ArticleJournal of virology1997
Protein interactions in the herpes simplex virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 32 citations in OpenAlex.
- Distinct effects of glucocorticoid on pseudorabies virus infection in neuron-like and epithelial cells.Journal of virology · 2025Article
- The precise function of alphaherpesvirus tegument proteins and their interactions during the viral life cycle.Frontiers in microbiology · 2024Review
- The Role of VP16 in the Life Cycle of Alphaherpesviruses.Frontiers in microbiology · 2020Review
- De Novo Herpes Simplex Virus VP16 Expression Gates a Dynamic Programmatic Transition and Sets the Latent/Lytic Balance during Acute Infection in Trigeminal Ganglia.PLoS pathogens · 2016Article
- Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1.Molecular and cellular biology · 2009Article
- Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection.Antimicrobial agents and chemotherapy · 2009Article
- Article
- The reading frame BPLF1 of Epstein-Barr virus: a homologue of herpes simplex virus protein VP16.Virus genes · 2004Article
- HCF-1 functions as a coactivator for the zinc finger protein Krox20.The Journal of biological chemistry · 2003Article
- A single amino acid substitution in herpes simplex virus type 1 VP16 inhibits binding to the virion host shutoff protein and is incompatible with virus growth.Journal of virology · 2003Article
- Molecular cloning of Drosophila HCF reveals proteolytic processing and self-association of the encoded protein.Journal of cellular physiology · 2003Article
- Interaction of HCF-1 with a cellular nuclear export factor.The Journal of biological chemistry · 2002Article
- An activation domain in the C-terminal subunit of HCF-1 is important for transactivation by VP16 and LZIP.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Zhangfei: a second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16.Nucleic acids research · 2000Article
- Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP.Molecular and cellular biology · 2000Article
- Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells.Journal of virology · 2000Article
- Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.Genes & development · 1999Article
- Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2.Journal of virology · 1999Article
- HCF-dependent nuclear import of VP16.The EMBO journal · 1999Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The herpes simplex virus VP16 protein functions as a potent transcriptional activator and targets DNA sites with the consensus TAATGARAT present in all the viral immediate-early gene promoters. To do so, VP16 directs assembly of a multiprotein complex involving two cellular proteins, host cell factor (HCF) and the Oct-1 DNA-binding transcription factor. To investigate the importance of specific protein-protein interactions to formation of this VP16-induced complex (VIC), we used oligopeptides to prevent VIC assembly. Linear and cyclic peptides corresponding to a region of VP16 previously implicated in complex formation were potent inhibitors of VIC assembly. To further characterize the protein interactions involved, we cloned a human cDNA encoding the minimal VP16 interaction domain of HCF, containing amino acids 1 to 380 [HCF (1-380)]. The REHAYS-based peptides active in preventing VIC assembly were found to specifically block binding of VP16 to HCF (1-380), without affecting VP16-Oct-1 binding. The inhibitory activity of these VP16 peptides was strictly sequence specific for the EHAY residues. Site-directed mutagenesis of the HCF (1-380) domain revealed residues E102 and K105 to be critical determinants in support of VIC formation. Alteration of a single residue in HCF, K105, was shown to virtually abolish complex assembly. Interestingly however, none of the HCF mutants that were impaired in their ability to support complex formation exhibited defects in direct VP16 binding, supporting loss of function at a higher order in complex assembly.
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