The pseudorabies virus (PRV) UL31 protein (pUL31) is a homologue of the herpes simplex virus 1 pUL31, which is a multifunctional protein that is important for HSV-1 infection. However, little is known concerning the subcellular localization signal of PRV UL31. Here, by transfection with a series of PRV UL31 deletion mutants fused to an enhanced yellow fluorescent protein (EYFP) gene, a bipartite nuclear localization signal (NLS) and a PY motif NLS of UL31 were identified and mapped to amino acids (aa) 4 to 20 (RRRLLRRKSSAARRKTL) and aa 21 to 34 (TRAARDRYAPYFAY), respectively. Additionally, the predicted nuclear export signal (NES) was shown to be nonfunctional. Taken together, this information opens up new avenues for investigating the biological functions of UL31 during PRV infection.
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Alphaherpesvirus upregulates NDRG1 expression to facilitate the nuclear import of viral UL31 and UL34 proteins.
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College of Veterinary Medicine, Henan Agricultural University, Zhengzhou, Henan Province, China.
Proteins UL31 and UL34 encoded by alphaherpesvirus are critical for viral primary envelopment and nuclear egress. We report here that pseudorabies virus (PRV), a useful model for research on herpesvirus pathogenesis, uses N-myc downstream regulated 1 (NDRG1) to assist the nuclear import of UL31 and UL34. PRV promoted NDRG1 expression through DNA damage-induced P53 activation, which was beneficial to viral proliferation.
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Friedrich-Loeffler-Institut, Institute of Molecular Virology and Cell Biology, Greifswald-Insel Riems, Germany
Nuclear egress of herpesvirus capsids is mediated by the conserved nuclear egress complex (NEC), composed of the membrane-anchored pUL34 and its nucleoplasmic interaction partner, pUL31. The recently solved crystal structures of the NECs from different herpesviruses show a high structural similarity, with the pUL34 homologs building a platform recruiting pUL31 to the inner nuclear membrane. Both proteins possess a central globular fold, while the conserved N-terminal portion of pUL31 forms an extension reaching around the core of pUL34.
View Article and Find Full Text PDFIdentification of molecular determinants for the nuclear import of pseudorabies virus UL31.
Arch Biochem Biophys
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Department of Pathogenic Biology and Immunology, School of Basic Science, Guangzhou Medical University, Guangzhou 511436, PR China; Guangzhou Hoffmann Institute of Immunology, School of Basic Science, Guangzhou Medical University, Guangzhou 511436, PR China. Electronic address:
Herpes simplex virus 1 (HSV-1) UL31 is a multifunctional protein and important for HSV-1 infection. Pseudorabies virus (PRV) UL31 is a late protein homologous to HSV-1 UL31. Previous studies showed that PRV UL31 is predominantly localized to nucleus, however, the molecular determinants for its nuclear import were unclear to date.
View Article and Find Full Text PDFPseudorabies virus (PRV) early protein UL31 is a homologue of herpes simplex virus 1 (HSV-1) UL31, which is a multifunctional protein important for HSV-1 infection. However, the precise roles of PRV UL31 in virus life cycle are still poorly understood. A relatively crucial tool for uncovering the function of UL31 is an antiserum that specifically detects UL31 in the PRV-infected cells.
View Article and Find Full Text PDFCharacterization of the nuclear import and export signals of pseudorabies virus UL31.
Arch Virol
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Department of Pathogenic Biology and Immunology, School of Basic Science, Guangzhou Medical University, Xinzao Town, Panyu, Guangzhou, 511436, Guangdong, People's Republic of China.
The pseudorabies virus (PRV) UL31 protein (pUL31) is a homologue of the herpes simplex virus 1 pUL31, which is a multifunctional protein that is important for HSV-1 infection. However, little is known concerning the subcellular localization signal of PRV UL31. Here, by transfection with a series of PRV UL31 deletion mutants fused to an enhanced yellow fluorescent protein (EYFP) gene, a bipartite nuclear localization signal (NLS) and a PY motif NLS of UL31 were identified and mapped to amino acids (aa) 4 to 20 (RRRLLRRKSSAARRKTL) and aa 21 to 34 (TRAARDRYAPYFAY), respectively.
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