Target silencing of components of the conserved oligomeric Golgi complex impairs HIV-1 replication

Liu, Sicen; Dominska-Ngowe, Monika; Dykxhoorn, Derek M.

doi:10.1016/j.virusres.2014.08.015

Cited by 13 publications

(16 citation statements)

References 79 publications

(115 reference statements)

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“…COG functions have been previously linked to Chlamydia trachomatis intracellular growth (Pokrovskaya et al, 2012) and HIV replication (Liu et al, 2014), yet no microbial effector was known to directly target this MTC. Through its interactions with many vesicular trafficking and fusion machinery proteins (Willett et al, 2013), the COG complex controls multiple aspects of Golgi-associated membrane trafficking, making it an ideal target for a bacterial effector to coordinately modulate various secretory trafficking stages.…”

Section: Discussionmentioning

confidence: 99%

A Brucella Type IV Effector Targets the COG Tethering Complex to Remodel Host Secretory Traffic and Promote Intracellular Replication

Miller

Smith

Cundiff

et al. 2017

Cell Host & Microbe

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Summary Many intracellular pathogens exploit host secretory trafficking to support their intracellular cycle, but knowledge of these pathogenic processes is limited. The bacterium Brucella abortus uses a Type IV secretion system (VirB T4SS) to generate a replication-permissive Brucella-containing vacuole (rBCV) derived from the host endoplasmic reticulum (ER), a process that requires host early secretory trafficking. Here we show that the VirB T4SS effector BspB contributes to rBCV biogenesis and Brucella replication by interacting with the Conserved Oligomeric Golgi (COG) tethering complex, a major coordinator of Golgi vesicular trafficking, thus remodeling Golgi membrane traffic and redirecting Golgi-derived vesicles to the BCV. Altogether, these findings demonstrate that Brucella modulates COG-dependent trafficking via delivery of a T4SS effector to promote rBCV biogenesis and intracellular proliferation, providing mechanistic insight into how bacterial exploitation of host secretory functions promotes pathogenesis.

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Section: Discussionmentioning

confidence: 99%

A Brucella Type IV Effector Targets the COG Tethering Complex to Remodel Host Secretory Traffic and Promote Intracellular Replication

Miller

Smith

Cundiff

et al. 2017

Cell Host & Microbe

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“…Syntaxins are also involved in cellular trafficking by DNA viruses [ 72 , 73 , 74 ]. Silencing of syntaxin 5, a Golgi SNARE, inhibited the reverse transcription step in HIV infection [ 75 ]. Altogether, all these works support the emerging significance of co-opted SNARE proteins during viral infections.…”

Section: Discussionmentioning

confidence: 99%

Assembly-hub function of ER-localized SNARE proteins in biogenesis of tombusvirus replication compartment

et al. 2018

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Positive-strand RNA viruses assemble numerous membrane-bound viral replicase complexes within large replication compartments to support their replication in infected cells. Yet the detailed mechanism of how given subcellular compartments are subverted by viruses is incompletely understood. Although, Tomato bushy stunt virus (TBSV) uses peroxisomal membranes for replication, in this paper, we show evidence that the ER-resident SNARE (soluble NSF attachment protein receptor) proteins play critical roles in the formation of active replicase complexes in yeast model host and in plants. Depletion of the syntaxin 18-like Ufe1 and Use1, which are components of the ER SNARE complex in the ERAS (ER arrival site) subdomain, in yeast resulted in greatly reduced tombusvirus accumulation. Over-expression of a dominant-negative mutant of either the yeast Ufe1 or the orthologous plant Syp81 syntaxin greatly interferes with tombusvirus replication in yeast and plants, thus further supporting the role of this host protein in tombusvirus replication. Moreover, tombusvirus RNA replication was low in cell-free extracts from yeast with repressed Ufe1 or Use1 expression. We also present evidence for the mislocalization of the tombusviral p33 replication protein to the ER membrane in Ufe1p-depleted yeast cells. The viral p33 replication protein interacts with both Ufe1p and Use1p and co-opts them into the TBSV replication compartment in yeast and plant cells. The co-opted Ufe1 affects the virus-driven membrane contact site formation, sterol-enrichment at replication sites, recruitment of several pro-viral host factors and subversion of the Rab5-positive PE-rich endosomes needed for robust TBSV replication. In summary, we demonstrate a critical role for Ufe1 and Use1 SNARE proteins in TBSV replication and propose that the pro-viral functions of Ufe1 and Use1 are to serve as assembly hubs for the formation of the extensive TBSV replication compartments in cells. Altogether, these findings point clearly at the ERAS subdomain of ER as a critical site for the biogenesis of the TBSV replication compartment.

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“…Another intracellular pathogen, Brucella abortus , also interacts with the COG complex via BspB protein, likely redirecting Golgi‐derived vesicles to Brucella‐containing vacuoles . Additionally, the infectivity and/or life cycle of numerous viruses (HIV, Chikungunya Virus, Hepatitis C, Dengue) and toxins (typhoid toxin, SubAB, Cholera toxin, Shiga toxin) somehow depends on COG complex's activity . How have these diverse groups of pathogens evolved to rely on COG function?…”

Section: Further Questions and Perspectivesmentioning

confidence: 99%

Maintaining order: COG complex controls Golgi trafficking, processing, and sorting

2019

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The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG‐congenital disorders of glycosylation (COG‐CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra‐Golgi trafficking, namely SNAREs, SNARE‐interacting proteins, Rabs, coiled‐coil tethers, and vesicular coats. Here, we review our current knowledge of COG‐related trafficking and glycosylation defects in humans and model organisms, and analyze possible scenarios for the molecular mechanism of the COG orchestrated vesicle targeting.

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Target silencing of components of the conserved oligomeric Golgi complex impairs HIV-1 replication

Cited by 13 publications

References 79 publications

A Brucella Type IV Effector Targets the COG Tethering Complex to Remodel Host Secretory Traffic and Promote Intracellular Replication

A Brucella Type IV Effector Targets the COG Tethering Complex to Remodel Host Secretory Traffic and Promote Intracellular Replication

Assembly-hub function of ER-localized SNARE proteins in biogenesis of tombusvirus replication compartment

Maintaining order: COG complex controls Golgi trafficking, processing, and sorting

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