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Borrelia burgdorferi lipoproteins are secreted to the outer surface by default.

Authors :
Schulze RJ
Zückert WR
Source :
Molecular microbiology [Mol Microbiol] 2006 Mar; Vol. 59 (5), pp. 1473-84.
Publication Year :
2006

Abstract

Borrelia spirochaetes are unique among diderm bacteria in their abundance of surface-displayed lipoproteins, some of which play important roles in the pathogenesis 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 spirochaetal 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.

Details

Language :
English
ISSN :
0950-382X
Volume :
59
Issue :
5
Database :
MEDLINE
Journal :
Molecular microbiology
Publication Type :
Academic Journal
Accession number :
16468989
Full Text :
https://doi.org/10.1111/j.1365-2958.2006.05039.x