The properties of recombinant Sendai virus having the P gene of Sendai virus pi strain derived from BHK cells persistently ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-09

AUTHORS

Machiko Nishio, Ai Nagata, Ayako Yamamoto, Masato Tsurudome, Morihiro Ito, Mitsuo Kawano, Hiroshi Komada, Yasuhiko Ito

ABSTRACT

We prepared the chimeric recombinant Sendai virus [rSeV(Ppi)] by replacing the P gene of the Z strain with that of pi strain for analyzing the function of Ppi, Vpi and Cpi proteins. Intriguingly, HA production by rSeV(Ppi) is significantly lower at 38 degrees C than at 32 degrees C, showing that virus growth of rSeV(Ppi) is slightly suppressed at 38 degrees C. However, the main phenotypes of SeVpi, a marked temperature sensitivity as viral replication and an ability of establishing persistent infection, are not explained by the Ppi, Vpi and Cpi proteins. The V and C proteins form inclusion bodies in L929 cells infected with rSeV(Ppi) and incubated at 38 degrees C. L929 cells infected with rSeV(Ppi) and L929 cells stably expressing the Cpi protein show resistance to interferon-beta at 32 and 38 degrees C, indicating that the Cpi protein per se is not temperature-sensitive to inhibition of IFN signaling. The complete genome sequences of Sendai virus (SeV) pi and parent Nagoya strains were determined. Fifty nucleic acid substitutions are found in the genome sequence of SeV pi strain in comparison with Nagoya strain. There are three nucleic acid substitutions in the leader sequence, while the trailer, intergenic, gene-end and gene-start sequences of both strains are completely identical. Deletions and insertions of nucleotide are not found. There are 32 amino acid substitutions in Sendai virus pi strain. The specific amino acid substitutions unique to the SeVpi are 18. Information about the complete genome sequences of SeVpi strain is important to totally understand the persistent infection and lower pathogenicity of SeV. More... »

PAGES

151-158

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00430-006-0012-3

DOI

http://dx.doi.org/10.1007/s00430-006-0012-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026740489

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16465546


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