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Journal of Virology, December 2001, p. 11755-11765, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11755-11765.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The trans Golgi Network Is Lost from Cells Infected with African Swine Fever Virus

Mari McCrossan,1,dagger Miriam Windsor,1 Sreenivasan Ponnambalam,2 John Armstrong,3 and Thomas Wileman1,*

Institute for Animal Health, Pirbright Laboratories, Woking, Surrey,1 School of Biological Studies, University of Sussex, Falmer, Brighton, Sussex,3 and School of Biochemistry and Molecular Biology, University of Leeds, Leeds, Yorkshire2 United Kingdom

Received 7 March 2001/Accepted 23 August 2001

The cellular secretory pathway is important during the assembly and envelopment of viruses and also controls the transport of host proteins, such as cytokines and major histocompatibility proteins, that function during the elimination of viruses by the immune system. African swine fever virus (ASFV) encodes at least 26 proteins with stretches of hydrophobic amino acids suggesting entry into the secretory pathway (R. J. Yanez, J. M. Rodriguez, M. L. Nogal, L. Yuste, C. Enriquez, J. F. Rodriguez, and E. Vinuela, Virology 208:249-278, 1995). To predict how and where these potential membrane proteins function, we have studied the integrity of the secretory pathway in cells infected with ASFV. Remarkably, ASFV caused complete loss of immunofluorescence signal for the trans Golgi network (TGN) marker protein TGN46 and dispersed the AP1 TGN adapter complex. Loss of TGN46 signal was not due to degradation of TGN46, suggesting redistribution of TGN46 to other membrane compartments. ASFV markedly slowed transport of cathepsin D to lysosomes, demonstrating that loss of TGN structure correlated with loss of TGN function. ASFV shows a tropism for macrophages, and it is possible that ASFV compromises TGN function to augment the activity of viral membrane proteins or to suppress the function of host immunoregulatory proteins.


* Corresponding author. Mailing address: Institute for Animal Health, Pirbright Laboratory, Ash Rd., Woking, Surrey GU240NF, United Kingdom. Phone: 44 01483 232441. Fax: 44 01483 232448. E-mail: thomas.wileman{at}bbsrc.ac.uk.

dagger Present address: Department of Cell Biology, Washington University Medical School, St. Louis, MO 63110.


Journal of Virology, December 2001, p. 11755-11765, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11755-11765.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



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