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Capsid destabilization and epitope alterations of human papillomavirus 18 in the presence of thimerosal

Journal of Pharmaceutical Analysis 2021年第5期11卷 617-627页

作者： Xiaofen Huang Yike Li Meifeng Nie Mingxi Yue Yufang Li Zhijie Lin Huirong Pan mujin fang Ting Wu Shaowei Li Jun Zhang Ningshao Xia Qinjian Zhao State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics National Institute of Diagnostics and Vaccine Development in Infectious DiseasesSchool of Public HealthXiamen UniversityXiamenFujian361102China School of Public Health Xiamen UniversityXiamenFujian361102China School of Life Science Xiamen UniversityXiamenFujian361102China Xiamen Innovax Biotech Company XiamenFujian361005China

Thimerosal has been widely used as a preservative in drug and vaccine products for *** to the strong propensity to modify thiols in proteins,conformational changes could occur due to covalent bond formation between ethylmercury(a degradant of thimerosal)and *** a conformational change could lead to partial or even complete loss of desirable protein *** study aims to investigate the effects of thimerosal on the capsid stability and antigenicity of recombinant human papillomavirus(HPV)18 virus-like particles(VLPs).Dramatic destabilization of the recombinant viral capsid upon thimerosal treatment was *** a negative effect on the thermal stability of VLPs preserved with thimerosal was shown to be dependent on the thimerosal *** highly neutralizing antibodies,13H12 and 3C3,were found to be the most sensitive to thimerosal *** kinetics of antigenicity loss,when monitored with 13H12 or 3C3 as probes,yielded two distinctly different sets of kinetic parameters,while the data from both monoclonal antibodies(mAbs)followed a biphasic exponential decay *** potential effect of thimerosal on protein function,particularly for thiolcontaining proteinaceous active components,needs to be comprehensively characterized during formulation development when a preservative is necessary.

关键词： Thiol-modifying agent Monoclonal antibody Antigenicity loss Epitope-specific Conformational stability

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