Proteomics

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Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome


ABSTRACT: Localization of lipoproteins endogenously expressed under standard culture conditions was determined using multidimensional protein identification technology (MudPIT) mass spectrometry. B. burgdorferi B31A3 intact spirochetes were subjected to surface proteolysis with proteinase K.

INSTRUMENT(S): LTQ

ORGANISM(S): Borrelia Burgdorferi B31 (ncbitaxon:224326)

SUBMITTER: Wolfram R. Zuckert  

PROVIDER: MSV000080434 | MassIVE | Wed Dec 21 11:22:00 GMT 2016

SECONDARY ACCESSION(S): PXD005617

REPOSITORIES: MassIVE

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Publications

Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.

Dowdell Alexander S AS   Murphy Maxwell D MD   Azodi Christina C   Swanson Selene K SK   Florens Laurence L   Chen Shiyong S   Zückert Wolfram R WR  

Journal of bacteriology 20170228 6


The Lyme disease spirochete <i>Borrelia burgdorferi</i> is unique among bacteria in its large number of lipoproteins that are encoded by a small, exceptionally fragmented, and predominantly linear genome. Peripherally anchored in either the inner or outer membrane and facing either the periplasm or the external environment, these lipoproteins assume varied roles. A prominent subset of lipoproteins functioning as the apparent linchpins of the enzootic tick-vertebrate infection cycle have been exp  ...[more]

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