Structural Aspects of Adhesion to and Invasion of Host Cells by the Human Pathogen Listeria monocytogenes

ChemBioChemVolume 4, Issue 12 p. 1285-1291 Minireview Structural Aspects of Adhesion to and Invasion of Host Cells by the Human Pathogen Listeria monocytogenes Wolf-Dieter Schubert Dr., Wolf-Dieter Schubert Dr. Department of Structural Biology, German Research Center for Biotechnology (GBF), Mascheroder Weg 1, 38124 Braunschweig, Germany, Fax: (+49) 531-6181-763Search for more papers by this authorDirk W. Heinz Prof. Dr., Dirk W. Heinz Prof. Dr. [email protected] Department of Structural Biology, German Research Center for Biotechnology (GBF), Mascheroder Weg 1, 38124 Braunschweig, Germany, Fax: (+49) 531-6181-763Search for more papers by this author Wolf-Dieter Schubert Dr., Wolf-Dieter Schubert Dr. Department of Structural Biology, German Research Center for Biotechnology (GBF), Mascheroder Weg 1, 38124 Braunschweig, Germany, Fax: (+49) 531-6181-763Search for more papers by this authorDirk W. Heinz Prof. Dr., Dirk W. Heinz Prof. Dr. [email protected] Department of Structural Biology, German Research Center for Biotechnology (GBF), Mascheroder Weg 1, 38124 Braunschweig, Germany, Fax: (+49) 531-6181-763Search for more papers by this author First published: 24 November 2003 https://doi.org/10.1002/cbic.200300624Citations: 14Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Graphical Abstract Molecular Infection. Listeria monocytogenes, a widespread contaminant of processed food, infects both humans and other mammals by the oral route. The first dedicated step of the infection process is the recognition of human E-cadherin (purple) by the listerial protein internalin (InlA, yellow-green). The bacterium thereby adheres to the epithelial lining of the intestine. It then induces its own uptake into the host cells, where it finds ideal conditions to multiply and spread to neighboring cells. The affinity of InlA for E-cadherin, controlled by Ca2+ (orange sphere), is fine-tuned to allow complex formation in the intestinal lumen and dissociation when uptake has occurred to release the bacterium into the epithelial cell. References 1 J. A. Vazquez-Boland, M. Kuhn, P. Berche, T. Chakraborty, G. Dominguez-Bernal, W. Goebel, B. Gonzalez-Zorn, J. Wehland, J. Kreft, Clin. Microbiol. Rev. 2001, 14, 584–640. 2 P. Glaser, L. Frangeul, C. Buchrieser, C. Rusniok, A. Amend, F. Baquero, P. Berche, H. Bloecker, P. Brandt, T. Chakraborty, A. Charbit, F. Chetouani, E. Couvé, A. de Daruvar, P. Dehoux, E. Domann, G. Domínguez-Bernal, E. Duchaud, L. Durant, O. Dussurget, K.-D. Entian, H. Fsihi, F. Garcia-Del Portillo, P. Garrido, L. Gautier, W. Goebel, N. Gómez-López, T. Hain, J. Hauf, D. Jackson, L.-M. Jones, U. Kaerst, J. Kreft, M. Kuhn, F. Kunst, G. Kurapkat, E. Madueño, A. Maitournam, J. Mata Vicente, E. Ng, H. Nedjari, G. Nordsiek, S. Novella, B. de Pablos, J.-C. Pérez-Diaz, R. Purcell, B. Remmel, M. Rose, T. Schlueter, N. Simoes, A. Tierrez, J.