An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines

Ali Saber Abdelhameed, Gordon A. Morris, Gary G. Adams, Arthur J. Rowe, Olivier Laloux, Louis Cerny, Benjamin Bonnier, Pierre Duvivier, Karel Conrath, Christophe Lenfant, Stephen E. Harding

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Tetanus toxoid protein has been characterized with regard oligomeric state and hydrodynamic (low-resolution) shape, important parameters with regard its use in glycoconjugate vaccines. From sedimentation velocity and sedimentation equilibrium analysis in the analytical ultracentrifuge tetanus toxoid protein is shown to be mostly monomeric in solution (∼86%) with approximately 14% dimer. The relative proportions do not appear to change significantly with concentration, suggesting the two components are not in reversible equilibrium. Hydrodynamic solution conformation studies based on high precision viscometry, combined with sedimentation data show the protein to be slightly extended conformation in solution with an aspect ratio ∼3. The asymmetric structure presents a greater surface area for conjugation with polysaccharide than a more globular structure, underpinning its popular choice as a conjugation protein for glycoconjugate vaccines.

LanguageEnglish
Pages1831-1835
Number of pages5
JournalCarbohydrate Polymers
Volume90
Issue number4
Early online date15 Jul 2012
DOIs
Publication statusPublished - 6 Nov 2012
Externally publishedYes

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Tetanus Toxoid
Glycoconjugates
Vaccines
Sedimentation
Proteins
Conformations
Hydrodynamics
Viscosity measurement
Polysaccharides
Dimers
Aspect ratio

Cite this

Abdelhameed, Ali Saber ; Morris, Gordon A. ; Adams, Gary G. ; Rowe, Arthur J. ; Laloux, Olivier ; Cerny, Louis ; Bonnier, Benjamin ; Duvivier, Pierre ; Conrath, Karel ; Lenfant, Christophe ; Harding, Stephen E. / An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines. In: Carbohydrate Polymers. 2012 ; Vol. 90, No. 4. pp. 1831-1835.
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Abdelhameed, AS, Morris, GA, Adams, GG, Rowe, AJ, Laloux, O, Cerny, L, Bonnier, B, Duvivier, P, Conrath, K, Lenfant, C & Harding, SE 2012, 'An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines', Carbohydrate Polymers, vol. 90, no. 4, pp. 1831-1835. https://doi.org/10.1016/j.carbpol.2012.07.032

An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines. / Abdelhameed, Ali Saber; Morris, Gordon A.; Adams, Gary G.; Rowe, Arthur J.; Laloux, Olivier; Cerny, Louis; Bonnier, Benjamin; Duvivier, Pierre; Conrath, Karel; Lenfant, Christophe; Harding, Stephen E.

In: Carbohydrate Polymers, Vol. 90, No. 4, 06.11.2012, p. 1831-1835.

Research output: Contribution to journalArticle

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T1 - An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines

AU - Abdelhameed, Ali Saber

AU - Morris, Gordon A.

AU - Adams, Gary G.

AU - Rowe, Arthur J.

AU - Laloux, Olivier

AU - Cerny, Louis

AU - Bonnier, Benjamin

AU - Duvivier, Pierre

AU - Conrath, Karel

AU - Lenfant, Christophe

AU - Harding, Stephen E.

PY - 2012/11/6

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KW - Analytical ultracentrifugation

KW - Hydrodynamics

KW - Solution conformation

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