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Journal of Virology, May 2001, p. 4625-4632, Vol. 75, No. 10
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.10.4625-4632.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

M-X-I Motif of Semliki Forest Virus Capsid Protein Affects Nucleocapsid Assembly

Ulrica Skoging-Nyberg1 and Peter Liljeström1,2,*

Microbiology and Tumorbiology Center, Karolinska Institutet,1 and Department of Vaccine Research, Swedish Institute for Infectious Disease Control,2 Stockholm, Sweden

Received 16 November 2000/Accepted 21 February 2001

Alphavirus budding is driven by interactions between spike and nucleocapsid proteins at the plasma membrane. The binding motif, Y-X-L, on the spike protein E2 and the corresponding hydrophobic cavity on the capsid protein were described earlier. The spike-binding cavity has also been suggested to bind an internal hydrophobic motif, M113-X-I115, of the capsid protein. In this study we found that replacement of amino acids M113 and I115 with alanines, as single or double mutations, abolished formation of intracellular nucleocapsids. The mutants could still bud efficiently, but the NCs in the released virions were not stable after removal of the membrane and spike protein layer. In addition to wild-type spherical particles, elongated multicored particles were found at the plasma membrane and released from the host cell. We conclude that the internal capsid motif has a biological function in the viral life cycle, especially in assembly of nucleocapsids. We also provide further evidence that alphaviruses may assemble and bud from the plasma membrane in the absence of preformed nucleocapsids.

* Corresponding author. Mailing address: Microbiology and Tumorbiology Center, Karolinska Institutet, Box 280, S-171 77 Stockholm, Sweden. Phone: 46-8-457 2550. Fax: 46-8-310 848. E-mail: Peter.Liljestrom{at}mtc.ki.se.

Journal of Virology, May 2001, p. 4625-4632, Vol. 75, No. 10
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.10.4625-4632.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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