Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus.

ABSTRACT: Borrelia burgdorferi surface lipoproteins are essential to the pathogenesis of Lyme borreliosis, but the mechanisms responsible for their localization are only beginning to emerge. We have previously demonstrated the critical nature of the amino-terminal 'tether' domain of the mature lipoprotein for sorting a fluorescent reporter to the Borrelia cell surface. Here, we show that individual deletion of four contiguous residues within the tether of major surface lipoprotein OspA results in its inefficient translocation across the Borrelia outer membrane. Intriguingly, C-terminal epitope tags of these N-terminal deletion mutants were selectively surface-exposed. Fold-destabilizing C-terminal point mutations and deletions did not block OspA secretion, but rather restored one of the otherwise pe

SUBMITTER: Schulze RJ 

PROVIDER: S-EPMC2999405 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature