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Journal of Virology, December 1998, p. 9747-9754, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Cytoplasmic Domain of Sendai Virus HN Protein Contains a Specific
Sequence Required for Its Incorporation into Virions
Toru
Takimoto,1
Tatiana
Bousse,1
Elizabeth C.
Coronel,1
Ruth Ann
Scroggs,1 and
Allen
Portner1,2,*
Department of Virology and Molecular Biology,
St. Jude Children's Research Hospital, Memphis, Tennessee
38105,1 and
Department of Pathology, The
Health Science Center, University of Tennessee, Memphis, Tennessee
381632
Received 29 May 1998/Accepted 31 August 1998
In the assembly of paramyxoviruses, interactions between viral
proteins are presumed to be specific. The focus of this study is to
elucidate the protein-protein interactions during the final stage of
viral assembly that result in the incorporation of the viral envelope
proteins into virions. To this end, we examined the specificity of HN
incorporation into progeny virions by transiently transfecting HN cDNA
genes into Sendai virus (SV)-infected cells. SV HN expressed from
cDNA was efficiently incorporated into progeny Sendai virions, whereas
Newcastle disease virus (NDV) HN was not. This observation supports the
theory of a selective mechanism for HN incorporation. To identify the
region on HN responsible for the selective incorporation, we
constructed chimeric SV and NDV HN cDNAs and evaluated the
incorporation of expressed proteins into progeny virions. Chimera HN
that contained the SV cytoplasmic domain fused to the transmembrane and
external domains of the NDV HN was incorporated to SV particles,
indicating that amino acids in the cytoplasmic domain are
responsible for the observed specificity. Additional experiments
using the chimeric HNs showed that 14 N-terminal amino acids are
sufficient for the specificity. Further analysis identified five
consecutive amino acids (residues 10 to 14) that were
required for the specific incorporation of HN into SV. These residues
are conserved among all strains of SV as well as those of its
counterpart, human parainfluenza virus type 1. These results
suggest that this region near the N terminus of HN interacts with
another viral protein(s) to lead to the specific incorporation of HN
into progeny virions.
*
Corresponding author. Mailing address: Department of
Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105. Phone: (901) 495-3400. Fax: (901)
523-2622. E-mail: allen.portner{at}stjude.org.
Journal of Virology, December 1998, p. 9747-9754, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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