Vaccinia Virus F13L Protein with a Conserved Phospholipase Catalytic Motif Induces Colocalization of the B5R Envelope Glycoprotein in Post-Golgi Vesicles

Husain, Matloob; Moss, Bernard

doi:10.1128/jvi.75.16.7528-7542.2001

Cited by 50 publications

(68 citation statements)

References 72 publications

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“…Under similar transfection conditions, the B5R protein was targeted to juxtanuclear Golgi membranes (24,29,48). However, coexpression of F13L-GFP and B5R resulted in the colocalization of the two proteins in endosomal vesicles (22). Furthermore, colocalization was dependent on both an unmutated phospholipase motif and the palmitylation site in the F13L protein.…”

mentioning

confidence: 92%

“…Plasmids pF13L-GFP containing the GFP coding sequence at the C terminus of the F13L ORF and pB5R containing the B5R ORF were described previously (22). Plasmid pSVGL1, containing wild-type vesicular stomatitis virus (VSV) G protein, and VSVG-GFP, containing a GFP-tagged ts045 VSV G protein, were generously provided by J.…”

Section: Cells and Virusesmentioning

confidence: 99%

“…The mutant vF13L⌬, originally referred to as vRB12 (3), has most of the F13L ORF replaced with the Escherichia coli xanthine guanine phosphoribosyltransferase ORF. Recombinant vF13L-GFP contains the GFP coding sequence at the C terminus of the F13L ORF (22). For virus titration and analysis of plaque size, infected BS-C-1 monolayers were fixed and stained with 0.1% crystal violet in 20% methanol.…”

Section: Cells and Virusesmentioning

confidence: 99%

“…Additional plasmids were constructed by standard procedures. Briefly, the F13L-GFP fusion ORF in plasmid pGF13L (22) was replaced by PLD1-HA or PLD1-GFP fusion ORFs containing the hemagglutinin (HA) tag or GFP sequence at the N terminus. The HA tag or GFP ORF was joined with PLD1 coding sequence by two-stage PCR, and the final PCR products were cloned into plasmid pGF13L, yielding plasmids pGPLD-LR and pGPLD-LR2, respectively.…”

Section: Cells and Virusesmentioning

confidence: 99%

“…The GFP moiety had no deleterious effect, as the fusion protein complemented a mutant vaccinia virus with a deleted F13L gene and was localized in the IEV, CEV, and EEV membranes (22). When expressed by transfection in the absence of other viral gene products, F13L-GFP was localized in Golgi membranes and post-Golgi vesicles that contained early and late endosomal markers (22). Under similar transfection conditions, the B5R protein was targeted to juxtanuclear Golgi membranes (24,29,48).…”

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confidence: 99%

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Similarities in the Induction of Post-Golgi Vesicles by the Vaccinia Virus F13L Protein and Phospholipase D

