein, in which the VWFA domain is exposed to the periplasmic space. Further, BB0173 was predicted to have an aerotolerance regulator domain, and expression of BB0173 and the surrounding genes was evaluated under aerobic and microaerophilic conditions, revealing that these genes are downregulated under aerobic conditions. Since the VWFA domain containing proteins of B. burgdorferi are highly conserved, they are likely required for survival of the pathogen through sensing diverse environmental oxygen conditions.Presently, the complex mechanisms that B. burgdorferi uses to detect and respond to environmental changes are not completely understood. However, studying the mechanisms that allow B. burgdorferi to survive in the highly disparate environments of the tick vector and mammalian host could allow for the development of novel methods of preventing acquisition, survival, or transmission of the spirochete. In this regard, a putative membrane protein, BB0173, was characterized. BB0173 was found to be highly conserved across pathogenic Borrelia, and additionally contains several truly transmembrane domains, and a Bacteroides aerotolerance-like domain. The presence of these functional domains and the highly conserved nature of this protein, strongly suggests a required function of BB0173 in the survival of B. burgdorferi.

Dataset Information

Immunogenicity of Borrelia burgdorferi arthritis-related protein.

Publications

Immunogenicity of Borrelia burgdorferi arthritis-related protein.

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