ArticleJournal of molecular biology2019
Structure and Function Characterization of the a1a2 Motifs of Streptococcus pyogenes M Protein in Human Plasminogen Binding.
Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Structural basis for collagen recognition by theeLife · 2025Article
- Hydrophobic residues in the D-domain of a plasminogen-binding M-protein modulate α-helicity, oligomerization, and surface anchoring in Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- Hijacking of plasminogen by dengue virus: The kringle-4 and -5 domains of plasminogen binds synergistically to the domain I of envelope protein.Protein science : a publication of the Protein Society · 2025Article
- Streptolysin O accelerates the conversion of plasminogen to plasmin.Nature communications · 2024Article
- A local α-helix drives structural evolution of streptococcal M-protein affinity for host human plasminogen.The Biochemical journal · 2020Article
- The M Protein of Streptococcus pyogenes Strain AP53 Retains Cell Surface Functional Plasminogen Binding after Inactivation of the Sortase A Gene.Journal of bacteriology · 2020Article
- Streptococcus co-opts a conformational lock in human plasminogen to facilitate streptokinase cleavage and bacterial virulence.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
Abstract
Plasminogen (Plg)-binding M protein (PAM) is a group A streptococcal cell surface receptor that is crucial for bacterial virulence. Previous studies revealed that, by binding to the kringle 2 (KR2) domain of host Plg, the pathogen attains a proteolytic microenvironment on the cell surface that facilitates its dissemination from the primary infection site. Each of the PAM molecules in their dimeric assembly consists of two Plg binding motifs (called the a1 and a2 repeats). To date, the molecular interactions between the a1 repeat and KR2 have been structurally characterized, whereas the role of the a2 repeat is less well defined. Here, we report the 1.7-Å x-ray crystal structure of KR2 in complex with a monomeric PAM peptide that contains both the a1 and a2 motifs. The structure reveals how the PAM peptide forms key interactions simultaneously with two KR2 via the high-affinity lysine isosteres within the a1a2 motifs. Further studies, through combined mutagenesis and functional characterization, show that a2 is a stronger KR2 binder than a1, suggesting that these two motifs may play discrete roles in mediating the final PAM-Plg assembly.
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Registered trials
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