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Borrelia burgdorferi lipoproteins are secreted to the outer surface by default.
- 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.
- Subjects :
- Amino Acid Sequence
Antigens, Surface genetics
Bacterial Outer Membrane Proteins genetics
Bacterial Outer Membrane Proteins metabolism
Bacterial Proteins genetics
Bacterial Vaccines
Carrier Proteins genetics
Carrier Proteins metabolism
Lipoproteins genetics
Luminescent Proteins genetics
Luminescent Proteins metabolism
Molecular Sequence Data
Mutation
Protein Sorting Signals
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Red Fluorescent Protein
Bacterial Proteins metabolism
Borrelia burgdorferi metabolism
Cell Membrane metabolism
Lipoproteins metabolism
Subjects
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