ArticleThe EMBO journal2002
GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 127 citations in OpenAlex.
- Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Unprecedented Diversity of the Glycoside Hydrolase Family 70: A Comprehensive Analysis of Sequence, Structure, and Function.Journal of agricultural and food chemistry · 2024Article
- Review
- A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat.Acta crystallographica. Section D, Structural biology · 2022Article
- New insights in the coordinated amidase and glucosaminidase activity of the major autolysin (Atl) in Staphylococcus aureus.Communications biology · 2020Article
- Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase.Chemical science · 2020Article
- Phylogenetically Defined Isoforms ofInternational journal of molecular sciences · 2019Article
- A choline binding polypeptide of LytA inhibits the growth of Streptococcus pneumoniae by binding to choline in the cell wall.The Journal of antibiotics · 2018Article
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- MET-activating Residues in the B-repeat of the Listeria monocytogenes Invasion Protein InlB.The Journal of biological chemistry · 2016Article
- Innate and adaptive immunologic functions of complement in the host response to Listeria monocytogenes infection.Immunobiology · 2016Review
- LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.Microbial drug resistance (Larchmont, N.Y.) · 2016Article
- Identification of a Lipoteichoic Acid Glycosyltransferase Enzyme Reveals that GW-Domain-Containing Proteins Can Be Retained in the Cell Wall of Listeria monocytogenes in the Absence of Lipoteichoic Acid or Its Modifications.Journal of bacteriology · 2016Article
- Proteomics identifies Bacillus cereus EntD as a pivotal protein for the production of numerous virulence factors.Frontiers in microbiology · 2015Article
- House dust mites possess a polymorphic, single domain putative peptidoglycan d,l endopeptidase belonging to the NlpC/P60 Superfamily.FEBS open bio · 2015Article
- In situ proteolysis, crystallization and preliminary X-ray diffraction analysis of a VHH that binds listeria internalin B.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystal structure of an engineered YopM-InlB hybrid protein.BMC structural biology · 2014Article
- How Listeria monocytogenes organizes its surface for virulence.Frontiers in cellular and infection microbiology · 2014Review
- Multifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes.Sub-cellular biochemistry · 2014Review
- Characterization of a potential Listeria monocytogenes virulence factor associated with attachment to fresh produce.Applied and environmental microbiology · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
InlB, a surface-localized protein of Listeria monocytogenes, induces phagocytosis in non-phagocytic mammalian cells by activating Met, a receptor tyrosine kinase. InlB also binds glycosaminoglycans and the protein gC1q-R, two additional host ligands implicated in invasion. We present the structure of InlB, revealing a highly elongated molecule with leucine-rich repeats that bind Met at one end, and GW domains that dissociably bind the bacterial surface at the other. Surprisingly, the GW domains are seen to resemble SH3 domains. Despite this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. However, we do show that the GW domains, in addition to binding glycosaminoglycans, bind gC1q-R specifically, and that this binding requires release of InlB from the bacterial surface. Dissociable attachment to the bacterial surface via the GW domains may be responsible for restricting Met activation to a small, localized area of the host cell and for coupling InlB-induced host membrane dynamics with bacterial proximity during invasion.
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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.