Synthesis of mitochondrial macromolecules in herpes simplex type 1 virus infected Vero cells

Lund, Karen; Ziola, Barry

doi:10.1139/o86-171

Cited by 8 publications

(5 citation statements)

References 10 publications

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“…Herpes simplex viruse infection of the cell has been known to degrade the mitochondrial DNA (mtDNA) rapidly and completely by an HSV nuclease, UL12 gene product (Saffran et al, 2007). This is in compliance with the early findings where the production of mitochondrial proteins decreased by 60% in HSV-infected cells when compared to the uninfected cells (Lund and Ziola, 1986;Latchman, 1988). In another study, the mitochondrial damage has been associated with encephalitis caused by HSV infection.…”

Section: Maintenance and Exploitation Of Mitochondria Until Mid-herpesupporting

confidence: 73%

Herpes Simplex Virus: The Hostile Guest That Takes Over Your Home

2020

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Alpha (α)-herpesviruses (HSV-1 and HSV-2), like other viruses, are obligate intracellular parasites. They hijack the cellular machinery to survive and replicate through evading the defensive responses by the host. The viral genome of herpes simplex viruses (HSVs) contains viral genes, the products of which are destined to exploit the host apparatus for their own existence. Cellular modulations begin from the entry point itself. The two main gateways that the virus has to penetrate are the cell membrane and the nuclear membrane. Changes in the cell membrane are triggered when the glycoproteins of HSV interact with the surface receptors of the host cell, and from here, the components of the cytoskeleton take over. The rearrangement in the cytoskeleton components help the virus to enter as well as transport to the nucleus and back to the cell membrane to spread out to the other cells. The entire carriage process is also mediated by the motor proteins of the kinesin and dynein superfamily and is directed by the viral tegument proteins. Also, the virus captures the cell's most efficient cargo carrying system, the endoplasmic reticulum (ER)-Golgi vesicular transport machinery for egress to the cell membrane. For these reasons, the host cell has its own checkpoints where the normal functions are halted once a danger is sensed. However, a cell may be prepared for the adversities from an invading virus, and it is simply commendable that the virus has the antidote to these cellular strategies as well. The HSV viral proteins are capable of limiting the use of the transcriptional and translational tools for the cell itself, so that its own transcription and translation pathways remain unhindered. HSV prefers to constrain any self-destruction process of the cell-be it autophagy in the lysosome or apoptosis by the mitochondria, so that it can continue to parasitize the cell for its own survival. This review gives a detailed account of the significance of compartmentalization during HSV pathogenesis. It also highlights the undiscovered areas in the HSV cell biology research which demand attention for devising improved therapeutics against the infection.

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Section: Maintenance and Exploitation Of Mitochondria Until Mid-herpesupporting

confidence: 73%

Herpes Simplex Virus: The Hostile Guest That Takes Over Your Home

2020

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“…Interestingly, levels of cellular ATP and lactate as well as Δψ m are maintained for at least 6 h after infection before decreasing at later stages (Murata et al, 2000a). Earlier studies demonstrated that mitochondrial protein synthesis in HSV-infected cells decreases progressively, dropping to about 60% of normal levels (Latchman, 1988;Lund and Ziola, 1986). Moreover, mitochondria exhibit a gradual decline in the rate of calcium uptake, which reaches 65% of the control rate at later stages of infection (Lund and Ziola, 1985).…”

Section: Hsv Affects Intracellular Compartmentalization Of Mitochondriamentioning

confidence: 95%

Mitochondria and viruses

Ohta

Nishiyama

2011

Mitochondrion

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Mitochondria are involved in a variety of cellular metabolic processes, and their functions are regulated by extrinsic and intrinsic stimuli including viruses. Recent studies have shown that mitochondria play a central role in the primary host defense mechanisms against viral infections, and a number of novel viral and mitochondrial proteins are involved in these processes. Some viral proteins localize in mitochondria and interact with mitochondrial proteins to regulate cellular responses. This review summarizes recent findings on the functions and roles of these molecules as well as mitochondrial responses to viral infections.

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“…If that is the case, the acquisition by ASFV of a prenyltransferase gene for the synthesis of the ubiquinone (coenzyme Q) prenyl chain could be related to an increase in mitochondrial function that might be required to provide extra energy for viral processes, such as macromolecular synthesis and morphogenesis. In this connection, it should be mentioned that mitochondrial DNA synthesis has been found to increase in herpes simplex type 1 virus-infected Vero cells (57) and that adenovirus infection of human cells stimulates mitochondrial activity (58).…”

Section: Properties and Transcriptional Analysis Of Orf B318l-mentioning

confidence: 99%

African Swine Fever Virus trans-Prenyltransferase

Alejo¹,

Yáñez²,

Rodrı́guez³

et al. 1997

Journal of Biological Chemistry

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The present study describes the characterization of an African swine fever virus gene homologous to prenyltransferases. The gene, designated B318L, is located within the EcoRI B fragment in the central region of the virus genome, and encodes a polypeptide with a predicted molecular weight of 35,904. The protein is characterized by the presence of a putative hydrophobic transmembrane domain at the amino end. The gene is expressed at the late stage of virus infection, and transcription is initiated at positions -118, -119, -120, and -122 relative to the first nucleotide of the translation start codon. Protein B318L presents a colinear arrangement of the four highly conserved regions and the two aspartate-rich motifs characteristic of geranylgeranyl diphosphate synthases, farnesyl diphosphate synthases, and other prenyltransferases. Throughout these regions, the percentages of identity between protein B318L and various prenyltransferases range from 28.6 to 48.7%. The gene was cloned in vector pTrxFus without the amino-terminal hydrophobic region and expressed in Escherichia coli. The recombinant protein, purified essentially to homogeneity by affinity chromatography, catalyzes the sequential condensation of isopentenyl diphosphate with different allylic diphosphates, farnesyl diphosphate being the best allylic substrate of the reaction. All-trans-polyprenyl diphosphates containing 3-13 isoprene units are synthesized, which identifies the B318L protein as a trans-prenyltransferase.

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Synthesis of mitochondrial macromolecules in herpes simplex type 1 virus infected Vero cells

Cited by 8 publications

References 10 publications

Herpes Simplex Virus: The Hostile Guest That Takes Over Your Home

Herpes Simplex Virus: The Hostile Guest That Takes Over Your Home

Mitochondria and viruses

African Swine Fever Virus trans-Prenyltransferase

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