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Journal of Virology, December 2006, p. 11852-11860, Vol. 80, No. 23
0022-538X/06/$08.00+0     doi:10.1128/JVI.01225-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Effects of Picornavirus 3A Proteins on Protein Transport and GBF1-Dependent COP-I Recruitment{triangledown}

Els Wessels,1 Daniël Duijsings,1 Kjerstin H. W. Lanke,1 Sander H. J. van Dooren,1 Catherine L. Jackson,2 Willem J. G. Melchers,1 and Frank J. M. van Kuppeveld1*

Department of Medical Microbiology, Radboud University, Nijmegen Medical Centre, Nijmegen Centre for Molecular Life Sciences, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands,1 Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 208922

Received 12 June 2006/ Accepted 4 September 2006

The 3A protein of the coxsackievirus B3 (CVB3), an enterovirus that belongs to the family of the picornaviruses, inhibits endoplasmic reticulum-to-Golgi transport. Recently, we elucidated the underlying mechanism by showing that CVB3 3A interferes with ADP-ribosylation factor 1 (Arf1)-dependent COP-I recruitment to membranes by binding and inhibiting the function of GBF1, a guanine nucleotide exchange factor that is required for the activation of Arf1 (E. Wessels et al., Dev. Cell 11:191-201, 2006). Here, we show that the 3A protein of poliovirus, another enterovirus, is also able to interfere with COP-I recruitment through the same mechanism. No interference with protein transport or COP-I recruitment was observed for the 3A proteins of any of the other picornaviruses tested here (human rhinovirus [HRV], encephalomyocarditis virus, foot-and-mouth disease virus, and hepatitis A virus). We show that the 3A proteins of HRV, which are the most closely related to the enteroviruses, are unable to inhibit COP-I recruitment, due to a reduced ability to bind GBF1. When the N-terminal residues of the HRV 3A proteins are replaced by those of CVB3 3A, chimeric proteins are produced that have gained the ability to bind GBF1 and, by consequence, to inhibit protein transport. These results show that the N terminus of the CVB3 3A protein is important for binding of GBF1 and its transport-inhibiting function. Taken together, our data demonstrate that the activity of the enterovirus 3A protein to inhibit GBF1-dependent COP-I recruitment is unique among the picornaviruses.

* Corresponding author. Mailing address: Department of Medical Microbiology, Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. Phone: (31) 24 3617574. Fax: (31) 24 3540216. E-mail: f.vankuppeveld{at}ncmls.ru.nl.

{triangledown} Published ahead of print on 27 September 2006.

Journal of Virology, December 2006, p. 11852-11860, Vol. 80, No. 23
0022-538X/06/$08.00+0     doi:10.1128/JVI.01225-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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