Premium
The paramyxovirus, Sendai virus, V protein encodes a luxury function required for viral pathogenesis
Author(s) -
Kato Atsushi,
Kiyotani Katsuhiro,
Sakai Yuko,
Yoshida Tetsuya,
Nagai Yoshiyuki
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.3.578
Subject(s) - biology , sendai virus , virology , pathogenesis , virus , viral structural protein , viral pathogenesis , function (biology) , genetics , viral replication , viral entry , immunology
The Sendai virus (SeV) V protein is characterized by the unique cysteine‐rich domain in its carboxy‐terminal half which is fused to the amino‐terminal half of the P protein, but its function has remained enigmatic. The V protein‐directing mRNA is generated by a remarkable process known as mRNA editing involving the pseudotemplated addition of a single G residue at a specific septinucleotide locus in the P gene, whereas the unedited exact copy encodes the P protein. Here, we introduced two nucleotide changes in the septinucleotide motif (UUUUCCC to UUCUUCC) in a full‐length SeV cDNA and were able to recover a virus from the cDNA, which was devoid of mRNA editing and hence unable to synthesize the V protein. Compared with the parental wild‐type virus with regard to gene expression, replication and cytopathogenicity in various cell lines in vitro , the V(−) virus was found to be either potentiated or comparable but never attenuated. The V(−) virus, however, showed markedly attenuated in vivo replication capacity in and pathogenicity for mice. Thus, though categorized as a non‐essential gene product, SeV V protein encodes a luxury function required for in vivo pathogenicity.