Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry

Carol L. Nilsson, Helen J. Cooper, Kristina Håkansson, Alan G. Marshall, Yngve Östberg, Marija Lavrinovicha, Sven Bergström

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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. ESI Fourier transform ion cyclotron resonance (FT-ICR) MS at 9.4 tesla revealed that the Borrelia membrane protein is not only pyroglutamylated, but also contains an amino acid substitution near the N-terminus.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
JournalJournal of the American Society for Mass Spectrometry
Volume13
Issue number4
DOIs
StatePublished - 2002
Externally publishedYes

Fingerprint

Electrospray ionization
Borrelia burgdorferi
Mass spectrometry
Borrelia
Mass Spectrometry
Membrane Proteins
Pathogens
Molecular Weight
Molecular weight
Borrelia burgdorferi Group
Cyclotrons
Cyclotron resonance
Peptide Mapping
Lyme Disease
Ticks
Fourier Analysis
Amino Acid Substitution
Ionization
Desorption
Fourier transforms

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy

Cite this

Nilsson, C. L., Cooper, H. J., Håkansson, K., Marshall, A. G., Östberg, Y., Lavrinovicha, M., & Bergström, S. (2002). Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry. Journal of the American Society for Mass Spectrometry, 13(4), 295-299. https://doi.org/10.1016/S1044-0305(01)00365-8

Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry. / Nilsson, Carol L.; Cooper, Helen J.; Håkansson, Kristina; Marshall, Alan G.; Östberg, Yngve; Lavrinovicha, Marija; Bergström, Sven.

In: Journal of the American Society for Mass Spectrometry, Vol. 13, No. 4, 2002, p. 295-299.

Research output: Contribution to journalArticle

Nilsson, CL, Cooper, HJ, Håkansson, K, Marshall, AG, Östberg, Y, Lavrinovicha, M & Bergström, S 2002, 'Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry', Journal of the American Society for Mass Spectrometry, vol. 13, no. 4, pp. 295-299. https://doi.org/10.1016/S1044-0305(01)00365-8
Nilsson, Carol L. ; Cooper, Helen J. ; Håkansson, Kristina ; Marshall, Alan G. ; Östberg, Yngve ; Lavrinovicha, Marija ; Bergström, Sven. / Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry. In: Journal of the American Society for Mass Spectrometry. 2002 ; Vol. 13, No. 4. pp. 295-299.
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