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

I. C. Boulton; Andrew Gorringe; R. J.G. Carr; B. Gorinsky; Christopher L. Joannou; R. W. Evans

doi:10.1016/S0014-5793(97)01025-9

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

I. C. Boulton, Andrew Gorringe, R. J.G. Carr, B. Gorinsky, Christopher L. Joannou, R. W. Evans^*

^*Corresponding author for this work

Countermeasures Development & Evaluation Scientific Leaders

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

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 bad 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.

Original language	English
Pages (from-to)	409-413
Number of pages	5
Journal	FEBS Letters
Volume	414
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(97)01025-9
Publication status	Published - 8 Sept 1997

Bibliographical note

Funding Information:
Acknowledgements." This work was supported by Biotechnology and Biological Sciences Research Council studentship no. 9456368X, CAMR and the Special Trustees for St. Thomas Hospital.

Keywords

Neisseria meningitidis
Photon correlation spectroscopy
Transferrin

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10.1016/S0014-5793(97)01025-9

Cite this

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title = "Characterisation of the meningococcal transferrin binding protein complex by photon correlation spectroscopy",

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 bad 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.",

keywords = "Neisseria meningitidis, Photon correlation spectroscopy, Transferrin",

author = "Boulton, \{I. C.\} and Andrew Gorringe and Carr, \{R. J.G.\} and B. Gorinsky and Joannou, \{Christopher L.\} and Evans, \{R. W.\}",

note = "Funding Information: Acknowledgements.{"} This work was supported by Biotechnology and Biological Sciences Research Council studentship no. 9456368X, CAMR and the Special Trustees for St. Thomas Hospital.",

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doi = "10.1016/S0014-5793(97)01025-9",

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T1 - Characterisation of the meningococcal transferrin binding protein complex by photon correlation spectroscopy

AU - Boulton, I. C.

AU - Gorringe, Andrew

AU - Carr, R. J.G.

AU - Gorinsky, B.

AU - Joannou, Christopher L.

AU - Evans, R. W.

N1 - Funding Information: Acknowledgements." This work was supported by Biotechnology and Biological Sciences Research Council studentship no. 9456368X, CAMR and the Special Trustees for St. Thomas Hospital.

PY - 1997/9/8

Y1 - 1997/9/8

N2 - 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 bad 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.

AB - 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 bad 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.

KW - Neisseria meningitidis

KW - Photon correlation spectroscopy

KW - Transferrin

UR - https://www.scopus.com/pages/publications/0031559912

U2 - 10.1016/S0014-5793(97)01025-9

DO - 10.1016/S0014-5793(97)01025-9

M3 - Article

C2 - 9315730

AN - SCOPUS:0031559912

SN - 0014-5793

VL - 414

SP - 409

EP - 413

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

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

Abstract

Bibliographical note

Keywords

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