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Journal of Virology, March 2007, p. 2249-2262, Vol. 81, No. 5
0022-538X/07/$08.00+0     doi:10.1128/JVI.01577-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Exceptional Flexibility in the Sequence Requirements for Coronavirus Small Envelope Protein Function{triangledown}

Lili Kuo,1 Kelley R. Hurst,1 and Paul S. Masters1,2*

Wadsworth Center, New York State Department of Health,1 Department of Biomedical Sciences, State University of New York, Albany, New York 122012

Received 24 July 2006/ Accepted 8 December 2006

The small envelope protein (E) plays a role of central importance in the assembly of coronaviruses. This was initially established by studies demonstrating that cellular expression of only E protein and the membrane protein (M) was necessary and sufficient for the generation and release of virus-like particles. To investigate the role of E protein in the whole virus, we previously generated E gene mutants of mouse hepatitis virus (MHV) that were defective in viral growth and produced aberrantly assembled virions. Surprisingly, however, we were also able to isolate a viable MHV mutant ({Delta}E) in which the entire E gene, as well as the nonessential upstream genes 4 and 5a, were deleted. We have now constructed an E knockout mutant that confirms that the highly defective phenotype of the {Delta}E mutant is due to loss of the E gene. Additionally, we have created substitution mutants in which the MHV E gene was replaced by heterologous E genes from viruses spanning all three groups of the coronavirus family. Group 2 and 3 E proteins were readily exchangeable for that of MHV. However, the E protein of a group 1 coronavirus, transmissible gastroenteritis virus, became functional in MHV only after acquisition of particular mutations. Our results show that proteins encompassing a remarkably diverse range of primary amino acid sequences can provide E protein function in MHV. These findings suggest that E protein facilitates viral assembly in a manner that does not require E protein to make sequence-specific contacts with M protein.

* Corresponding author. Mailing address: David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Avenue, P.O. Box 22002, Albany, NY 12201-2002. Phone: (518) 474-1283. Fax: (518) 473-1326. E-mail: masters{at}wadsworth.org.

{triangledown} Published ahead of print on 20 December 2006.

Journal of Virology, March 2007, p. 2249-2262, Vol. 81, No. 5
0022-538X/07/$08.00+0     doi:10.1128/JVI.01577-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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