ArticleMolecular microbiology2012
SpyA is a membrane-bound ADP-ribosyltransferase of Streptococcus pyogenes which modifies a streptococcal peptide, SpyB.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Translational coupling of neighboring genes in prokaryotes.Journal of bacteriology · 2025Review
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- T6SS and ExoA of flesh-eatingProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections.Toxins · 2019Review
- Group A Streptococcus encounters with host macrophages.Future microbiology · 2018Review
- SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall inFrontiers in cellular and infection microbiology · 2016Article
- Article
- Novel bacterial ADP-ribosylating toxins: structure and function.Nature reviews. Microbiology · 2014Review
- The globally disseminated M1T1 clone of group A Streptococcus evades autophagy for intracellular replication.Cell host & microbe · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
All sequenced genomes of Streptococcus pyogenes (Group A Streptococcus, GAS) encode a protein, SpyA, with homology to C3-like ADP-ribosyltransferase toxins. SpyA is a novel virulence factor which plays a role in pathogenesis in a mouse model of soft-tissue infection. In this study we demonstrate that SpyA is a surface-exposed membrane protein which is anchored to the streptococcal membrane by an N-terminal transmembrane sequence. We identified a small gene upstream of spyA, designated spyB, which encodes a peptide of 35 amino acids, and is co-transcribed with spyA. Expression of spyBA is strongly influenced by translational coupling: mutational inactivation of spyB translation completely abolishes translation of spyA. spyB expression increases with increasing cell density and reaches its maximum at late exponential growth phase. The SpyB N-terminus is predicted to fold into an amphipathic α-helix, a structural motif that targets a protein to the cytoplasmic membrane. Consistent with the prediction, we found that a SpyB fusion with peptide affinity tags is located in the streptococcal membrane. An ADP-ribosylation assay with recombinant SpyA demonstrated that SpyA modifies SpyB. Thus, our study suggests that ADP-ribosylation of SpyB may be an important function of SpyA.
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Registered trials
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