Factor H binding proteins protect division septa on encapsulated Streptococcus pneumoniae against complement C3b deposition and amplification

Anuj Pathak, Jan Bergstrand, Vicky Sender, Laura Spelmink, Marie-Stephanie Aschtgen, Sandra Muschiol, Jerker Widengren and Birgitta Henriques-Normark ()
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Anuj Pathak: Karolinska Institutet
Jan Bergstrand: Royal Institute of Technology (KTH), Experimental Biomolecular Physics
Vicky Sender: Karolinska Institutet
Laura Spelmink: Karolinska Institutet
Marie-Stephanie Aschtgen: Karolinska Institutet
Sandra Muschiol: Karolinska Institutet
Jerker Widengren: Royal Institute of Technology (KTH), Experimental Biomolecular Physics
Birgitta Henriques-Normark: Karolinska Institutet

Nature Communications, 2018, vol. 9, issue 1, 1-16

Abstract: Abstract Streptococcus pneumoniae evades C3-mediated opsonization and effector functions by expressing an immuno-protective polysaccharide capsule and Factor H (FH)-binding proteins. Here we use super-resolution microscopy, mutants and functional analysis to show how these two defense mechanisms are functionally and spatially coordinated on the bacterial cell surface. We show that the pneumococcal capsule is less abundant at the cell wall septum, providing C3/C3b entry to underlying nucleophilic targets. Evasion of C3b deposition at division septa and lateral amplification underneath the capsule requires localization of the FH-binding protein PspC at division sites. Most pneumococcal strains have one PspC protein, but successful lineages in colonization and disease may have two, PspC1 and PspC2, that we show affect virulence differently. We find that spatial localization of these FH-recruiting proteins relative to division septa and capsular layer is instrumental for pneumococci to resist complement-mediated opsonophagocytosis, formation of membrane-attack complexes, and for the function as adhesins.

Date: 2018
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DOI: 10.1038/s41467-018-05494-w

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