ArticleJournal of virology1995
Nuclear targeting of the tegument protein pp65 (UL83) of human cytomegalovirus: an unusual bipartite nuclear localization signal functions with other portions of the protein to mediate its efficient nuclear transport.
Article in Journal of virology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 107 citations in OpenAlex.
- Nuclear transport of human cytomegalovirus tegument protein pp65 through nucleoplasmic reticulum.PLoS pathogens · 2026Article
- Human induced pluripotent stem cells are resistant to human cytomegalovirus infection primarily at the attachment level due to the reduced expression of cell-surface heparan sulfate.Journal of virology · 2024Article
- Distinct early role of PTEN regulation during HCMV infection of monocytes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Subviral Dense Bodies of Human Cytomegalovirus Induce an Antiviral Type I Interferon Response.Cells · 2022Article
- Advanced Cell Therapies for Glioblastoma.Frontiers in immunology · 2022Review
- Guinea pig cytomegalovirus protective T cell antigen GP83 is a functional pp65 homolog for innate immune evasion and pentamer dependent virus tropism.Journal of virology · 2021Article
- Article
- Recognition of a highly conserved glycoprotein B epitope by a bivalent antibody neutralizing HCMV at a post-attachment step.PLoS pathogens · 2020Article
- Animal Models of Congenital Cytomegalovirus Transmission: Implications for Vaccine Development.The Journal of infectious diseases · 2020Review
- Identification of adipocyte plasma membrane-associated protein as a novel modulator of human cytomegalovirus infection.PLoS pathogens · 2019Article
- Functionally inactivated dominant viral antigens of human cytomegalovirus delivered in replication incompetent adenovirus type 6 vectors as vaccine candidates.Human vaccines & immunotherapeutics · 2017Article
- Cytomegalovirus Late Protein pUL31 Alters Pre-rRNA Expression and Nuclear Organization during Infection.Journal of virology · 2017Article
- B cell epitope of human cytomegalovirus phosphoprotein 65 (HCMV pp65) induced anti-dsDNA antibody in BALB/c mice.Arthritis research & therapy · 2017Article
- Viral evasion of DNA-stimulated innate immune responses.Cellular & molecular immunology · 2017Review
- Article
- Viral binding-induced signaling drives a unique and extended intracellular trafficking pattern during infection of primary monocytes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Review
- Human cytomegalovirus pUL97 regulates the viral major immediate early promoter by phosphorylation-mediated disruption of histone deacetylase 1 binding.Journal of virology · 2013Article
- Nuclear targeting of human cytomegalovirus large tegument protein pUL48 is essential for viral growth.Journal of virology · 2013Article
- Nucleocytoplasmic shuttling and CRM1-dependent MHC class I peptide presentation of human cytomegalovirus pp65.Medical microbiology and immunology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Large amounts of pp65 (UL83) of human cytomegalovirus are translocated to the cell nucleus during the first minutes after uptake of the tegument protein from infecting viral particles. Two stretches of basic amino acids which resembled nuclear localization signals (NLS) of both the simian virus 40 type and the bipartite type were found in the primary structure of pp65. Deletion of these sequences significantly impaired nuclear localization of the truncated proteins after transient expression. The results indicated that both elements contributed to the nuclear localization of the protein. When fused to the bacterial beta-galactosidase, only one of the two basic elements was sufficient to mediate nuclear translocation. This element consisted of two clusters of basic amino acids (boxes C and D), which were separated by a short spacer sequence. In contrast to other bipartite NLS of animal cells, both basic boxes C and D functioned independently in nuclear transport, thus resembling simian virus 40-type NLS. Yet, complete translocation of beta-galactosidase was only found in the bipartite configuration. When both boxes C and D were fused, thereby deleting the intervening sequences, the nuclear transport of beta-galactosidase was reduced to levels seen with constructs in which only one of the boxes was present. Appropriate spacing, therefore, was important but not absolutely required. This was in contrast with results for other bipartite NLS, in which spacer deletions led to complete cytoplasmic retention. The presented results demonstrate that efficient nuclear transport of pp65 is mediated by one dominant NLS and additional targeting sequences. The major NLS of pp65 is an unusual signal sequence composed of two weak NLS which function together as one strong bipartite nuclear targeting signal.
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