Budding of Marburgvirus is associated with filopodia

Kolesnikova, Larissa; Bohil, Aparna B.; Cheney, Richard E.; Becker, Stephan

doi:10.1111/j.1462-5822.2006.00842.x

Cited by 75 publications

(112 citation statements)

References 95 publications

(131 reference statements)

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“…Viral infection also caused extensive cytoskeletal changes which may have some bearing on normal synaptogenesis in vivo. In addition, actin cytoskeletal hijacking may be a common viral invasion strategy [18].…”

Section: Discussionmentioning

confidence: 99%

Herpes simplex virus type 1 induces filopodia in differentiated P19 neural cells to facilitate viral spread

Dixit

Tiwari

Shukla

2008

Neuroscience Letters

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Herpes simplex virus type-1 (HSV-1) is a neurotropic virus with significant potential as a viral vector for CNS gene therapy. This study provides visual evidence that recombinant green fluorescent protein (GFP) expressing HSV-1 travel down dendrites in differentiated P19 neuronal-like cells to efficiently reach the soma. The virus also promotes cytoskeletal rearrangements which facilitate viral spread in vitro, including often dramatic increases in dendritic filopodia. Viral movements, cell infection and filopodia induction were each reduced with the actin polymerization inhibitor cytochalasin D, suggesting the involvement of the actin cortex in these processes. The observation of neural cytoskeletal reorganization in response to HSV-1 may shed light on the mechanisms by which acute viral infection associated with herpes encephalitis produces cognitive deficits in patients.

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Section: Discussionmentioning

confidence: 99%

Herpes simplex virus type 1 induces filopodia in differentiated P19 neural cells to facilitate viral spread

Dixit

Tiwari

Shukla

2008

Neuroscience Letters

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“…Later in the replication cycle, NCs are detected in the cytosol, at the plasma membrane, and in filopodia, the preferred sites of MARV budding (12,13). The glycoprotein GP reaches the plasma membrane via vesicular secretory membrane traffic and is recruited to sites where viral protein VP40 accumulates (14,15).…”

mentioning

confidence: 99%

Live-cell imaging of Marburg virus-infected cells uncovers actin-dependent transport of nucleocapsids over long distances

Schudt

Kolesnikova

Dolnik

et al. 2013

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

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122

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Transport of large viral nucleocapsids from replication centers to assembly sites requires contributions from the host cytoskeleton via cellular adaptor and motor proteins. For the Marburg and Ebola viruses, related viruses that cause severe hemorrhagic fevers, the mechanism of nucleocapsid transport remains poorly understood. Here we developed and used live-cell imaging of fluorescently labeled viral and host proteins to characterize the dynamics and molecular requirements of nucleocapsid transport in Marburg virus-infected cells under biosafety level 4 conditions. The study showed a complex actin-based transport of nucleocapsids over long distances from the viral replication centers to the budding sites. Only after the nucleocapsids had associated with the matrix viral protein VP40 at the plasma membrane were they recruited into filopodia and cotransported with host motor myosin 10 toward the budding sites at the tip or side of the long cellular protrusions. Three different transport modes and velocities were identified: (i) Along actin filaments in the cytosol, nucleocapsids were transported at ∼200 nm/s; (ii) nucleocapsids migrated from one actin filament to another at ∼400 nm/s; and (iii) VP40-associated nucleocapsids moved inside filopodia at 100 nm/s. Unique insights into the spatiotemporal dynamics of nucleocapsids and their interaction with the cytoskeleton and motor proteins can lead to novel classes of antivirals that interfere with the trafficking and subsequent release of the Marburg virus from infected cells.dual-color imaging | reverse genetics | viral inclusion bodies T he filoviruses Marburg (MARV) and Ebola (EBOV) cause severe hemorrhagic fever with high-case-fatality rates in humans and nonhuman primates (1-3). Although the interplay of filoviral proteins leading to the transcription and replication of the viral genome and the formation of the viral nucleocapsids (NCs) is rather well understood, we are only just beginning to unravel the complex interactions between the viral and cellular proteins that are necessary to transport the NCs from the sites of their formation to the budding sites. The central protein within the NC is the nucleoprotein NP, which forms complexes with VP35, VP30, and VP24 (4, 5). The helical MARV NC is composed of the RNAdependent RNA polymerase (L), the polymerase cofactor VP35, the viral proteins VP30 and VP24, and NP, which encapsidates the viral genome (5-7). Within the viral particle, the NC is surrounded by a regular lattice of the matrix protein VP40 (5, 8, 9). The outside of the VP40 lattice contacts the viral envelope, in which the glycoprotein GP is inserted (10).MARV virogenesis begins with the formation of perinuclear inclusions which, analogous to the EBOV, are considered to be sites of viral replication and the assembly of new NCs (8, 9, 11). Later in the replication cycle, NCs are detected in the cytosol, at the plasma membrane, and in filopodia, the preferred sites of MARV budding (12, 13). The glycoprotein GP reaches the plasma membrane via vesicular se...

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“…Interestingly, marburgvirus NP also contains the late domain motif and interacts with Tsg101 [82], suggesting that NP may share transport pathways with VP40. It was indeed demonstrated that both VP40 and nucleocapsid were associated with cytoskeletal proteins such as actins in cytoplasmic transport [83][84][85][86]. Since VP40 is also detected in inclusion bodies along with NP and VP35 [68], it is of interest to clarify whether the nucleocapsid is trafficked to the assembly site alone or with VP40.…”

Section: Assembly/egressmentioning

confidence: 99%

“…It is assumed that majority of marburgvirus particles are released from the tips or sides of cellular filopodia [83]. It has been shown that actindependent molecular motor protein Myo10, which mediates intrafilopodial movement of proteins, is important for VP40-mediated vesicle release [83]. Similarly, IQGAP1, which is involved in cytoskeletal remodeling during cell migration and the formation of filopodia, interacts with ebolavirus VP40 and facilitates the release of virus-like particles [88].…”

Section: Assembly/egressmentioning

confidence: 99%

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Host Cell Factors Involved in Filovirus Infection

Kajihara

Takada

2015

Curr Trop Med Rep

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Filoviruses (ebolaviruses and marburgviruses) cause severe hemorrhagic fever in humans and nonhuman primates with high mortality rates of up to 90 %. The latest epidemic of Ebola virus disease in Western African countries has underscored the urgent need for effective prophylactic and therapeutic interventions for this deadly infectious disease. However, neither approved prophylactics nor therapeutics are currently available for filovirus diseases. Recent studies have been unveiling the molecular mechanisms underlying the filovirus lifecycle, including cellular entry, egress, and the evasion from host immunity, suggesting possibilities to develop effective pan-filovirus drugs.

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Budding of Marburgvirus is associated with filopodia

Cited by 75 publications

References 95 publications

Herpes simplex virus type 1 induces filopodia in differentiated P19 neural cells to facilitate viral spread

Herpes simplex virus type 1 induces filopodia in differentiated P19 neural cells to facilitate viral spread

Live-cell imaging of Marburg virus-infected cells uncovers actin-dependent transport of nucleocapsids over long distances

Host Cell Factors Involved in Filovirus Infection

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