Identification of invasin: A protein that allows enteric bacteria to penetrate cultured mammalian cells
Abstract
Bacterial strains harboring the Yersinia pseudotuberculosis inv locus were analyzed in order to investigate the mechanism of host cell penetration by an invasive pathogen. The inv locus was found to be necessary for Y. pseudotuberculosis to enter HEp-2 cells and sufficient to convert E. coli into a microorganism able to penetrate cultured cells. Both E. coli and Y. pseudotuberculosis strains harboring inv mutations were defective for entry into HEp-2 cells. Furthermore, molecular clones containing inv, and little additional DNA, converted E. coli into a microorganism that was indistinguishable from the parental Yersinia strain with regard to the entry of cultured cells. Data from in vitro protein synthesis indicated that a 103 kd protein was synthesized from inv, saturating the coding capacity of the locus. The nucleotide sequence shows an open reading frame corresponding to a protein of similar size. This protein, called invasin, is necessary for the microorganisms to penetrate HEp-2 cells, and is compartmentalized on the outer surface of the bacterium.
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The predicted 3-D structures of the N-termini of many Als proteins are remarkably similar to the Yersinia pseudotuberculosis invasin, a protein that induces the endocytosis of Y. pseudotuberculosis by mammalian epithelial cells.
“Interestingly, the predicted 3-D structures of the N-termini of many Als proteins are remarkably similar to the Yersinia pseudotuberculosis invasin, a protein that induces the endocytosis of Y. pseudotuberculosis by mammalian epithelial cells [28,29].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [29]
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MSCRAMM-MEDIATED ADHERENCE OF MICROORGANISMS TO HOST TISSUES
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Bacterial Adhesion and Entry into Host Cells
Pizarro-Cerdá, J., & Cossart, P. (2006) · Cell · doi:10.1016/j.cell.2006.02.012 · Cited by 977 · see citing works
“The first bacterial invasion protein ever described was invasin (Isberg et al., 1987), a surface protein of Y. enterocolitica and Y. pseudo-tuberculosis .”
Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells
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<i>Yersinia</i> adhesins: An arsenal for infection
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- Authors
- Isberg, R. R., Voorhis, D. L., & Falkow, S.
- Affiliations
- Tufts University (US)
- Stanford Medicine (US)
- ORCID
- Isberg, Ralph R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1987-08
- Volume
- 50
- Issue
- 5
- Pages
- 769-778
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2008132225
- Cited by
- 597
- References
- 1
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 5 · 2023: 10 · 2022: 3 · 2021: 8 · 2020: 11 · 2019: 7 · 2018: 8 · 2017: 9 · 2016: 17 · 2015: 8 · 2014: 17 · 2013: 11 · 2012: 14
- FWCI
- 16.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Agencja Badań Medycznych
- National Institute of Allergy and Infectious Diseases (R01AI023538, R01 AI 23538)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Yersinia bacterium, plague, ectoparasites research
- Keywords
- invasin, Yersinia pseudotuberculosis, enteric bacteria, host cell invasion, Escherichia coli transformation, HEp-2 cells, bacterial outer membrane proteins
- MeSH terms
- Animals, Bacterial Adhesion, Bacterial Proteins, Base Sequence, Cell Line, Cell Membrane, DNA, Bacterial, DNA, Recombinant, Escherichia coli, Molecular Weight, Mutation, Plasmids, Trypsin, Yersinia pseudotuberculosis, Adhesins, Bacterial
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