ArticleStructure (London, England : 1993)2012
Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 95 citations in OpenAlex.
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- Structural Modeling of the Treponema pallidum Outer Membrane Protein Repertoire: a Road Map for Deconvolution of Syphilis Pathogenesis and Development of a Syphilis Vaccine.Journal of bacteriology · 2021Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action.Scientific reports · 2020Article
- Identification and study of InV as an inverse autotransporter family representative in Edwardsiella piscicida.Archives of microbiology · 2020Article
- Staying out or Going in? The Interplay between Type 3 and Type 5 Secretion Systems in Adhesion and Invasion of Enterobacterial Pathogens.International journal of molecular sciences · 2020Review
- Bioinformatic and Molecular Analysis of Inverse Autotransporters from Escherichia coli.mSphere · 2019Article
- Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins.International journal of molecular sciences · 2019Review
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Expression of Leptospira membrane proteins Signal Peptidase (SP) and Leptospira Endostatin like A (Len A) in BL-21(DE3) is toxic to the host cells.Journal, genetic engineering & biotechnology · 2018Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They contain C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal β domains that are embedded in the outer membrane. Here, we identify the domain boundaries of an E. coli intimin β domain and use this information to solve its structure and the β domain structure of a Y. pseudotuberculosis invasin. Both β domain structures crystallized as monomers and reveal that the previous range of residues assigned to the β domain also includes a protease-resistant domain that is part of the passenger. Additionally, we identify 146 nonredundant representative members of the intimin/invasin family based on the boundaries of the highly conserved intimin and invasin β domains. We then use this set of sequences along with our structural data to find and map the evolutionarily constrained residues within the β domain.
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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.