ArticleNature communications2020
Mechanism and inhibition of Streptococcus pneumoniae IgA1 protease.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Innovative engineering approaches to model host-microbiome interactions in vitro.Advanced drug delivery reviews · 2025Review
- Human immunodeficiency virus and antiretroviral therapies exert distinct influences across diverse gut microbiomes.Nature microbiology · 2025Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases.The EMBO journal · 2025Article
- Biochemical and structural characterization of the human gut microbiome metallopeptidase IgAse provides insight into its unique specificity for the Fab' region of IgA1 and IgA2.PLoS pathogens · 2025Article
- Host Serum Amyloid A1 FacilitatesMicroorganisms · 2025Article
- The structure of the Gemella haemolysans M26 IgA1 protease trypsin-like domain.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Trichocystatin-2 fromFrontiers in parasitology · 2025Article
- Genomic and panproteomic analysis of the development of infant immune responses to antigenically-diverse pneumococci.Nature communications · 2024Article
- Effects ofFrontiers in molecular biosciences · 2024Article
- A substrate-induced gating mechanism is conserved among Gram-positive IgA1 metalloproteases.Communications biology · 2022Article
- Human and Bacterial Toll-Interleukin Receptor Domains Exhibit Distinct Dynamic Features and Functions.Molecules (Basel, Switzerland) · 2022Article
- Inhibition ofMicrobiology (Reading, England) · 2022Article
- Yields and Immunomodulatory Effects of Pneumococcal Membrane Vesicles Differ with the Bacterial Growth Phase.Advanced healthcare materials · 2022Article
- Secretory Proteases of the Human Skin Microbiome.Infection and immunity · 2022Article
- Pathogenesis of IgA Nephropathy: Current Understanding and Implications for Development of Disease-Specific Treatment.Journal of clinical medicine · 2021Review
- Immunoglobulin A Glycosylation and Its Role in Disease.Experientia supplementum (2012) · 2021Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Opportunistic pathogens such as Streptococcus pneumoniae secrete a giant metalloprotease virulence factor responsible for cleaving host IgA1, yet the molecular mechanism has remained unknown since their discovery nearly 30 years ago despite the potential for developing vaccines that target these enzymes to block infection. Here we show through a series of cryo-electron microscopy single particle reconstructions how the Streptococcus pneumoniae IgA1 protease facilitates IgA1 substrate recognition and how this can be inhibited. Specifically, the Streptococcus pneumoniae IgA1 protease subscribes to an active-site-gated mechanism where a domain undergoes a 10.0 Å movement to facilitate cleavage. Monoclonal antibody binding inhibits this conformational change, providing a direct means to block infection at the host interface. These structural studies explain decades of biological and biochemical studies and provides a general strategy to block Streptococcus pneumoniae IgA1 protease activity to potentially prevent infection.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.