Structural highlights
FunctionA0A3R9NIL7_STRSA Required for transformation and DNA binding.[ARBA:ARBA00003988] Publication Abstract from PubMedType 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. Characterization of a glycan-binding complex of minor pilins completes the analysis of Streptococcus sanguinis type 4 pili subunits.,Shahin M, Sheppard D, Raynaud C, Berry JL, Gurung I, Silva LM, Feizi T, Liu Y, Pelicic V Proc Natl Acad Sci U S A. 2023 Jan 17;120(3):e2216237120. doi: , 10.1073/pnas.2216237120. Epub 2023 Jan 10. PMID:36626560[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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