Abstract
White spot syndrome virus (WSSV) is one of the major and most serious pathogen in the shrimp industry. As one of the most abundant envelope protein, VP24 acts as a core protein interacting with other structure proteins and plays an important role in virus assembly and infection. Here, we have presented the crystal structure of VP24 from WSSV. In the structure, VP24 consists of a nine-stranded β–barrel fold with mostly antiparallel β-strands, and the loops extending out the β–barrel at both N-terminus and C-terminus, which is distinct to those of the other two major envelope proteins VP28 and VP26. Structural comparison of VP24 with VP26 and VP28 reveals opposite electrostatic surface potential properties of them. These structural differences could provide insight into their differential functional mechanisms and roles for virus assembly and infection. Moreover, the structure reveals a trimeric assembly, suggesting a likely natural conformation of VP24 in viral envelope. Therefore, in addition to confirming the evolutionary relationship among the three abundant envelope proteins of WSSV, our structural studies also facilitate a better understanding of the molecular mechanism underlying special roles of VP24 in WSSV assembly and infection.
Highlights
White spot syndrome virus (WSSV) is a rod-shaped enveloped virus with a large, double-stranded DNA genome[1,2,3,4], and belongs to the family Nimaviridae as the sole member of a novel genus Whispovirus[5,6]
Previous studies have showed that VP28 is crucial for virus entry involving in attaching and penetrating into host cells[16,17], while VP24 could not bind to host cell membrane though it could interact with VP28 to form a protein complex and participate in virus infection together[18,19]
Studies have further shown VP24 could bind with many other structural proteins including VP28, VP26, VP19, VP33, VP38, VP51A, VP53A and wsv[010] for its function in WSSV infection or morphogenesis[11,20,21,22,23]
Summary
Syndrome Virus received: 18 April 2016 accepted: 01 August 2016 Published: 30 August 2016. As one of the most abundant envelope protein, VP24 acts as a core protein interacting with other structure proteins and plays an important role in virus assembly and infection. Structural comparison of VP24 with VP26 and VP28 reveals opposite electrostatic surface potential properties of them These structural differences could provide insight into their differential functional mechanisms and roles for virus assembly and infection. In addition to confirming the evolutionary relationship among the three abundant envelope proteins of WSSV, our structural studies facilitate a better understanding of the molecular mechanism underlying special roles of VP24 in WSSV assembly and infection. In addition to confirming the evolutionary conservation among the three abundant envelope proteins of WSSV, VP24, VP26 and VP28, our structural studies provide insight into a better understanding of the molecular mechanism underlying special roles of VP24 in WSSV infection and assembly
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
