Characterization of a glycan-binding complex of minor pilins completes the
analysis of Streptococcus sanguinis type 4 pili subunits
analysis of Streptococcus sanguinis type 4 pili subunits
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Author(s)
Type
Journal Article
Abstract
Type 4 filaments (T4F)—of which type 4 pili (T4P) are the archetype—are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we complete the structure/function analysis of the full set of T4P pilins in the opportunistic bacterial pathogen Streptococcus sanguinis. We determined the structure of the minor pilin PilA, which is unexpectedly similar to one of the subunits of a tip-located complex of four minor pilins, widely conserved in T4F. We found that PilA interacts and dramatically stabilizes the minor pilin PilC. We determined the structure of PilC, showing that it is a modular pilin with a lectin module binding a subset of glycans prevalent in the human glycome, the host of S. sanguinis. Altogether, our findings support a model whereby the minor pilins in S. sanguinis T4P form a tip-located complex promoting adhesion to various host receptors. This has general implications for T4F.
Date Issued
2023-01-17
Date Acceptance
2022-12-09
Citation
Proceedings of the National Academy of Sciences of USA, 2023, 120 (3)
ISSN
0027-8424
Publisher
National Academy of Sciences
Journal / Book Title
Proceedings of the National Academy of Sciences of USA
Volume
120
Issue
3
Copyright Statement
© 2023 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY) https://creativecommons.org/licenses/by/4.0/
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Publication Status
Published
Article Number
ARTN e2216237120
Date Publish Online
2023-01-10