bioRxiv Science⌕ Search

bioRxiv · 10.1101/2024.06.21.599992

Virus-host interaction: investigating novel transcription factors involved in coupling HPV life cycle and epithelial differentiation.

Abstract

High-risk human papillomavirus (HPV) causes almost all cervical cancer, and HPV-18 is the second most prevalent type. The HPV life cycle is intimately associated with the epithelial differentiation program, and the repertoire of cellular transcription factors (TFs) has a crucial role in coordinating viral gene expression across epithelial layers. We aimed to identify host TFs involved in the virus differentiation-dependent life cycle. We initially compared the DNA binding activity of 345 TFs in nuclear extracts of undifferentiated and high calcium-induced differentiated HaCaT cells. Next, we searched in silico for putative binding sites within the HPV-18 long control region (LCR) for the TFs affected by differentiation. Chromatin immunoprecipitation assays (ChIP) were used to assess direct binding of selected TFs, protein levels were evaluated by immunohistochemistry in rafts obtained from human foreskin keratinocytes (HFK) and HPV-18 E6/E7 immortalized HFK, and the impact upon LCR activity was measured in reporter assays. The binding activity of 40 TFs was influenced by differentiation among which 16 putative binding sites within the LCR were identified. We next focused our analysis in PAX6, HMGB1, FOXI1, and NFE2, and all bound to the LCR except FOXI1. Whether FOXI1 activates HPV-18 early promoter activity, PAX6, HMGB1, and NFE2 inhibit viral transcription in undifferentiated normal HFK in which these proteins are mostly expressed. Finally, HPV-18 E6/E7 impaired the normal expression of these TFs throughout epithelial layers. In conclusion, we describe the involvement of PAX6, HMGB1, NFE2, and FOXIl in coupling HPV-18 transcriptional regulation with the epithelia differentiation program, a key event for the productive HPV life cycle. Furthermore, these TFs may also be relevant for HPV-driven carcinogenesis. The identification of proteins involved in the differentiation-dependent HPV life cycle and viral induced transformation may contribute to unveiling novel therapeutic targets for HPV-related malignancies. Author SummaryHPV-16 and HPV-18 respond together for over 70% of cervical cancers. HPV infection is established in basal layers cells of the stratified epithelia and the viral life cycle is highly dependent on the epithelial differentiation program. In this study, we focused on identifying host transcription factors (TFs) involved in the finely tuned regulation of the HPV-18 differentiation-dependent life cycle. We initially screened 345 cellular TFs and found 40 with differential binding activity after differentiation, among which we chose to focus on PAX6, HMGB1, FOXI1, and NFE2. Besides investigating TFs binding to HPV-18 LCR in silico and with immunoprecipitation assays, we evaluated protein levels throughout epithelial layers and demonstrated that the impact of these TFs upon HPV-18 early promoter activity depends on the differentiation status of cells. Finally, we show that HPV-18 oncoproteins lead to abnormal expression of these TFs. Our results contribute to a clearer understanding of pivotal mechanisms governing spatiotemporal regulation of viral early transcription and open avenues for innovative therapeutic strategies for HPV-associated diseases.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Ribeiro, A. L., Nunes, V. T., Caodaglio, A. S., Lima, R. A., Pereira Sobrinho, J. S., Sichero, L.. 2024-06-22. Virus-host interaction: investigating novel transcription factors involved in coupling HPV life cycle and epithelial differentiation.. https://doi.org/10.1101/2024.06.21.599992

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Ctcf deficiency in myofibers induces pathological genome reprogramming toward the spontaneous development of myopathy