-A. Vázquez-Boland, H. Voss, J. Wehland, P. Cossart, Science 2001, 294, 849–852. 3 J. M. Farber, P. I. Peterkin, Microbiol. Rev. 1991, 55, 476–511. 4 J. L. Gaillard, P. Berche, C. Frehel, E. Gouin, P. Cossart, Cell 1991, 65, 1127–1141. 5 D. Cabanes, P. Dehoux, O. Dussurget, L. Frangeul, P. Cossart, Trends Microbiol. 2002, 10, 238–245. 6 R. Jonquieres, H. Bierne, F. Fiedler, P. Gounon, P. Cossart, Mol. Microbiol. 1999, 34, 902–914. 7 B. Bergmann, D. Raffelsbauer, M. Kuhn, M. Goetz, S. Hom, W. Goebel, Mol. Microbiol. 2002, 43, 557–570. 8 J. Mengaud, H. Ohayon, P. Gounon, R. M. Mege, P. Cossart, Cell 1996, 84, 923–932. 9 S. Dramsi, P. Cossart, J. Cell Biol. 2002, 156, 943–946. 10 P. Cossart, H. Bierne, Curr. Opin. Immunol. 2001, 13, 96–103. 11 L. P. Cousins, E. J. Wing, Immunol. Rev. 2000, 174, 150–159. 12 H. Bierne, P. Cossart, J. Cell Sci. 2002, 115, 3357–3367. 13 C. Garandeau, H. Reglier-Poupet, I. Dubail, J. L. Beretti, P. Berche, A. Charbit, Infect. Immun. 2002, 70, 1382–1390. 14 H. Bierne, S. K. Mazmanian, M. Trost, M. G. Pucciarelli, G. Liu, P. Dehoux, L. Jänsch, F. Garcia-del Portillo, O. Schneewind, P. Cossart, Mol. Microbiol. 2002, 43, 869–881. 15 E. Domann, S. Zechel, A. Lingnau, T. Hain, A. Darji, T. Nichterlein, J. Wehland, T. Chakraborty, Infect. Immun. 1997, 65, 101–109. 16 S. Dramsi, P. Dehoux, M. Lebrun, P. L. Goossens, P. Cossart, Infect. Immun. 1997, 65, 1615–1625. 17 D. Raffelsbauer, A. Bubert, F. Engelbrecht, J. Scheinpflug, A. Simm, J. Hess, S. H. E. Kaufmann, W. Goebel, Mol. Gen. Genet. 1998, 260, 144–158. 18 M. Marino, L. Braun, P. Cossart, P. Ghosh, Mol. Cell 1999, 4, 1063–1072. 19 W.-D. Schubert, C. Urbanke, T. Ziehm, V. Beier, M. P. Machner, E. Domann, J. Wehland, T. Chakraborty, D. W. Heinz, Cell 2002, 111, 825–836. 20 M. Marino, M. Banerjee, R. Jonquieres, P. Cossart, P. Ghosh, EMBO J. 2002, 21, 5623–5634. 21 B. Kobe, A. V. Kajava, Curr. Opin. Struc. Biol. 2001, 11, 725–732. 22 B. Kobe, J. Deisenhofer, Nature 1993, 366, 751–756. 23 W.-D. Schubert, G. Göbel, M. Diepholz, A. Darji, D. Kloer, T. Hain, T. Chakraborty, J. Wehland, E. Domann, D. W. Heinz, J. Mol. Biol. 2001, 312, 783–794. 24 A. G. Evdokimov, D. E. Anderson, K. M. Routzahn, D. S. Waugh, J. Mol. Biol. 2001, 312, 807–821. 25 B. D. Angst, C. Marcozzi, A. I. Magee, J. Cell. Sci. 2001, 114, 629–641. 26 A. H. Huber, W. I. Weis, Cell 2001, 105, 391–402. 27 L. Shapiro, A. M. Fannon, P. D. Kwong, A. Thompson, M. S. Lehmann, G. Grubel, J. F. Legrand, J. Als-Nielsen, D. R. Colman, W. A. Hendrickson, Nature 1995, 374, 327–337. 28 M. Overduin, T. S. Harvey, S. Bagby, K. I. Tong, P. Yau, M. Takeichi, M. Ikura, Science 1995, 267, 386–389. 29 T. J. Boggon, J. Murray, S. Chappuis-Flament, E. Wong, B. M. Gumbiner, L. Shapiro, Science 2002, 296, 1308–1313. 30 A. H. Huber, D. B. Stewart, D. V. Laurents, W. J. Nelson, W. I. Weis, J. Biol. Chem. 2001, 276, 12 301–12 309. 31 A. S. Yap, W. M. Brieher, B. M. Gumbiner, Annu. Rev. Cell Dev. Biol. 1997, 13, 119–146. 32 A. Nagafuchi, Curr. Opin. Cell Biol. 2001, 13, 600–603. 