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Staphylococcal Complement Evasion Protein Sbi Stabilises C3d Dimers by Inducing an N-Terminal Helix Swap.
Dunphy, Rhys W; Wahid, Ayla A; Back, Catherine R; Martin, Rebecca L; Watts, Andrew G; Dodson, Charlotte A; Crennell, Susan J; van den Elsen, Jean M H.
Afiliação
  • Dunphy RW; Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
  • Wahid AA; Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
  • Back CR; Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
  • Martin RL; Department of Pharmacy and Pharmacology, University of Bath, Bath, United Kingdom.
  • Watts AG; Department of Pharmacy and Pharmacology, University of Bath, Bath, United Kingdom.
  • Dodson CA; Department of Pharmacy and Pharmacology, University of Bath, Bath, United Kingdom.
  • Crennell SJ; Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
  • van den Elsen JMH; Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
Front Immunol ; 13: 892234, 2022.
Article em En | MEDLINE | ID: mdl-35693766
Staphylococcus aureus is an opportunistic pathogen that is able to thwart an effective host immune response by producing a range of immune evasion molecules, including S. aureus binder of IgG (Sbi) which interacts directly with the central complement component C3, its fragments and associated regulators. Recently we reported the first structure of a disulfide-linked human C3d17C dimer and highlighted its potential role in modulating B-cell activation. Here we present an X-ray crystal structure of a disulfide-linked human C3d17C dimer, which undergoes a structurally stabilising N-terminal 3D domain swap when in complex with Sbi. These structural studies, in combination with circular dichroism and fluorescence spectroscopic analyses, reveal the mechanism underpinning this unique helix swap event and could explain the origins of a previously discovered N-terminally truncated C3dg dimer isolated from rat serum. Overall, our study unveils a novel staphylococcal complement evasion mechanism which enables the pathogen to harness the ability of dimeric C3d to modulate B-cell activation.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Staphylococcus aureus / Proteínas de Bactérias Limite: Animals Idioma: En Revista: Front Immunol Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Staphylococcus aureus / Proteínas de Bactérias Limite: Animals Idioma: En Revista: Front Immunol Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Reino Unido