How perennial, postmitotic multinucleated tissues, such as skeletal myofibers, maintain their identity and transcriptional adaptation to homeostatic perturbations through adult life is an outstanding question. To address this issue, we investigated the consequences of loss of 3D-genome architecture in skeletal muscles by generating myofiber-specific Ctcf-deficient (CtcfmKO) mice. CtcfmKO mice did not exhibit muscular phenotype at birth but spontaneously developed a severe myopathy. Integrated analysis of snRNAseq, ATACseq and promoter-capture Hi-C revealed both common and fiber-type specific patterns of dysregulated gene expression associated with alterations in chromatin accessibility and promoter-based interactions in Ctcf-deficient myonuclei at distinct stages of myopathy development. Decreased chromatin accessibility at promoters and changes in their connectivity with distal elements were observed across all myonuclei as a direct consequence of Ctcf deficiency at early stages and associated with downregulation of genes implicated in myofiber contraction and anabolism, metabolism, adhesion and neuromuscular transmission. Conversely, at later stages, upregulation of genes leading to persistent activation of ER stress/UPR and catabolism resulted from global reconfiguration of chromatin structure and connectivity, partly as indirect consequence of Ctcf deficiency. Notably, type-IIB myonuclei exhibited specific alterations in gene expression that culminated in loss of fiber-type identity and ectopic expression of inflammatory genes. These results reveal a requirement of Ctcf for maintenance of fiber-type identity and transcriptional adaptation in vivo, through multilayered control of 3D genome integrity. They also indicate an unprecedented association between Ctcf deficiency in myofibers and susceptibility to develop myopathies, whereby Ctcf dispensability for developmental myogenesis confers vulnerability to develop myopathic syndromes.

molecular biology↗

Thiomorpholino antisense oligonucleotides inhibit telomerase and limit cancer cell proliferation

Reactivation of telomerase confers immortality to approximately 90% of human tumors by enabling continuous elongation of the DNA at chromosome ends, or telomeres. The telomerase catalytic subunit TERT adds TTAGGG repeats using a portion of the telomerase RNA component hTR as a template. Because telomerase is inactive in most normal somatic cells, it remains an attractive therapeutic target; however, no telomerase inhibitor has yet demonstrated robust clinical efficacy with acceptable safety. Here we evaluate thiomorpholino oligonucleotides (TMOs) as a new class of antisense oligonucleotides targeting the template region of hTR. TMOs incorporate morpholino rings and phosphorothioate linkages, which enhance nuclease resistance, RNA binding and nuclear uptake. Two anti-hTR TMOs inhibited telomerase activity in vitro with an IC50 below 1 nM, whereas two control TMOs were at least 100-fold less active. HeLa cells treated with anti-hTR TMOs showed progressive telomere shortening, detectable after one week of treatment. Growth inhibition was observed after substantial telomere erosion, and both telomere length and proliferation recovered upon withdrawal of TMOs. These findings establish TMOs as a promising new chemistry for telomerase-targeted therapeutics.

molecular biology↗

Msp1-dependent extraction promotes ubiquitylation of translocation-stalled mitochondrial precursor proteins

The translocase of the outer membrane (TOM complex) imports more than 1,000 proteins into mitochondria. Clogging of the TOM pore with a precursor protein causes proteotoxic stress and eventually cell death. Two quality control pathways remove translocation-stalled precursor proteins. In the mitochondrial protein translocation-associated degradation (mitoTAD), Ubx2 recruits the cytosolic AAA-ATPase Cdc48 to clear precursor proteins from the TOM complex. In the mitochondrial compromised protein import response (mitoCPR), the stress-induced Cis1 recruits the AAA-ATPase Msp1 to Tom70. The role of Msp1 for the removal of mitochondrial precursor proteins remains unknown. Here, we demonstrate that parallel loss of Msp1 and Ubx2 strongly affects removal of precursor proteins and cell viability. Msp1 and Ubx2 bind independently of import stress and Cis1 to the TOM complex to remove a large variety of precursor proteins. Msp1-dependent extraction promotes ubiquitylation of precursor proteins, which in turn allows Ubx2-recruited Cdc48 to transfer the substrates to proteasomal degradation. We conclude that two AAA-ATPases cooperate in mitochondrial precursor quality control. Msp1-dependent extraction from the TOM complex facilitates precursor ubiquitylation and Cdc48-mediated transfer to proteasomal degradation.

molecular biology↗