33 M. Lecuit, S. Dramsi, C. Gottardi, M. Fedor-Chaiken, B. Gumbiner, P. Cossart, EMBO J. 1999, 18, 3956–3963. 34 M. Lecuit, S. Vandormael-Pournin, J. Lefort, M. Huerre, P. Gounon, C. Dupuy, C. Babinet, P. Cossart, Science 2001, 292, 1722–1725. 35 O. Pertz, D. Bozic, A. W. Koch, C. Fauser, A. Brancaccio, J. Engel, EMBO J. 1999, 18, 1738–1747. 36 B. Kobe, J. Deisenhofer, Nature 1995, 374, 183–186. 37 A. C. Papageorgiou, R. Shapiro, K. R. Acharya, EMBO J. 1997, 16, 5162–5177. 38 S. Pokutta, K. Herrenknecht, R. Kemler, J. Engel, Eur. J. Biochem. 1994, 223, 1019–1026. 39 B. Nagar, M. Overduin, M. Ikura, J. M. Rini, Nature 1996, 380, 360–364. 40 P. Cossart, J. Pizarro-Cerda, M. Lecuit, Trends Cell Biol. 2003, 13, 23–31. 41 C. R. Roy, F. Gisou van der Goot, Nature Cell Biol. 2003, 5, 16–19. 42 Z. A. Hamburger, M. S. Brown, R. R. Isberg, P. J. Borkman, Science 1999, 286, 291–295. 43 U. Schwarz-Linek, J. M. Werner, A. R. Pickford, S. Gurusiddappa, J. H. Kim, E. S. Pilka, J. A. Briggs, T. S. Gough, M. Hook, I. D. Campbell, J. R. Potts, Nature 2003, 423, 177–181. 44 S. Dramsi, I. Biswas, E. Maguin, L. Braun, P. Mastroeni, P. Cossart, Mol. Microbiol. 1995, 16, 251–261. 45 L. Braun, S. Dramsi, P. Dehoux, H. Bierne, G. Lindahl, P. Cossart, Mol. Microbiol. 1997, 25, 285–294. 46 L. Braun, H. Ohayon, P. Cossart, Mol. Microbiol. 1998, 27, 1077–1087. 47 K. Ireton, B. Payrastre, H. Chap, W. Ogawa, H. Sakaue, M. Kasuga, P. Cossart, Science 1996, 274, 780–782. 48 S. K. Parida, E. Domann, M. Rohde, S. Müller, A. Darji, T. Hain, J. Wehland, T. Chakraborty, Mol. Biobiol. 1998, 28, 81–93. 49 L. Greiffenberg, W. Goebel, K. S. Kim, I. Weiglein, A. Bubert, F. Engelbrecht, M. Stins, M. Kuhn, Infect. Immun. 1998, 66, 5260–5267. 50 J. L. Gaillard, F. Jaubert, P. Berche, J. Exp. Med. 1996, 183, 359–369. 51 Y. Shen, M. Naujokas, M. Park, K. Ireton, Cell 2000, 103, 501–510. 52 S. Giordano, M. F. Di Renzo, R. P. Narsimhan, C. S. Cooper, C. Rosa, P. M. Comoglio, Oncogene 1989, 4, 1383–1388. 53 L. Braun, F. Nato, B. Payrastre, J. C. Mazie, P. Cossart, Mol. Microbiol. 1999, 34, 10–23. 54 M. P. Machner, S. Frese, H. H. Niemann, W.-D. Schubert, V. Orian-Rousseau, J. Wehland, D. W. Heinz, Mol. Microbiol. 2003, 48, 1525–1536. 55 M. Komada, K. Miyazawa, T. Ishii, N. Kitamura, Eur. J. Biochem. 1992, 204, 857–864. 56 H. Tajima, O. Higuchi, K. Mizuno, T. Nakamura, J. Biochem. 1992, 111, 401–406. 57 L. Braun, B. Ghebrehiwet, P. Cossart, EMBO J. 2000, 19, 1458–1466. 58 R. Jonquieres, J. Pizarro-Cerda, P. Cossart, Mol. Microbiol. 2001, 42, 955–965. 59 L. G. Tilney, D. A. Portnoy, J. Cell Biol. 1989, 109, 1597–1608. 60 P. J. Kraulis, J. Appl. Crystallogr. 1991, 24, 946–950. 61 A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 1993, 64, A166. 62 E. A. Merritt, D. J. Bacon, Methods Enzymol. 1997, 277, 505–524. 63 A. Musacchio, M. Saraste, M. Wilmanns, Nat. Struct. Biol. 1994, 1, 546–551. Citing Literature Volume4, Issue12December 5, 2003Pages 1285-1291 ReferencesRelatedInformation