Expression, Purification, and Antiserum Production of the Truncated UL31 Protein of Herpes Simplex Virus 1

Abstract

<strong>Background:</strong> The UL31 protein of herpes simplex virus 1 (HSV-1) plays an important role in the HSV-1 replication, however, its pinpoint functions in the life cycle of the virus have yet to be adequately elucidated.<br /> <strong>Objectives:</strong> An antiserum specific for detecting HSV-1 UL31 was prepared as the foundation for future research on the role of UL31 in the course of HSV-1 infection.<br /> <strong>Materials and Methods:</strong> Recombinant protein of UL31 was expressed in <em>Escherichia coli</em>, which was then purified and employed to raise the level of antiserum in mice. Subsequently, western blot and immunofluorescence assay (IFA) were utilized to detect the specific antiserum.<br /> <strong>Results:</strong> The recombinant UL31 protein consisting of N-terminal 27 aa of UL31 was fused to EYFP and His-tag. It was expressed, purified, and applied to the preparation of the antiserum. Western blot analysis and IFA demonstrated that this antiserum could detect both the recombinant UL31 and the native UL31.<br /> <strong>Conclusions:</strong> Our results manifest that this antiserum could be conducive to further investigations concerning the roles of UL31 in the HSV-1 infection.