Characterisation of the meningococcal transferrin binding protein complex by photon correlation spectroscopy

FEBS Lett. 1997 Sep 8;414(2):409-13. doi: 10.1016/s0014-5793(97)01025-9.

Abstract

Photon correlation spectroscopy demonstrated for the first time that co-purified meningococcal TbpA+B form a complex in solution. This structure bound hTf and the resultant species underwent partial dissociation after exposure to additional hTf or following prolonged incubation. Purified TbpA and TbpB had similar apparent sizes but showed distinctive size profiles suggesting that TbpA forms a largely homogeneous population while TbpB may produce more variable particle sizes under these conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / isolation & purification
  • Carrier Proteins / chemistry*
  • Carrier Proteins / isolation & purification
  • Humans
  • Iron-Binding Proteins
  • Macromolecular Substances
  • Neisseria meningitidis / growth & development
  • Neisseria meningitidis / metabolism*
  • Spectrum Analysis / methods
  • Transferrin / chemistry
  • Transferrin / metabolism
  • Transferrin-Binding Proteins

Substances

  • Bacterial Outer Membrane Proteins
  • Carrier Proteins
  • Iron-Binding Proteins
  • Macromolecular Substances
  • Transferrin
  • Transferrin-Binding Proteins