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Cited by 798Cell Adhesion Molecules ResearchBiochemical and Structural CharacterizationCellular Mechanics and Interactions

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Multiple β1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells

Isberg, Ralph R., Leong, John M.·1990·Cell
DOI 10.1016/0092-8674(90)90099-z
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Abstract

Mammalian cell receptors that promote entry of intracellular bacteria into nonphagocytic cells have not been identified. We show here that multiple members of the integrin superfamily of cell adhesion receptors bind the Y. pseudotuberculosis invasin protein prior to bacterial penetration into mammalian cells. Affinity chromatography of crude detergent extracts demonstrated that integrins containing the subunit structures alpha 3 beta 1, alpha 5 beta 1, and alpha 6 beta 1 bound to immobilized invasin. Furthermore, phospholipid vesicles containing isolated integrin proteins were able to attach to invasin. Specificity for invasin binding to the identified integrin receptors was also demonstrated, as immunoprobing and phospholipid reconstitution studies showed that the alpha 2 beta 1 integrin, beta 2 chain integrins, and vitronectin receptor (alpha v beta 3) were not involved in cellular attachment to invasin.

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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 [28]

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Research works printed but not linked: 45

  1. Argraves, 1987, Amino acid sequence of the human fibronectin receptor, J. Cell Biol., 105, 1183, 10.1083/jcb.105.3.1183 · DOI
  2. Argraves, 1989, Fibulin, a novel protein that interacts with the fibronectin receptor β subunit, Cell, 58, 623, 10.1016/0092-8674(89)90097-4 · DOI
  3. Brasaemle, 1988, Microelisa reader quantitation of fixed stained, solubilized cells in microtitre dishes, Biotechniques, 6, 418
  4. Buck, 1987, Integrin, a transmembrane glycoprotein complex mediating cell-substratum adhesion, J. Cell Sci. (Suppl.), 8, 231, 10.1242/jcs.1987.Supplement_8.13 · DOI
  5. Cheresh, 1989, A novel vitronectin receptor integrin (αvβx) is responsible for distinct adhesive properties of carcinoma cells, Cell, 57, 59, 10.1016/0092-8674(89)90172-4 · DOI
  6. Corbi, 1988, The human leukocyte adhesion glycoprotein Mac-1 (complement receptor type 3, CD11b) alpha subunit, J. Biol. Chem., 263, 12403, 10.1016/S0021-9258(18)37770-6 · DOI
  7. Dedhar, 1987, A cell surface receptor complex for collagen type I recognizes the Arg-Gly-Asp sequence, J. Cell Biol., 104, 585, 10.1083/jcb.104.3.585 · DOI
  8. D'Souza, 1988, Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor, Science, 242, 91, 10.1126/science.3262922 · DOI
  9. Finlay, 1988, Comparison of the invasion strategies used by Salmonella choleraesuis, Shigella flexneri and Yersinia enterocolitica to enter cultured animal cells: endosome acidification is not required for bacterial invasion or intracellular replication, Biochimie, 70, 1089, 10.1016/0300-9084(88)90271-4 · DOI
  10. Finlay, 1988, Identification of TnphoA mutants of Salmonella that are unable to pass through a polarized MDCK epithelial cell monolayer, Mol. Microbiol., 2, 757, 10.1111/j.1365-2958.1988.tb00087.x · DOI
  11. Flock, 1987, Cloning and expression of the gene for a fibronectin-binding protein from Staphylococcus aureus, EMBO J., 6, 2351, 10.1002/j.1460-2075.1987.tb02511.x · DOI
  12. Ginsberg, 1988, Cytoadhesins, integrins, and platelets, Thromb. Haemost., 59, 1, 10.1055/s-0038-1642555 · DOI
  13. Hemler, 1987, The VLA protein family, J. Biol. Chem., 262, 3300, 10.1016/S0021-9258(18)61504-2 · DOI
  14. Hemler, 1987, Characterization of the cell surface heterodimer VLA-4 and related peptides, J. Biol. Chem., 262, 11478, 10.1016/S0021-9258(18)60831-2 · DOI
  15. Hemler, 1988, Multiple very late antigen (VLA) heterodimers on platelets: evidence for distinct VLA-2, VLA-5 (fibronectin receptor), and VLA-6 structures, J. Biol. Chem., 263, 7660, 10.1016/S0021-9258(18)68549-7 · DOI
  16. Hemler, 1989, Association of the VLA α6 subunit with a novel protein, J. Biol. Chem., 264, 6529, 10.1016/S0021-9258(18)83380-4 · DOI
  17. Hodinka, 1988, Ultrastructural study of endocytosis of Chlamydia trachomatis, Infect. Immun., 56, 1456, 10.1128/IAI.56.6.1456-1463.1988 · DOI
  18. Holzmann, 1989, Identification of a murine Peyer's patch-specific lymphocyte homing receptor as an integrin molecule with an α chain homologous to human VLA-4α, Cell, 56, 37, 10.1016/0092-8674(89)90981-1 · DOI
  19. Hynes, 1987, Integrins: a family of cell surface receptors, Cell, 48, 549, 10.1016/0092-8674(87)90233-9 · DOI
  20. Isberg, 1989, Two determinants for Yersinia pseudotuberculosis cell binding and penetration detected in the absence of invasin, Infect. Immun., 57, 1998, 10.1128/IAI.57.7.1998-2005.1989 · DOI
  21. Isberg, 1985, A single genetic locus encoded by Yersinia pseudotuberculosis permits invasion of cultured animal cells by Escherichia coli K-12, Nature, 317, 262, 10.1038/317262a0 · DOI
  22. Isberg, 1987, Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells, Cell, 50, 769, 10.1016/0092-8674(87)90335-7 · DOI · Paper page
  23. Kishimoto, 1987, Cloning of the β subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family, Cell, 48, 681, 10.1016/0092-8674(87)90246-7 · DOI
  24. Kramer, 1989, Identification of integrin collagen receptors on human melanoma cells, J. Biol. Chem., 264, 4684, 10.1016/S0021-9258(18)83797-8 · DOI
  25. Matsudaira, 1987, Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes, J. Biol. Chem., 262, 10035, 10.1016/S0021-9258(18)61070-1 · DOI
  26. Maurelli, 1988, Genetic determinants of Shigella pathogenicity, Annu. Rev. Microbiol., 42, 127, 10.1146/annurev.mi.42.100188.001015 · DOI
  27. Messing, 1983, New M13 vectors for cloning, Meth. Enzymol., 101, 20, 10.1016/0076-6879(83)01005-8 · DOI
  28. Miller, 1988, Evidence for two genetic loci from Yersinia enterocolitica that can promote invasion of epithelial cells, Infect. Immun., 56, 1242, 10.1128/IAI.56.5.1242-1248.1988 · DOI
  29. Miller, 1988, Factors essential for penetration of mammalian cells by Yersinia, Curr. Topics Microbiol. Immunol., 138, 15
  30. Mimms, 1981, Phospholipid vesicle formation and transmembrane protein incorporation using octylglucoside, Biochemistry, 20, 833, 10.1021/bi00507a028 · DOI
  31. Obara, 1988, Site-directed mutagenesis of the cell-binding domain of human fibronectin: separable, synergistic sites mediate adhesive function, Cell, 53, 649, 10.1016/0092-8674(88)90580-6 · DOI
  32. Olsen, 1989, Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli, Nature, 338, 652, 10.1038/338652a0 · DOI
  33. Payne, 1987, Phagocytosis of Legionella pneumophila is mediated by human monocyte complement receptors, J. Exp. Med., 166, 1377, 10.1084/jem.166.5.1377 · DOI
  34. Pierschbacher, 1984, Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule, Nature, 309, 30, 10.1038/309030a0 · DOI
  35. Ross, 1985, Membrane complement receptor type three (CR3) has lectin-like properties analogous to bovine conglutinin and functions as a receptor for zymosan and rabbit erythrocytes as well as a receptor for iC3b, J. Immunol., 134, 3307, 10.4049/jimmunol.134.5.3307 · DOI
  36. Ruoslahti, 1988, Fibronectin and its receptors, Annu. Rev. Biochem., 57, 375, 10.1146/annurev.bi.57.070188.002111 · DOI
  37. Russell, 1988, Complement receptor type 3 (CR3) binds to an Arg-Gly-Asp-containing region of the major surface glycoprotein, gp63, of Leishmania promastigotes, J. Exp. Med., 168, 279, 10.1084/jem.168.1.279 · DOI
  38. Schenkman, 1988, Trypanosoma cruzi invade a mammalian epithelial cell in a polarized manner, Cell, 55, 157, 10.1016/0092-8674(88)90018-9 · DOI
  39. Staunton, 1989, Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1, Nature, 339, 61, 10.1038/339061a0 · DOI
  40. Takada, 1987, Fibronectin receptor structures in the VLA family of heterodimers, Nature, 326, 607, 10.1038/326607a0 · DOI
  41. Toivanen, 1988, Factors associated with the development of reactive arthritis, Br. J. Rheumatol., 27, 46, 10.1093/rheumatology/XXVII.suppl_2.46 · DOI
  42. Une, 1977, Studies on the pathogenicity of Yersinia enterocolitica: III. Comparative studies between Y. enterocolitica and Y. pseudotuberculosis, Microbiol. Immunol., 21, 505, 10.1111/j.1348-0421.1977.tb00316.x · DOI
  43. Van de Water, 1983, Fibronectin binds to some bacteria but does not promote their uptake by phagocytic cells, Science, 220, 201, 10.1126/science.6338594 · DOI
  44. Wayner, 1988, The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa, J. Cell Biol., 107, 1881, 10.1083/jcb.107.5.1881 · DOI
  45. Wright, 1985, Activation of phagocytic cells' C3 receptors for phagocytosis, J. Leukocyte Biol., 38, 327, 10.1002/jlb.38.2.327 · DOI

