Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain.

ABSTRACT: Surface lipoproteins of Borrelia spirochetes are important virulence determinants in the transmission and pathogenesis of Lyme disease and relapsing fever. To further define the conformational secretion requirements and to identify potential lipoprotein translocation intermediates associated with the bacterial outer membrane (OM), we generated constructs in which Borrelia burgdorferi outer surface lipoprotein A (OspA) was fused to calmodulin (CaM), a conserved eukaryotic protein undergoing calcium-dependent folding. Protein localization assays showed that constructs in which CaM was fused to full-length wild-type (wt) OspA or to an intact OspA N-terminal "tether" peptide retained their competence for OM translocation even in the presence of calcium. In contrast, constructs in which CaM was

SUBMITTER: Chen S 

PROVIDER: S-EPMC3232903 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature