Identification of a nonconventional motif necessary for the nuclear import of the human parvovirus B19 major capsid protein (VP2)

• Published in: Virology (New York, N.Y.) N.Y.), 2003-02, Vol.306 (1), p.25-32
• Main Authors: Pillet, Sylvie, Annan, Zeinab, Fichelson, Serge, Morinet, F.rédéric
• Format: Article
• Language: English
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Animals; Capsid - chemistry; Capsid - metabolism; Capsid protein; Capsid Proteins; Cell Nucleus - metabolism; Cells, Cultured; COS Cells; Erythroid Precursor Cells; Erythrovirus; Erythrovirus - chemistry; Erythrovirus - genetics; Erythrovirus - metabolism; Gene Expression Regulation, Viral; Humans; Life Sciences; Microbiology and Parasitology; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear localization signal; Nuclear Localization Signals - chemistry; Parvovirus B19; Parvovirus B19, Human - chemistry; Parvovirus B19, Human - genetics; Parvovirus B19, Human - metabolism; Virology
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/S0042-6822(02)00047-8

Human parvovirus B19 replicates and encapsidates its genome in the nucleus of erythroid progenitors in vivo and in vitro. We wanted to understand the determinants necessary for the nuclear transport of the major coat protein, VP2, which makes up about 96% of the viral capsid proteins. A nonconsensus basic motif, KLGPRKATGRW, necessary for the nuclear localization of VP2 was identified and shown to be able to import reporter proteins into the nucleus. The sequence is conserved among the VP2 C-terminal region of erythroviruses. This newly identified sequence will facilitate the understanding of the replication of these viruses.