Listeria en lutte avec SUMO

David Ribet; Pascale Cossart

doi:10.1051/medsci/2010265545

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Volume 26 / Numéro 5 (Mai 2010)

Med Sci (Paris), 26 5 (2010) 545-547

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Numéro		Med Sci (Paris) Volume 26, Numéro 5, Mai 2010


Page(s)		545 - 547
Section		Dernière heure
DOI		https://doi.org/10.1051/medsci/2010265545
Publié en ligne		15 mai 2010

Boggio R, Chiocca S. Viruses and sumoylation: recent highlights. Curr Opin Microbiol 2006; 9 : 430–6. [Google Scholar]
Boggio R, Colombo R, Hay RT, et al. A mechanism for inhibiting the SUMO pathway. Mol Cell 2004; 16 : 549–61. [Google Scholar]
Bonazzi M, Veiga E, Cerda JP, Cossart P. Successive post-translational modifications of E-cadherin are required for InlA-mediated internalisation of Listeria monocytogenes. Cell Microbiol 2008; 10 : 2208–22. [Google Scholar]
Chang PC, Izumiya Y, Wu CY, et al. 2010. Kaposi’s sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific. J Biol Chem 2010; 285 : 5266–73. [Google Scholar]
Chang TH, Kubota T, Matsuoka M, et al. Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PLoS Pathog 2009; 5 : e1000493. [Google Scholar]
Cossart P, Toledo-Arana A. Listeria monocytogenes, a unique model in infection biology: an overview. Microbes Infect 2008; 10 : 1041–50. [Google Scholar]
Geiss-Friedlander R, Melchior F. Concepts in sumoylation: a decade on. Nat Rev Mol Cell Biol 2007; 8 : 947–56. [Google Scholar]
Hamon MA, Batsche E, Regnault B, et al. Histone modifications induced by a family of bacterial toxins. Proc Natl Acad Sci USA 2007; 104 : 13467–72. [Google Scholar]
Ribet D, Hamon M, Gouin E, et al. Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 2010; 464 : 1192–5. [Google Scholar]
Saitoh H, Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 2000; 275 : 6252–8. [Google Scholar]
Schnupf P, Portnoy DA. Listeriolysin O: a phagosome-specific lysin. Microbes Infect 2007; 9 : 1176–87. [Google Scholar]
Veiga E, Cossart P. Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat Cell Biol 2005; 7 : 894–900. [Google Scholar]

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[1] Boggio R, Chiocca S. Viruses and sumoylation: recent highlights. Curr Opin Microbiol 2006; 9 : 430–6. [Google Scholar]

[2] Boggio R, Colombo R, Hay RT, et al. A mechanism for inhibiting the SUMO pathway. Mol Cell 2004; 16 : 549–61. [Google Scholar]

[3] Bonazzi M, Veiga E, Cerda JP, Cossart P. Successive post-translational modifications of E-cadherin are required for InlA-mediated internalisation of Listeria monocytogenes. Cell Microbiol 2008; 10 : 2208–22. [Google Scholar]

[4] Chang PC, Izumiya Y, Wu CY, et al. 2010. Kaposi’s sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific. J Biol Chem 2010; 285 : 5266–73. [Google Scholar]

[5] Chang TH, Kubota T, Matsuoka M, et al. Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PLoS Pathog 2009; 5 : e1000493. [Google Scholar]

[6] Cossart P, Toledo-Arana A. Listeria monocytogenes, a unique model in infection biology: an overview. Microbes Infect 2008; 10 : 1041–50. [Google Scholar]

[7] Geiss-Friedlander R, Melchior F. Concepts in sumoylation: a decade on. Nat Rev Mol Cell Biol 2007; 8 : 947–56. [Google Scholar]

[8] Hamon MA, Batsche E, Regnault B, et al. Histone modifications induced by a family of bacterial toxins. Proc Natl Acad Sci USA 2007; 104 : 13467–72. [Google Scholar]

[9] Ribet D, Hamon M, Gouin E, et al. Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 2010; 464 : 1192–5. [Google Scholar]

[10] Saitoh H, Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 2000; 275 : 6252–8. [Google Scholar]

[11] Schnupf P, Portnoy DA. Listeriolysin O: a phagosome-specific lysin. Microbes Infect 2007; 9 : 1176–87. [Google Scholar]

[12] Veiga E, Cossart P. Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat Cell Biol 2005; 7 : 894–900. [Google Scholar]