ArticleCurrent microbiology2014
Both GtfA and GtfB are required for SraP glycosylation in Staphylococcus aureus.
Article in Current microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Glycosylation of oral bacteria in modulating adhesion and biofilm formation.Journal of oral microbiology · 2025Review
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Opportunities and Challenges of Bacterial Glycosylation for the Development of Novel Antibacterial Strategies.Frontiers in microbiology · 2021Review
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.Glycobiology · 2019Article
- Unraveling the sequence of cytosolic reactions in the export of GspB adhesin fromThe Journal of biological chemistry · 2018Article
- The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus.Scientific reports · 2017Article
- Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein.Scientific reports · 2017Article
- Bacterial size matters: Multiple mechanisms controlling septum cleavage and diplococcus formation are critical for the virulence of the opportunistic pathogen Enterococcus faecalis.PLoS pathogens · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- The Plasmin-Sensitive Protein Pls in Methicillin-Resistant Staphylococcus aureus (MRSA) Is a Glycoprotein.PLoS pathogens · 2017Article
- Engineering and Dissecting the Glycosylation Pathway of a Streptococcal Serine-rich Repeat Adhesin.The Journal of biological chemistry · 2016Article
- Insights into bacterial protein glycosylation in human microbiota.Science China. Life sciences · 2016Review
- The pan-genome of Lactobacillus reuteri strains originating from the pig gastrointestinal tract.BMC genomics · 2015Article
- Glycosyltransferase-mediated Sweet Modification in Oral Streptococci.Journal of dental research · 2015Review
- O-acetylation controls the glycosylation of bacterial serine-rich repeat glycoproteins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus has been shown to bind to human platelets through a variety of surface molecules, including serine-rich adhesin for platelets (SraP). The SraP mutant strain of S. aureus is significantly impaired in its ability to initiate infection compared with the wild strain. SraP is a cell wall-anchored, glycosylated protein. A previous study revealed that SecY2, Asp1, Asp2, Asp3, and SecA2 in the SraP operon were required for the efficient transport of glycosylated SraP from the cytoplasm to the bacterial cell surface. However, no glycosyltransferase (Gtf) was found to be involved in the glycosylation of SraP. In this study, SraP was found in all of the 55 clinical isolates of S. aureus using a real-time polymerase chain reaction assay. Sequence and phylogenetic analysis showed that GtfA and GtfB in the SraP operon were highly conserved in most of these clinical isolates. Conserved domains analysis revealed that both GtfA and GtfB contained a GT1_GtfA-like domain. Structural homology analysis inferred that they are both Gtfs. We then constructed an in vivo glycosylation system in Escherichia coli using SraP1–743 as the substrate and GtfA and GtfB as the Gtfs. Using this system, we found that GtfA and GtfB were the Gtfs that transferred the N-acetylglucosamine-containing oligosaccharides to the recombinant SraP1–743. Deletion of either one or both of the Gtfs abolished the glycosylation of SraP. In summary, GtfA and GtfB in the SraP operon are highly conserved in most clinical isolates of S. aureus, and both GtfA and GtfB are required for SraP glycosylation.
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