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Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry.
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2002 (English)In: Journal of the American Society for Mass Spectrometry, ISSN 1044-0305, E-ISSN 1879-1123, Vol. 13, no 4, 295-299 p.Article in journal (Refereed) Published
Abstract [en]

Borrelia burgdorferi sensu lato is a tick-borne pathogen that causes Lyme disease. The characterization of membrane proteins from this and other pathogens may yield a better understanding of the mechanisms of infection and information useful for vaccine design. Characterization of the highly hydrophobic Borrelia outer membrane component P13 from a mutant (OspA- OspB- OspC- and OspD-) strain was undertaken by use of a combination of mass spectrometric methods. In a previous investigation, an electrospray ionization (ESI) mass spectrum of the intact protein provided an average molecular weight that was 20 Da lower than the predicted molecular weight. The mass deviation could be explained by a modification of the N-terminus of the protein such as pyroglutamylation (-17 Da) in combination with the experimental error of measurement, however more information was required. New structural information for this membrane protein was provided by peptide mapping with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF MS) and sequencing with ESI-quadrupole-TOF tandem MS.

Place, publisher, year, edition, pages
2002. Vol. 13, no 4, 295-299 p.
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Cell and Molecular Biology
URN: urn:nbn:se:umu:diva-48654DOI: 10.1016/S1044-0305(01)00365-8PubMedID: 11951966OAI: diva2:451708
Available from: 2011-10-26 Created: 2011-10-26 Last updated: 2011-10-26Bibliographically approved

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Östberg, YngveLavrinovicha, MarijaBergström, Sven
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Department of Molecular Biology (Faculty of Medicine)
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