» Articles » PMID: 9696857

Migration of Mitochondria to Viral Assembly Sites in African Swine Fever Virus-infected Cells

Overview
Journal J Virol
Date 1998 Aug 8
PMID 9696857
Citations 57
Authors
Affiliations
Soon will be listed here.
Abstract

An examination by electron microscopy of the viral assembly sites in Vero cells infected with African swine fever virus showed the presence of large clusters of mitochondria located in their proximity. These clusters surround viral factories that contain assembling particles but not factories where only precursor membranes are seen. Immunofluorescence microscopy revealed that these accumulations of mitochondria are originated by a massive migration of the organelle to the virus assembly sites. Virus infection also promoted the induction of the mitochondrial stress-responsive proteins p74 and cpn 60 together with a dramatic shift in the ultrastructural morphology of the mitochondria toward that characteristic of actively respiring organelles. The clustering of mitochondria around the viral factory was blocked in the presence of the microtubule-disassembling drug nocodazole, indicating that these filaments are implicated in the transport of the mitochondria to the virus assembly sites. The results presented are consistent with a role for the mitochondria in supplying the energy that the virus morphogenetic processes may require and make of the African swine fever virus-infected cell a paradigm to investigate the mechanisms involved in the sorting of mitochondria within the cell.

Citing Articles

Insights into the Role of VPS39 and Its Interaction with CP204L and A137R in ASFV Infection.

Dolata K, Karger A Viruses. 2024; 16(9).

PMID: 39339953 PMC: 11437485. DOI: 10.3390/v16091478.


African Swine Fever Virus Host-Pathogen Interactions.

Netherton C, Shimmon G, Hui J, Connell S, Reis A Subcell Biochem. 2023; 106:283-331.

PMID: 38159232 DOI: 10.1007/978-3-031-40086-5_11.


Host Cytoskeleton Gene Expression Is Correlated with the Formation of Ascovirus Reproductive Viral Vesicles.

Zaghloul H, Arensburger P, Federici B Viruses. 2022; 14(7).

PMID: 35891423 PMC: 9319082. DOI: 10.3390/v14071444.


Regulation of antiviral immune response by African swine fever virus (ASFV).

Zheng X, Nie S, Feng W Virol Sin. 2022; 37(2):157-167.

PMID: 35278697 PMC: 9170969. DOI: 10.1016/j.virs.2022.03.006.


Mitochondrial and Innate Immunity Transcriptomes from Spodoptera frugiperda Larvae Infected with the Spodoptera frugiperda Ascovirus.

Zaghloul H, Hice R, Bideshi D, Arensburger P, Federici B J Virol. 2020; 94(9).

PMID: 32075926 PMC: 7163118. DOI: 10.1128/JVI.01985-19.


References
1.
Breese Jr S, DeBOER C . Electron microscope observations of African swine fever virus in tissue culture cells. Virology. 1966; 28(3):420-8. DOI: 10.1016/0042-6822(66)90054-7. View

2.
Hackenbrock C . Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria. J Cell Biol. 1966; 30(2):269-97. PMC: 2107001. DOI: 10.1083/jcb.30.2.269. View

3.
Van Blerkom J . Microtubule mediation of cytoplasmic and nuclear maturation during the early stages of resumed meiosis in cultured mouse oocytes. Proc Natl Acad Sci U S A. 1991; 88(11):5031-5. PMC: 51801. DOI: 10.1073/pnas.88.11.5031. View

4.
Andres G, Simon-Mateo C, Vinuela E . Assembly of African swine fever virus: role of polyprotein pp220. J Virol. 1997; 71(3):2331-41. PMC: 191342. DOI: 10.1128/JVI.71.3.2331-2341.1997. View

5.
Salas M, Vinuela E, Salas J . Role of the host cell nucleus in the replication of African swine fever virus DNA. Virology. 1992; 188(2):637-49. DOI: 10.1016/0042-6822(92)90518-t. View