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

Nilsson, Carol L LU ; Cooper, Helen J; Håkansson, Kristina; Marshall, Alan G; Ostberg, Yngve; Lavrinovicha, Marija and Bergström, Sven (2002) In Journal of the American Society for Mass Spectrometry 13(4). p.9-295
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... (More)

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.

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publication status
published
keywords
Animals, Borrelia burgdorferi, Electrophoresis, Polyacrylamide Gel, Hydrolysis, Membrane Proteins, Peptide Mapping, Spectrometry, Mass, Electrospray Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectroscopy, Fourier Transform Infrared, Trypsin, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.
in
Journal of the American Society for Mass Spectrometry
volume
13
issue
4
pages
5 pages
publisher
Elsevier
external identifiers
  • scopus:0036206286
ISSN
1044-0305
DOI
10.1016/S1044-0305(01)00365-8
language
English
LU publication?
no
id
51b60606-9743-487d-9bdc-b53cbf738d20
date added to LUP
2017-05-16 10:41:37
date last changed
2017-05-31 11:56:55
@article{51b60606-9743-487d-9bdc-b53cbf738d20,
  abstract     = {<p>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.</p>},
  author       = {Nilsson, Carol L and Cooper, Helen J and Håkansson, Kristina and Marshall, Alan G and Ostberg, Yngve and Lavrinovicha, Marija and Bergström, Sven},
  issn         = {1044-0305},
  keyword      = {Animals,Borrelia burgdorferi,Electrophoresis, Polyacrylamide Gel,Hydrolysis,Membrane Proteins,Peptide Mapping,Spectrometry, Mass, Electrospray Ionization,Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization,Spectroscopy, Fourier Transform Infrared,Trypsin,Journal Article,Research Support, Non-U.S. Gov't,Research Support, U.S. Gov't, Non-P.H.S.,Research Support, U.S. Gov't, P.H.S.},
  language     = {eng},
  number       = {4},
  pages        = {9--295},
  publisher    = {Elsevier},
  series       = {Journal of the American Society for Mass Spectrometry},
  title        = {Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry},
  url          = {http://dx.doi.org/10.1016/S1044-0305(01)00365-8},
  volume       = {13},
  year         = {2002},
}