Characterisation of the meningococcal transferrin binding protein complex by photon correlation spectroscopy.
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.
Boulton
I C
IC
Centre for Applied Microbiology and Research, Salisbury, UK.
Gorringe
A R
AR
Carr
R J
RJ
Gorinsky
B
B
Joannou
C L
CL
Evans
R W
RW
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D033862:Iron-Binding Proteins; D046911:Macromolecular Substances; D009345:Neisseria meningitidis / Q000254:growth & development / Q000378:metabolism*; D013057:Spectrum Analysis / Q000379:methods; D014168:Transferrin / Q000737:chemistry / Q000378:metabolism; D033863:Transferrin-Binding Proteins
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D033862:Iron-Binding Proteins; D046911:Macromolecular Substances; D014168:Transferrin; D033863:Transferrin-Binding Proteins