Heat shock protein 70 inhibits hepatitis B virus replication by enhancing the deaminase activity of apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3B

VernacularTitle:热休克蛋白70通过增强载脂蛋白B mRNA编辑酶催化多肽样蛋白3B的脱氨酶活性抑制乙型肝炎病毒复制
Author: Yanmeng CHEN ¹ ; Xiaochuan ZHENG ; Yuan HU
Author Information

1. 重庆医科大学检验医学院，重庆　400016
Keywords: Hepatitis B virus; APOBEC3B; HSP70; Deamination
From: Chinese Journal of Microbiology and Immunology 2023;43(7):502-508
CountryChina
Language:Chinese
Abstract: Objective:To study the role and mechanism of heat shock protein 70 (HSP70) in apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3B (APOBEC3B)-mediated inhibition of hepatitis B virus(HBV) replication.Methods:The interaction between HSP70 and APOBEC3B was analyzed by co-immunopreciptation (Co-IP) and GST pull-down. After treating Huh7 cells with siHSP70 or HSP70 inhibitor VER155008 or overexpressing HSP70 in Huh7 cells, changes in the antiviral effect of APOBEC3B were detected by Southern blot and real-time PCR; the deaminase activity of APOBEC3B was tested by differential DNA denaturation PCR(3D-PCR) and clone sequencing.Results:HSP70 could bind to APOBEC3B. Overexpression of HSP70 promoted the deaminase activity and anti-HBV activity of APOBEC3B. On the contrary, knockdown of HSP70 or using HSP70 inhibitor VER155008 would attenuate the deaminase activity and anti-HBV activity of APOBEC3B.Conclusions:HSP70 could promote the anti-HBV activity of APOBEC3B by enhancing the deaminase activity of APOBEC3B.