Borrelia burgdorferi lipoproteins are secreted to the outer surface by default

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Show simple item record Schulze, Ryan 2006-06-29T18:32:13Z 2006-06-29T18:32:13Z 2006-06-29T18:32:13Z
dc.description Molecular and Cell Biology II Room G027 Dykes 1:54 PM Abstract 183 en
dc.description.abstract Borrelia spirochetes are unique among diderm bacteria in their abundance of surface-displayed lipoproteins, some of which play important roles in the athogenesis of Lyme disease and relapsing fever. To identify the lipoprotein-sorting signals in Borrelia burgdorferi, we generated chimeras between the outer surface lipoprotein OspA, the periplasmic oligopeptide-binding lipoprotein OppAIV and mRFP1, a monomeric red fluorescent reporter protein. Localization of OspA and OppAIV point mutants showed that Borrelia lipoproteins do not follow the '+2' sorting rule which targets lipoproteins to the cytoplasmic or outer membrane of Gram-negative bacteria via the Lol pathway. Fusions of mRFP1 to short N-terminal lipopeptides of OspA, and surprisingly OppAIV, were targeted to the spirochetal surface. Mutagenesis of the OspA N-terminus defined less than five N-terminal amino acids as the minimal secretion-facilitating signal. With the exception of negative charges, which can act as partial subsurface retention signals in certain peptide contexts, lipoprotein secretion occurs independent of N-terminal sequence. Together, these data indicate that Borrelia lipoproteins are targeted to the bacterial surface by default, but can be retained in the periplasm by sequence-specific signals. en
dc.description.sponsorship Zueckert, Wolfram Microbiology, Molecular Genetics and Immunology en
dc.format.extent 1803264 bytes
dc.format.mimetype application/
dc.language.iso en_US en
dc.subject Borrelia burgdorferi en
dc.subject Protein transport en
dc.title Borrelia burgdorferi lipoproteins are secreted to the outer surface by default en
dc.type Presentation en

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