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Mol Microbiol. 2010 Feb;75(3):692-709. doi: 10.1111/j.1365-2958.2009.07015.x. Epub 2009 Dec 16.

Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins.

Author information

1
Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.

Abstract

The outer membrane (OM) of the pathogenic diderm spirochete, Borrelia burgdorferi, contains integral beta-barrel outer membrane proteins (OMPs) in addition to its numerous outer surface lipoproteins. Very few OMPs have been identified in B. burgdorferi, and the protein machinery required for OMP assembly and OM localization is currently unknown. Essential OM BamA proteins have recently been characterized in Gram-negative bacteria that are central components of an OM beta-barrel assembly machine and are required for proper localization and insertion of bacterial OMPs. In the present study, we characterized a putative B. burgdorferi BamA orthologue encoded by open reading frame bb0795. Structural model predictions and cellular localization data indicate that the B. burgdorferi BB0795 protein contains an N-terminal periplasmic domain and a C-terminal, surface-exposed beta-barrel domain. Additionally, assays with an IPTG-regulatable bb0795 mutant revealed that BB0795 is required for B. burgdorferi growth. Furthermore, depletion of BB0795 results in decreased amounts of detectable OMPs in the B. burgdorferi OM. Interestingly, a decrease in the levels of surface-exposed lipoproteins was also observed in the mutant OMs. Collectively, our structural, cellular localization and functional data are consistent with the characteristics of other BamA proteins, indicating that BB0795 is a B. burgdorferi BamA orthologue.

PMID:
20025662
PMCID:
PMC5581936
DOI:
10.1111/j.1365-2958.2009.07015.x
[Indexed for MEDLINE]
Free PMC Article

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