M-X-I motif of semliki forest virus capsid protein affects nucleocapsid assembly

Journal of Virology
U Skoging-Nyberg, P Liljeström

Abstract

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.

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Citations

Apr 8, 2011·Journal of Virology·Jonathan E SnyderRichard J Kuhn
Aug 31, 2006·Journal of Virology·Eunmee M HongRichard J Kuhn
Jun 21, 2013·Journal of Virology·Yan Zheng, Margaret Kielian
Sep 3, 2009·Future Microbiology·Joyce JoseRichard J Kuhn
Oct 18, 2011·Journal of Molecular Biology·Jinghua TangTimothy S Baker
Nov 30, 2004·Virus Research·Henrik GaroffR Holland Cheng
Jan 8, 2008·Journal of Molecular Biology·Manuel MorillasEva Kuennemann
Feb 23, 2018·Viruses·Rebecca S BrownMargaret Kielian
Apr 4, 2014·Journal of Virology·Maria Guadalupe MartinezMargaret Kielian
Sep 19, 2020·Nature Communications·Rebecca S BrownMargaret Kielian
Sep 9, 2021·Journal of Virology·Julie M Button, Suchetana Mukhopadhyay

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