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Metadata

Authors
Isberg, R. R., & Leong, J. M.
Affiliations
Tufts University (US)
ORCID
Venue
Cell
Publisher
Elsevier BV
Published
1990-03
Volume
60
Issue
5
Pages
861-871
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/0092-8674(90)90099-z
OpenAlex
W1969540615
Cited by
798
References
0
Citations by year
2026: 6 · 2025: 7 · 2024: 6 · 2023: 12 · 2022: 10 · 2021: 11 · 2020: 12 · 2019: 11 · 2018: 13 · 2017: 12 · 2016: 15 · 2015: 12 · 2014: 18 · 2013: 14 · 2012: 25
FWCI
10.04
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation
  • National Institutes of Health
  • National Institute of Allergy and Infectious Diseases (R01AI023538, R01 AI 23538)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
invasin, integrins, beta1 integrin, Yersinia pseudotuberculosis, bacterial cell entry, non-phagocytic cells, alpha3beta1 integrin, alpha5beta1 integrin, alpha6beta1 integrin, cell adhesion receptors, bacterial adhesion
MeSH terms
Amino Acid Sequence, Bacterial Proteins, Blood Platelets, Humans, Kinetics, Liposomes, Molecular Sequence Data, Phosphatidylcholines, Yersinia pseudotuberculosis, Integrins, Adhesins, Bacterial, Macromolecular Substances

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