Husain

Moss

2002

J Virol

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Intracellular mature vaccinia virions are wrapped by cisternae, derived from virus-modified trans-Golgi or endosomal membranes, and then transported via microtubules to the cell periphery. Two viral proteins, encoded by the F13L and B5R open reading frames, are essential for the membrane-wrapping step. Previous transfection studies indicated that F13L induces the formation of post-Golgi vesicles that incorporate the B5R protein and that this activity depends on an intact F13L phospholipase motif. Here we show that the F13L protein has a general effect on the trafficking of integral membrane proteins from the Golgi apparatus, as both the vaccinia virus A36R protein and the vesicular stomatitis virus G protein also colocalized with the F13L protein in vesicles. In addition, increased expression of cellular phospholipase D, which has a similar phospholipase motif as, but little amino acid sequence identity with, F13L, induced post-Golgi vesicles that contained B5R and A36R proteins. Butanol-1, which prevents the formation of phosphatidic acid by phospholipase D and specifically inhibits phospholipase D-mediated vesicle formation, also inhibited F13L-induced vesicle formation, whereas secondary and tertiary alcohols had no effect. Moreover, inhibition of phospholipase activity by butanol-1 also reduced plaque size and decreased the formation of extracellular vaccinia virus without affecting the yield of intracellular mature virus. Phospholipase D, however, could not complement a vaccinia virus F13L deletion mutant, indicating that F13L has additional virus-specific properties. Taken together, these data support an important role for F13L in inducing the formation of vesicle precursors of the vaccinia virus membrane via phospholipase activity or activation.Poxviruses are large, enveloped DNA viruses that replicate entirely within the cytoplasm of infected cells (30). The assembly of vaccinia virus, the most intensively studied member of the poxvirus family, can be divided into two phases. The first culminates in the formation of infectious intracellular mature virions (IMV) (13,14,21,31,43). The second involves the wrapping of IMV with cisternae derived from virus-modified trans-Golgi or endosomal membranes to form intracellular enveloped virions (IEV) (18,39,47) that are transported along microtubules to the periphery where the outer IEV membrane and the plasma membrane fuse (12,20,35,49,50). Most extracellular virus, called cell-associated enveloped virions (CEV), adhere to the outside of the plasma membrane and mediate direct cell-to-cell spread (4), which is facilitated by motile actin tails (7,36,38,44,52). The released virions, called extracellular enveloped virions (EEV), provide an additional mechanism for long-range spreading (32). The ratio of CEV to EEV varies with different vaccinia virus strains.Of the seven known proteins associated with IEV-or EEVspecific membranes, the ones encoded by the F13L and B5R open reading frames (ORFs) are required for the wrapping of IMV to form IEV (3, 9, 51). The B5R produ...

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mentioning

confidence: 92%

Section: Cells and Virusesmentioning

confidence: 99%

Section: Cells and Virusesmentioning

confidence: 99%

Section: Cells and Virusesmentioning

confidence: 99%

mentioning

confidence: 99%

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Similarities in the Induction of Post-Golgi Vesicles by the Vaccinia Virus F13L Protein and Phospholipase D

Husain

Moss

2002

J Virol

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An in‐silico‐based study identified peptide inhibitors that can block the egression of the monkeypox virus by inhibiting the p37 protein target

et al. 2023

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Monkeypox is a zoonotic disease caused by the Poxviridiea family virus Monkeypox. According to the Centers for Disease Control and Prevention, 70,420 monkeypox virus infections had been reported in 107 countries as of October 6, 2022. New studies have concluded that the monkeypox outbreak is caused by a strain with a unique mutation, increasing the possibility that the virus may develop resistance to current medicines by accumulating mutations in therapeutic targets. As peptide‐based therapeutics impede the drug target through multiple interactions, it may offer a better therapeutic solution to the possible drug resistance issue related to monkeypox treatment. Therefore, in this work, we screened an antiviral peptide library, the CPP site 2.0 database, against the p37 target protein using molecular docking approaches. The p37 is required for the viral pathogen's successful egression and spread. The allergenicity and physicochemical properties of the peptides were thoroughly analyzed before the molecular docking studies for selecting druggable candidates. The interactions of the peptides bearing the highest docking score were validated further by using molecular dynamics (MD) simulation studies. Our investigation revealed that two cell‐penetrating peptides of the CPP site 2.0 database might effectively prevent the egression and spread of the MPXV by inhibiting p37. Following more testing, these peptides can be explored in developing peptide‐based therapies against the MPX therapy.

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Recombinant Poxviruses: Versatile Tools for Immunological Assays

Forsyth¹,

Addison²,

Eisenlohr³

2019

Antigen Processing

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Vaccinia Virus F13L Protein with a Conserved Phospholipase Catalytic Motif Induces Colocalization of the B5R Envelope Glycoprotein in Post-Golgi Vesicles

Cited by 50 publications

References 72 publications

Similarities in the Induction of Post-Golgi Vesicles by the Vaccinia Virus F13L Protein and Phospholipase D

Similarities in the Induction of Post-Golgi Vesicles by the Vaccinia Virus F13L Protein and Phospholipase D

An in‐silico‐based study identified peptide inhibitors that can block the egression of the monkeypox virus by inhibiting the p37 protein target

Recombinant Poxviruses: Versatile Tools for Immunological Assays

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