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. 2012 Apr 5;2(2):203-27.
doi: 10.3390/biom2020203.

Sumoylation at the host-pathogen interface

Affiliations

Sumoylation at the host-pathogen interface

Van G Wilson. Biomolecules. .

Abstract

Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own proteins, several viral pathogens have been shown to modulate overall host sumoylation levels. Given the large number of cellular targets for SUMO addition and the breadth of critical cellular processes that are regulated via sumoylation, viral modulation of overall sumoylation presumably alters the cellular environment to ensure that it is favorable for viral reproduction and/or persistence. Like some viruses, certain bacterial plant pathogens also target the sumoylation system, usually decreasing sumoylation to disrupt host anti-pathogen responses. The recent demonstration that Listeria monocytogenes also disrupts host sumoylation, and that this is required for efficient infection, extends the plant pathogen observations to a human pathogen and suggests that pathogen modulation of host sumoylation may be more widespread than previously appreciated. This review will focus on recent aspects of how pathogens modulate the host sumoylation system and how this benefits the pathogen.

Keywords: SIMs; SUMO; Virus; bacteria; immunity.

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Figures

Figure 1
Figure 1
Pathogens and the sumoylation pathway. The enzymology of the sumoylation is shown from the processing of the SUMO precursor to the final conjugation/deconjugation of substrates by the SUMO protease, SENP. Pathogen proteins that act at various steps in the sumoylation pathway are shown in boxes and are discussed in the text.

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References

    1. Yaniv M. Small DNA tumour viruses and their contributions to our understanding of transcription control. Virology. 2009;384:369–374. - PubMed
    1. Lazo P.A., Santos C.R. Interference with p53 functions in human viral infections, a target for novel antiviral strategies? Rev. Med. Virol. 2011;21:285–300. - PubMed
    1. Felsani A., Mileo A.M., Paggi M.G. Retinoblastoma family proteins as key targets of the small DNA virus oncoproteins. Oncogene. 2006;25:5277–5285. - PubMed
    1. Isaacson M.K., Ploegh H.L. Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection. Cell Host Microbe. 2009;5:559–570. doi: 10.1016/j.chom.2009.05.012. - DOI - PMC - PubMed
    1. Ohsumi Y. Molecular dissection of autophagy: Two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2001;2:211–216. - PubMed

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