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Zhang, Tian-Ying; Chen, Hong-Ying; Cao, Jia-Li; Xiong, Hua-Long; Mo, Xiao-Bing; Li, Tian-Liang; Kang, Xiao-Zhen; Zhao, Jing-Hua; Yin, Bo; Zhao, Xiang; Huang, Cheng-Hao; Yuan, Quan; Xue, Ding; Xia, Ning-Shao; Yuan, Y Adam
Nature communications, 07/2019, Volume: 10, Issue: 1Journal Article
Hepatitis B virus (HBV) X protein, HBx, interacts with anti-apoptotic Bcl-2 and Bcl-xL proteins through its BH3-like motif to promote HBV replication and cytotoxicity. Here we report the crystal structure of HBx BH3-like motif in complex with Bcl-xL where the BH3-like motif adopts a short α-helix to snuggle into a hydrophobic pocket in Bcl-xL via its noncanonical Trp120 residue and conserved Leu123 residue. This binding pocket is ~2 Å away from the canonical BH3-only binding pocket in structures of Bcl-xL with proapoptotic BH3-only proteins. Mutations altering Trp120 and Leu123 in HBx impair its binding to Bcl-xL in vitro and HBV replication in vivo, confirming the importance of this motif to HBV. A HBx BH3-like peptide, HBx-aa113-135, restores HBV replication from a HBx-null HBV replicon, while a shorter peptide, HBx-aa118-127, inhibits HBV replication. These results provide crucial structural and functional insights into drug designs for inhibiting HBV replication and treating HBV patients.
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