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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Staphylococcal complement evasion protein Sbi stabilises C3d dimers by inducing an N-terminal helix swap Rhys W. Dunphy , Ayla A. Wahid , Catherine R. Back , Rebecca L. Martin , Andrew G. Watts , Charlotte A. Dodson , Susan J. Crennell , Jean M. H. Van Den Elsen Frontiers In Immunology 13 DOI: 10.3389/fimmu.2022.892234 Diamond Proposal Number(s): [23269] Open Access Show Abstract ▼ Abstract: 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.	May 2022

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I04-Macromolecular Crystallography

Staphylococcal complement evasion protein Sbi stabilises C3d dimers by inducing an N-terminal helix swap

Rhys W. Dunphy , Ayla A. Wahid , Catherine R. Back , Rebecca L. Martin , Andrew G. Watts , Charlotte A. Dodson , Susan J. Crennell , Jean M. H. Van Den Elsen

Frontiers In Immunology 13

DOI: 10.3389/fimmu.2022.892234

Diamond Proposal Number(s): [23269]