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Previous reports have shown that glycolysis and gluconeogenesis are among the most deregulated pathways during HBV infection. We noted that despite being one of the rate\u2010limiting enzymes of gluconeogenesis, the role and regulation of Fructose\u20101,6\u2010bisphosphatase 1 (FBP1) during HBV infection is not much explored. In this study, we report FBP1 upregulation upon HBV infection and unravel a novel mechanism of epigenetic reprogramming of FBP1 by HBV via utilizing host factor Speckled 110\u2009kDa (Sp110). Here, we identified acetylated lysine 18 of histone H3 (H3K18Ac) as a selective interactor of Sp110 Bromodomain. Furthermore, we found that Sp110 gets recruited on H3K18Ac\u2010enriched <jats:italic>FBP1<\/jats:italic> promoter, and facilitates recruitment of deacetylase Sirtuin 2 (SIRT2) on that site in the presence of HBV. SIRT2 in turn brings its interactor and transcriptional activator Hepatocyte nuclear factor 4\u2010alpha to the promoter, which ultimately leads to a loss of DNA methylation near the cognate site. Interestingly, this Sp110 driven <jats:italic>FBP1<\/jats:italic> regulation during infection was found to promote viral\u2010borne HCC progression. Moreover, Sp110 can be used as a prognostic marker for the hepatitis\u2010mediated HCC patients, where high Sp110 expression significantly lowered their survival. Thus, the epigenetic reader protein Sp110 has potential to be a therapeutic target to challenge HBV\u2010induced HCCs.<\/jats:p>","DOI":"10.1111\/febs.16544","type":"journal-article","created":{"date-parts":[[2022,6,2]],"date-time":"2022-06-02T16:36:45Z","timestamp":1654187805000},"page":"6694-6713","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Epigenetic regulation of Fructose\u20101,6\u2010bisphosphatase 1 by host transcription factor Speckled 110\u2009<scp>kDa<\/scp> during hepatitis B virus infection"],"prefix":"10.1111","volume":"289","author":[{"given":"Isha","family":"Sengupta","sequence":"first","affiliation":[{"name":"Biophysics and Structural Genomics Division Saha Institute of Nuclear Physics  Kolkata India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Payel","family":"Mondal","sequence":"additional","affiliation":[{"name":"Biophysics and Structural Genomics Division Saha Institute 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