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Journal of Virology, October 1999, p. 8703-8712, Vol. 73, No. 10
Howard Hughes Medical
Institute1 and Department of
Biochemistry, Molecular Biology, and Cell
Biology,2 Northwestern University, Evanston,
Illinois 60208-3500
Received 20 May 1999/Accepted 7 July 1999
Efficient assembly of enveloped viruses at the plasma membranes of
virus-infected cells requires coordination between cytosolic viral
components and viral integral membrane glycoproteins. As viral
glycoprotein cytoplasmic domains may play a role in this coordination,
we have investigated the importance of the hemagglutinin-neuraminidase (HN) protein cytoplasmic domain in the assembly of the nonsegmented negative-strand RNA paramyxovirus simian virus 5 (SV5). By using reverse genetics, recombinant viruses which contain HN with truncated cytoplasmic tails were generated. These viruses were shown to be
replication impaired, as judged by small plaque size, reduced replication rate, and low maximum titers when compared to those features of wild-type (wt) SV5. Release of progeny virus particles from
cells infected with HN cytoplasmic-tail-truncated viruses was
inefficient compared to that of wt virus, but syncytium formation was
enhanced. Furthermore, accumulation of viral proteins at presumptive budding sites on the plasma membranes of infected cells was prevented by HN cytoplasmic tail truncations. We interpret these data to indicate
that formation of budding complexes, from which efficient release of
SV5 particles can occur, depends on the presence of an HN cytoplasmic tail.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Involvement of the Cytoplasmic Domain of the
Hemagglutinin-Neuraminidase Protein in Assembly of the
Paramyxovirus Simian Virus 5
*
Corresponding author. Mailing address: Department of
Biochemistry, Molecular Biology and Cell Biology, Northwestern
University, 2153 North Campus Dr., Evanston, IL 60208-3500. Phone:
(847) 491-5433. Fax: (847) 491-2467. E-mail: ralamb{at}nwu.edu.
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