Abstract
BackgroundPapillomavirus binding factor (PBF) or zinc finger protein 395 is a transcription factor associated to a poor prognosis in patients with osteosarcoma, an aggressive bone cancer that predominantly affects adolescents. To investigate the role of the PBF protein in the osteosarcoma genesis, in this paper we present the bioinformatics analysis of physicochemical properties of PBF and its probable interactions with several key cellular targets.ResultsThe physicochemical characteristics determined to PBF, disorder-promoting amino acids, flexibility, hydrophobicity, prediction of secondary and tertiary structures and probability to be crystallized, supported that this protein can be considered as an intrinsically disordered protein (IDP), with a zinc finger-like domain. The in silico analysis to find out PBF interactions with cellular factors, confirmed the experimentally demonstrated interaction of PBF with two key cellular proteins involved in regulation of cellular apoptosis, 14-3-3β and Scythe/BAT3 proteins. Furthermore, other interactions were found with proteins like HDAC1 and TPR which are known to be deregulated in several cancers. Experimental confirmation of specific interactions will contribute to understand the osteosarcoma process and might lead to the identification of new targets for diagnosis and treatments.ConclusionsAccording to the in silico PBF analyses, this protein can be considered as an IDP capable to bind several key cellular factors, and these interactions might play an important role in the osteosarcoma process.
Highlights
Papillomavirus binding factor (PBF) or zinc finger protein 395 is a transcription factor associated to a poor prognosis in patients with osteosarcoma, an aggressive bone cancer that predominantly affects adolescents
All these evidences have suggested that PBF has a central role in osteosarcoma genesis, and PBF might be used as a potential therapeutic target for anti-cancer drugs
To investigate the role of the PBF protein in the osteosarcoma carcinogenesis process, we analyzed if the PBF protein could be considered as an intrinsically disordered protein (IDP)
Summary
Papillomavirus binding factor (PBF) or zinc finger protein 395 is a transcription factor associated to a poor prognosis in patients with osteosarcoma, an aggressive bone cancer that predominantly affects adolescents. Osteosarcoma is the most common type of bone cancer It is a very aggressive cancer and is the sixth leading cancer in children under age 15, and more than 92% of biopsy specimens of osteosarcoma have shown a protein known as papillomavirus binding factor (PBF) highly expressed in the cellular nucleus [1]. Overexpression of PBF has been reported in many cases of bone and soft tissue sarcoma and epithelial carcinomas [1] All these evidences have suggested that PBF has a central role in osteosarcoma genesis, and PBF might be used as a potential therapeutic target for anti-cancer drugs. In 2008 Tsukahara et al, [1] developed a synthetic antigenic peptide from PBF capable to induce cytotoxic T lymphocytes from an HLA-A24-positive patient which killed an osteosarcoma cell line expressing PBF and HLA-A24
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