Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from Streptococcus gordonii

The Journal of Biological Chemistry
Yu ChenTom A Rapoport

Abstract

Many pathogenic bacteria, including Streptococcus gordonii, possess a pathway for the cellular export of a single serine-rich-repeat protein that mediates the adhesion of bacteria to host cells and the extracellular matrix. This adhesin protein is O-glycosylated by several cytosolic glycosyltransferases and requires three accessory Sec proteins (Asp1-3) for export, but how the adhesin protein is processed for export is not well understood. Here, we report that the S. gordonii adhesin GspB is sequentially O-glycosylated by three enzymes (GtfA/B, Nss, and Gly) that attach N-acetylglucosamine and glucose to Ser/Thr residues. We also found that modified GspB is transferred from the last glycosyltransferase to the Asp1/2/3 complex. Crystal structures revealed that both Asp1 and Asp3 are related to carbohydrate-binding proteins, suggesting that they interact with carbohydrates and bind glycosylated adhesin, a notion that was supported by further analyses. We further observed that Asp1 also has an affinity for phospholipids, which is attenuated by Asp2. In summary, our findings support a model in which the GspB adhesin is sequentially glycosylated by GtfA/B, Nss, and Gly and then transferred to the Asp1/2/3 complex in which Asp1 media...Continue Reading

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Citations

Dec 6, 2018·The Journal of Biological Chemistry·Cierra SpencerPaul M Sullam
May 1, 2019·Gut Microbes·Dimitrios LatousakisNathalie Juge
Apr 8, 2018·The Journal of Biological Chemistry·Christina Schäffer, Paul Messner
Jan 2, 2021·The Journal of Biological Chemistry·Ravin SeepersaudPaul M Sullam
Nov 17, 2020·Frontiers in Microbiology·Jia Mun ChanRobert S Heyderman
Jan 12, 2021·The Journal of Biological Chemistry·Ravin SeepersaudPaul M Sullam
Jun 20, 2019·Microbiology Spectrum·Miriam BraunsteinPaul M Sullam
Aug 19, 2020·ACS Chemical Biology·Asif ShajahanParastoo Azadi

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