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. 2020 Apr 30;11:697. doi: 10.3389/fmicb.2020.00697

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Copyright © 2020 Liu, Wang, Zhang, Yang, Bai, Zheng, Zheng, Wang, Li and Zhang.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The functional domain of serine incorporator 5 (SERINC5) required for hepatitis B virus (HBV) inhibition. (A) Schematic diagram of the transmembrane domains of SERINC5 and its mutants. The structure was predicted by Transmembrane Prediction using Hidden Marow Models (TMHMM) on a public server (http://www.cbs.dtu.dk/services/TMHMM-2.0/). (B–D) The effect of wild-type (WT) SERINC5 and SERINC5 truncated mutants on hepatitis B surface antigen (HBsAg) and HBV virion secretion. HepG2 cells were co-transfected as indicated. (B) Immunoblot analysis of SERINC5 and SERINC5 mutants using anti-HA antibody, tubulin served as a loading control. (C) The culture supernatants were monitored by HBsAg ELISA. HBsAg in the absence of SERINC5 was set as 100%. (D) Virion DNA from culture supernatant was detected by qPCR following the immunoprecipitation with anti-S Abs conjugated to protein G beads. HBV virion DNA in the absence of SERINC5 was set as 100% (n = 3, mean ± SD, **P < 0.01, ***P < 0.001, paired t-test). The effect of WT SERINC5 and SERINC5 mutants on the glycosylation of LHB (E) and MHB (F) proteins. HEK293T cells were co-transfected as indicated and then harvested for immunoblot analysis 48 h post-transfection. Immunoblot analysis of SERINC5, LHB, and MHB expression using anti-HA or anti-flag antibodies. The glycosylated (gp or ggp) and non-glycosylated (p) forms of LHB (L), and MHB (M) proteins are indicated. Tubulin served as a loading control. Quantitation of bands corresponding to the proteins of interest was performed using the ImageJ software and was shown below each panel (n = 3, mean ± SD).