Proximity proteomics identifies novel function of Rab14 in trafficking of Ebola virus matrix protein VP40

Fan, Jiannan; Liu, Xuechun; Mao, Feifei; Yue, Xihua; Lee, Intaek; Xu, Yingke

doi:10.1016/j.bbrc.2020.04.041

Cited by 14 publications

(14 citation statements)

References 32 publications

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“…It has been shown that some viruses use unconventional endocytosis, such as Herpes Simplex Virus 1 (Tebaldi et al, 2020), SARS-CoV (Castan ˜o-Rodriguez et al, 2018), Lassa virus, the Amr53b and We54 strains of LCMV (lymphocytic choriomeningitis virus) (Kunz, 2009;Pasqual et al, 2011;Quirin et al, 2008;Rojek et al, 2008), Lujo virus (Kunz and de la Torre, 2017;Raaben et al, 2017) and some influenza A strains (Wu et al, 2018) that appear to skip the early Rab5-positive endosomes. Rab14 also appears to be involved in viral trafficking, more specifically in the endocytosis of Ebola virus matrix protein VP40 (Fan et al, 2020). Additionally, Rab14 depletion delayed Candida albicans-containing phagosome maturation to Lamp1, even though Rab5 and Rab7 markers were still present during the maturation process (Okai et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

The endocytic pathway taken by cationic substances requires Rab14 but not Rab5 and Rab7

et al. 2021

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Section: Discussionmentioning

confidence: 99%

The endocytic pathway taken by cationic substances requires Rab14 but not Rab5 and Rab7

et al. 2021

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“…Fan et, al used proximity-dependent biotin-identification (BioID) to identify Rab14 GTPase as one of the interacting partners for eVP40. eVP40 colocalized with Rab14 when expressed in HeLa cells and in the absence of or with decreased Rab14, VP40 plasma membrane localization was diminished [ 21 ]. While less information on the mVP40 trafficking mechanism is available, mutation of a hydrophobic patch in the mVP40 CTD greatly diminished mVP40 plasma membrane localization [ 11 ].…”

Section: Filovirus Assembly and Buddingmentioning

confidence: 99%

“…Each has a distinct function required by the viral life cycle. The dimeric eVP40 is trafficked to the inner leaflet of the plasma membrane [21]. Once the dimers associate with the PM, they undergo structural rearrangements into an array of dimer-dimer interactions [9,18,22].…”

Section: Vp40 Traffickingmentioning

confidence: 99%

Lipid–protein interactions in virus assembly and budding from the host cell plasma membrane

Motsa

Stahelin

2021

Biochemical Society Transactions

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Lipid enveloped viruses contain a lipid bilayer coat that protects their genome to help facilitate entry into the new host cell. This lipid bilayer comes from the host cell which they infect. After viral replication, the mature virion hijacks the host cell plasma membrane where it is then released to infect new cells. This process is facilitated by the interaction between phospholipids that make up the plasma membrane and specialized viral matrix proteins. This step in the viral lifecycle may represent a viable therapeutic strategy for small molecules that aim to block enveloped virus spread. In this review, we summarize the current knowledge on the role of plasma membrane lipid–protein interactions on viral assembly and budding.

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“…Around 80% of the interactors have not been previously described, many of them are involved in critical cellular pathways relevant to the EBOV life cycle ( Figure 4A ). Twelve interactors were reported in other EBOV-protein interactomes ( Figure 4B ) (Fan et al, 2020; Garcia-Dorival et al, 2016; Morwitzer et al, 2019; Spurgers et al, 2010; Takahashi et al, 2013).…”

Section: Resultsmentioning

confidence: 99%

Functional interactomes of the Ebola virus polymerase identified by proximity proteomics in the context of viral replication

Fang

Pietzsch

Tsaprailis³

et al. 2021

Preprint

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Ebola virus (EBOV) critically depends on the viral polymerase to replicate and transcribe the viral RNA genome. To examine whether interactions between EBOV polymerase and cellular and viral factors affect distinct viral RNA synthesis events, we applied proximity proteomics to define the cellular interactome of EBOV polymerase, under conditions that recapitulate viral transcription and replication. We engineered EBOV polymerase tagged with the split-biotin ligase split-TurboID, which successfully biotinylated the proximal proteome while retaining polymerase activity. We further analyzed the interactomes in an siRNA-based, functional screen and uncovered 35 host factors, which, when depleted, affect EBOV infection. We validated one host factor, eukaryotic peptide chain release factor subunit 3a (eRF3a/GSPT1), which we show physically and functionally associates with EBOV polymerase to facilitate viral transcription termination. Our work demonstrates the utility of proximity proteomics to capture the functional host-interactome of the EBOV polymerase and to illuminate host-dependent regulations of viral RNA synthesis.

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Proximity proteomics identifies novel function of Rab14 in trafficking of Ebola virus matrix protein VP40

Cited by 14 publications

References 32 publications

The endocytic pathway taken by cationic substances requires Rab14 but not Rab5 and Rab7

The endocytic pathway taken by cationic substances requires Rab14 but not Rab5 and Rab7

Lipid–protein interactions in virus assembly and budding from the host cell plasma membrane

Functional interactomes of the Ebola virus polymerase identified by proximity proteomics in the context of viral replication

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