Abstract
The viral tegument is a layer of proteins between the herpesvirus capsid and its outer envelope. According to phylogenetic studies, only a third of these proteins are conserved amongst the three subfamilies (Alpha-, Beta- and Gammaherpesvirinae) of the family Herpesviridae. Although some of these tegument proteins have been studied in more detail, the structure and function of the majority of them are still poorly characterized. VP22 from Herpes simplex virus 1 (subfamily Alphaherpesvirinae) is a highly interacting tegument protein that has been associated with tegument assembly. We have determined the crystal structure of the conserved core domain of VP22, which reveals an elongated dimer with several potential protein–protein interaction regions and a peptide-binding site. The structure provides us with the structural basics to understand the numerous functional mutagenesis studies of VP22 found in the literature. It also establishes an unexpected structural homology to the tegument protein ORF52 from Murid herpesvirus 68 (subfamily Gammaherpesvirinae). Homologues for both VP22 and ORF52 have been identified in their respective subfamilies. Although there is no obvious sequence overlap in the two subfamilies, this structural conservation provides compelling structural evidence for shared ancestry and functional conservation.
Highlights
Human herpesviruses are known to cause vastly different diseases/illnesses that range from mild oral-facial blisters and chicken pox to fatal conditions such as Burkitt’s lymphoma and Kaposi’s sarcoma (Antman & Chang, 2000; Davison, 2007; Whitley & Roizman, 2001)
Twenty-four different tegument proteins have been identified in Herpes simplex virus 1 (HSV-1; Human herpesvirus 1) but, judging from sequence alignments, only a third of them are conserved across all the subfamilies (Alpha, Betaand Gammaherpesvirinae) of the family Herpesviridae (Kelly et al, 2009)
VP22core crystallized in the space group P6122 and the crystal structure [Protein Data Bank (PDB) ID: 4XAL] was determined at a resolution of 1.87 Ausing single isomorphous replacement with anomalous scattering (SIRAS)
Summary
Human herpesviruses are known to cause vastly different diseases/illnesses that range from mild oral-facial blisters and chicken pox to fatal conditions such as Burkitt’s lymphoma and Kaposi’s sarcoma (Antman & Chang, 2000; Davison, 2007; Whitley & Roizman, 2001). To generate insight into the VP22 structure and function, we crystallized and solved the structure of the conserved Cterminal domain of this protein, hereafter referred to as VP22core, to a resolution of 1.9 A . Similar to VP22core, ORF52MHV-68 is a highly expressed tegument protein that exists as a dimer made up of two identical monomers (Benach et al, 2007; Bortz et al, 2007).
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.
