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Defining the remarkable structural malleability of a bacterial surface protein Rib domain implicated in infection

DOI: 10.1073/pnas.1911776116 DOI Help

Authors: Fiona Whelan (The University of York) , Aleix Lafita (European Molecular Biology Laboratory) , Samuel C. Griffiths (The University of York) , Rachael E. M. Cooper (The University of York) , Jean L. Whittingham (The University of York) , Johan P. Turkenburg (The University of York) , Iain W. Manfield (The University of Leeds) , Alexander N. St. John (The University of Leeds) , Emanuele Paci (The University of Leeds) , Alex Bateman (European Molecular Biology Laboratory) , Jennifer R. Potts (The University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proceedings Of The National Academy Of Sciences , VOL 64

State: Published (Approved)
Published: December 2019
Diamond Proposal Number(s): 7864 , 9948 , 13587

Open Access Open Access

Abstract: Streptococcus groups A and B cause serious infections, including early onset sepsis and meningitis in newborns. Rib domain-containing surface proteins are found associated with invasive strains and elicit protective immunity in animal models. Yet, despite their apparent importance in infection, the structure of the Rib domain was previously unknown. Structures of single Rib domains of differing length reveal a rare case of domain atrophy through deletion of 2 core antiparallel strands, resulting in the loss of an entire sheet of the β-sandwich from an immunoglobulin-like fold. Previously, observed variation in the number of Rib domains within these bacterial cell wall-attached proteins has been suggested as a mechanism of immune evasion. Here, the structure of tandem domains, combined with molecular dynamics simulations and small angle X-ray scattering, suggests that variability in Rib domain number would result in differential projection of an N-terminal host-colonization domain from the bacterial surface. The identification of 2 further structures where the typical B-D-E immunoglobulin β-sheet is replaced with an α-helix further confirms the extensive structural malleability of the Rib domain.

Journal Keywords: Rib domain; domain atrophy; protein rod formation

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: B21-High Throughput SAXS , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography