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2010 | 15 | 3 |

Tytuł artykułu

Integrin receptors play a role in the internalin B-dependent entry of Listeria monocytogenes into host cells

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Listeria monocytogenes enters non-phagocytic cells by binding its surface proteins inlA (internalin) and inlB to the host’s E-cadherin and Met, respectively. The two internalins play either separate or cooperative roles in the colonization of infected tissues. Here, we studied bacterial uptake into HeLa cells using an L. monocytogenes mutant strain (ΔinlA) carrying a deletion in the gene coding for inlA. The ΔinlA mutant strain showed the capability to invade HeLa cells. The monoclonal anti-β3- and anti-β1-integrin subunit antibodies prevented bacterial uptake into the cells, while the anti-β2- and anti-β4-integrin subunit antibodies failed to affect L. monocytogenes entry into HeLa cells. Three structurally distinct disintegrins (kistrin, echistatin and flavoridin) also inhibited bacterial uptake, showing different potencies correlated to their selective affinity for the β3- and β1-integrin subunits. In addition to inducing Met phosphorylation, infection of cells by the L. monocytogenes ΔinlA mutant strain promoted the tyrosine phosphorylation of the focal adhesion-associated proteins FAK and paxillin. Our findings provide the first evidence that β3- and β1-integrin receptors play a role in the inlB-dependent internalization of L. monocytogenes into host cells.

Wydawca

-

Rocznik

Tom

15

Numer

3

Opis fizyczny

p.496-506,fig.,ref.

Twórcy

autor
  • Istituto Zooprofilattico Sperimentale del Mezzogiorno, via Della Salute 2, 80055, Portici, Italy
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Bibliografia

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  • 3. Bierne, H., Sabet, C., Personnic, N. and Cossart, P. Internalins: a complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes. Microbes Infect. 9 (2007) 1156-1166.
  • 4. Mengaud, J., Ohayon, H., Gounon, P., Mege, R-M. and Cossart P. E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84 (1996) 923-932.
  • 5. Bonazzi, M., Lecuit, M. and Cossart, P. Listeria monocytogenes internalin and E-cadherin: from structure to pathogenesis. Cell. Microbiol. 11 (2009) 693-702.
  • 6. Shen, Y., Naujokas, M., Park, M. and Ireton K. InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103 (2000) 501-510.
  • 7. Pizarro-Cerdá, J., Sousa, S. and Cossart, P. Exploitation of host cell cytoskeleton and signalling during Listeria monocytogenes entry into mammalian cells. C. R. Biol. 327 (2004) 115-123.
  • 8. Cossart, P. Met, the HGF-SF receptor: another receptor for Listeria monocytogenes. Trends Microbiol. 9 (2001) 105-107.
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  • 10. Trusolino, L., Bertotti, A. and Comoglio P.M. A signaling adapter function for alpha6beta4 integrin in the control of HGF-dependent invasive growth. Cell 107 (2001) 643-654.
  • 11. Streuli, C.H. and Akhtar, N. Signal co-operation between integrins and other receptor systems. Biochem. J. 418 (2009) 491-506.
  • 12. Hynes, R.O. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687.
  • 13. Sastry, S.K. and Burridge, K. Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics. Exp. Cell Res. 261 (2000) 25-36.
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  • 15. Vicente-Manzanares, M., Choi, C.K. and Horwitz, A.R. Integrins in cell migration-the actin connection. J. Cell Sci. 122 (2009) 199-206.
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  • 17. Scibelli, A., Roperto, S., Manna, L., Pavone, L.M., Tafuri, S., Della Morte, R. and Staiano, N. Engagement of integrins as a cellular route of invasion by bacterial pathogens. Vet. J. 173 (2007) 482-491.
  • 18. Kwok, T., Zabler, D., Urman, S., Rohde, M., Hartig, R., Wessler, S., Misselwitz, R., Berger, J., Sewald, N., König, W. and Backert, S. Helicobacter exploits integrin for type IV secretion and kinase activation. Nature 449 (2007) 862-866.
  • 19. Bergmann, B., Raffelsbauer, D., Kuhn, M., Goetz, M., Hom, S. and Goebel, W. InlA- but not InlB-mediated internalization of Listeria monocytogenes by non-phagocytic mammalian cells needs the support of other internalins. Mol. Microbiol. 43 (2002) 557-570.
  • 20. McLane, M.A., Marcinkiewicz, C., Vijay-Kumar, S., WierzbickaPatynowski, I. and Niewiarowski, S. Viper venom disintegrins and related molecules. Proc. Soc. Exp. Biol. Med. 219 (1998) 109-119.
  • 21. Scibelli, A., Matteoli, G., Roperto, S., Alimenti, E., Dipineto, L., Pavone, L.M., Della Morte, R., Menna, L.F., Fioretti, A. and Staiano, N. Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells. FEMS Microbiol. Lett. 247 (2005) 51-57.
  • 22. Lu, X., Lu, D., Scully, M.F. and Kakkar, V.V. Modulation of integrinbinding selectivity by mutation within the RGD-loop of snake venom proteins: a novel drug development approach. Curr. Med. Chem. Cardiovasc. Hematol. Agents 1 (2003) 89-196.
  • 23. Senn, H. and Klaus, W. The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor. J. Mol. Biol. 232 (1993) 907-925.
  • 24. Schaller, M.D. Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim. Biophys. Acta 1540 (2001) 1-21.
  • 25. Hamadi, A., Bouali, M., Dontenwill, M., Stoeckel, H., Takeda, K. and Rondé, P. Regulation of focal adhesion dynamics and disassembly by phosphorylation of FAK at tyrosine 397. J. Cell Sci. 118 (2005) 4415-4425.
  • 26. Staiano, N., Garbi, C., Squillacioti, C., Esposito, S., Di Martino, E., Belisario, M.A., Nitsch, L. and Di Natale, P. Echistatin induces decrease of pp125FAK phosphorylation, disassembly of actin cytoskeleton and focal adhesions, and detachment of fibronectin-adherent melanoma cells. Eur. J. Cell Biol. 73 (1997) 298-305.
  • 27. Della Morte, R., Squillacioti, C., Garbi, C., Derkinderen, P., Belisario, M.A., Girault, J.A., Di Natale, P., Nitsch, L. and Staiano, N. Echistatin inhibits pp125FAK autophosphorylation, paxillin phosphorylation and pp125FAKpaxillin interaction in fibronectin-adherent melanoma cells. Eur. J. Biochem. 267 (2000) 5047-5054.
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  • 29. McCall-Culbreath, K. D., Li, Z. and Zutter, M.M. Crosstalk between the alpha2beta1 integrin and c-met/HGF-R regulates innate immunity. Blood 111 (2008) 3562-3570.
  • 30. Cabodi, S., Moro, L., Bergatto, E., Boeri Erba, E., Di Stefano, P., Turco, E., Tarone, G. and Defilippi, P. Integrin regulation of epidermal growth factor (EGF) receptor and of EGF-dependent responses. Biochem. Soc. Trans. 32 (2004) 438-442.

Typ dokumentu

Bibliografia

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