AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

Sakaguchi, Takemasa; Kato, Atsushi; Sugahara, Fumihiro; Shimazu, Yukie; Inoue, Makoto; Kiyotani, Katsuhiro; Nagai, Yoshinori; Yoshida, Takemi

doi:10.1128/jvi.79.14.8933-8941.2005

Cited by 80 publications

(90 citation statements)

References 50 publications

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“…Finally, ESCRT-III recruits the ATPase Vps4, which disassembles membrane-associated ESCRT complexes and thus allows further rounds of MVB sorting (19,20). Catalytic site mutants of Vps4 inhibit not only MVB sorting but also the L domain-mediated budding of HIV-1 and several other enveloped viruses (4,(21)(22)(23)(24)(25)(26), strongly supporting the notion that L domains function by engaging the MVB sorting machinery.…”

mentioning

confidence: 71%

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

Zamborlini

Usami²,

Radoshitzky³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

164

214

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The endosomal sorting complex ESCRT-III, which is formed by the structurally related CHMP proteins, is engaged by HIV-1 to promote viral budding. Here we show that progressive truncations into the C-terminal acidic domains of CHMP proteins trigger an increasingly robust anti-HIV budding activity. Together with biochemical evidence for specific intramolecular interactions between the basic and acidic halves of CHMP3 and CHMP4B, these results suggest that the acidic domains are autoinhibitory. The acidic half of CHMP3 also interacts with the endosome-associated ubiquitin isopeptidase AMSH, and the coexpression of AMSH or its CHMP3-binding domain converts wild-type CHMP3 into a potent inhibitor of HIV-1 release. Point mutations in CHMP3 that prevent binding to AMSH abrogate this effect, suggesting that binding to AMSH relieves the autoinhibition of CHMP3. Collectively, our results indicate that CHMP proteins are regulated through an autoinhibitory switch mechanism that allows tight control of ESCRT-III assembly.AMSH ͉ endosomal sorting machinery ͉ viral budding

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mentioning

confidence: 71%

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

Zamborlini

Usami²,

Radoshitzky³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

164

214

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“…MVB functions have been similarly implicated in budding by other enveloped RNA viruses, including other retroviruses (28)(29)(30)(31)(32)(33), rhabdoviruses (34), filoviruses (22,35,36), arenaviruses (37,38), paramyxoviruses (39,40), and probably also orthomyxoviruses (41). Therefore, host MVB machinery may be widely exploited for viral budding.…”

Section: H Epatitis B Virus (Hbv) Chronically Infects 350 Millionmentioning

confidence: 99%

Involvement of host cellular multivesicular body functions in hepatitis B virus budding

Watanabe

Sorensen

Naito

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

238

247

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Hepatitis B virus (HBV) is a major human pathogen that chronically infects Ϸ350 million people, causing liver disease and liver cancer. HBV virions bud into an endoplasmic reticulum (ER)-associated intracellular compartment, but the mechanisms of HBV assembly, budding, and release remain poorly understood. Budding of retroviruses and some other enveloped RNA viruses from plasma membranes requires host functions involved in protein sorting into late endosomal multivesicular bodies (MVBs). To determine whether budding of DNA-containing HBV virions at intracellular membranes also involves MVB functions, we used immunofluorescence to show that, in human hepatoma cells, HBV envelope protein colocalizes with MVB proteins AIP1/ALIX and VPS4B. We also found that a dominant negative (DN) AIP1 mutant inhibited production and/or release of enveloped virions without significant effects on intracellular nucleocapsid formation, whereas DN VPS4B inhibited both nucleocapsid production and budding. By contrast, DN AIP1 and VPS4 had no effect on the efficiency of release of enveloped, nucleocapsid-lacking HBV subviral particles, which are produced in vast excess over virions, and dramatically increased the release of unenveloped, naked nucleocapsids by an apparently nonlytic route. Thus, host MVB functions are required for efficient budding and release of enveloped HBV virions and may be a valuable target for HBV control. Moreover, HBV enveloped virions, enveloped subviral particles, and unenveloped nucleocapsids are all released by distinct pathways with separate host factor requirements.antiviral control ͉ hepadnavirus ͉ vacuolar protein sorting ͉ virus replication ͉ virus-host interaction

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“…Although several closely related paramyxoviruses share this motif, its importance in these viruses has yet to be demonstrated. In addition, yeast-two hybrid and co-precipitation experiments have suggested that the SeV C protein binds AIP1/Alix and appears to possess L-domain activity, however deletion and mutagenesis studies have failed to identify a sequence motif and the enhancement of VLP or virus production is limited to 2-to 3-fold (108).…”

Section: Late Budding Domainsmentioning

confidence: 99%

The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis

Patch¹

2007

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The author hereby certifies that the use of any copyrighted material in the thesis manuscript entitled:"The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis" is appropriately acknowledged and, beyond brief excerpts, is with the permission of the copyright owner. Additionally, NiV M contains a sequence that is important for budding and appears to serve as an L-domain. These findings further our understanding of paramyxovirus particle assembly in general and could help facilitate the development of a novel vaccine approach for henipaviruses.ii

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AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

Cited by 80 publications

References 50 publications

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

Involvement of host cellular multivesicular body functions in hepatitis B virus budding

The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis

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