乙肝病毒核心蛋白变构调制器可以扭曲和破坏完好的衣壳。

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https://www.ncbi.nlm.nih.gov/pub ... rupt+intact+capsids

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Hepatitis B virus core protein allosteric modulators can distort and disrupt intact capsids.
Schlicksup CJ1, Wang JC1,2, Francis S3, Venkatakrishnan B1, Turner WW3, VanNieuwenhze M4, Zlotnick A1.
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Abstract
Defining mechanisms of direct-acting antivirals facilitates drug development and our understanding of virus function. Heteroaryldihydropyrimidines (HAPs) inappropriately activate assembly of hepatitis B virus (HBV) core protein (Cp), suppressing formation of virions. We examined a fluorophore-labeled HAP, HAP-TAMRA. HAP-TAMRA induced Cp assembly and also bound pre-assembled capsids. Kinetic and spectroscopic studies imply that HAP-binding sites are usually not available but are bound cooperatively. Using cryo-EM, we observed that HAP-TAMRA asymmetrically deformed capsids, creating a heterogeneous array of sharp angles, flat regions, and outright breaks. To achieve high resolution reconstruction (<4 Å), we introduced a disulfide crosslink that rescued particle symmetry. We deduced that HAP-TAMRA caused quasi-sixfold vertices to become flatter and fivefold more angular. This transition led to asymmetric faceting. That a disordered crosslink could rescue symmetry implies that capsids have tensegrity properties. Capsid distortion and disruption is a new mechanism by which molecules like the HAPs can block HBV infection.
KEYWORDS:
biochemistry; cryo-EM; direct acting antiviral; hepatitis B virus; image reconstruction; infectious disease; microbiology; self-assembly; virus