6TM8

Crystal structure of glycoprotein D of Equine Herpesvirus Type 4

Summary for 6TM8

• Entry DOI: 10.2210/pdb6tm8/pdb
• Descriptor: Envelope glycoprotein D, GLYCEROL (3 entities in total)
• Functional Keywords: glycoprotein d; equine herpesvirus type 4; ehv-4, viral entry, viral protein
• Biological source: Equid alphaherpesvirus 4 (Equine herpesvirus 4)
• Total number of polymer chains: 1
• Total formula weight: 38392.03

Authors

Kremling, V.,Loll, B.,Osterrieder, N.,Wahl, M.,Dahmani, I.,Chiantia, P.,Azab, W. (deposition date: 2019-12-03, release date: 2020-11-11, Last modification date: 2024-02-07)

Primary citation

Kremling, V.,Loll, B.,Pach, S.,Dahmani, I.,Weise, C.,Wolber, G.,Chiantia, S.,Wahl, M.C.,Osterrieder, N.,Azab, W.
Crystal structures of glycoprotein D of equine alphaherpesviruses reveal potential binding sites to the entry receptor MHC-I.
Front Microbiol, 14:1197120-1197120, 2023

PubMed Abstract: Cell entry of most alphaherpesviruses is mediated by the binding of glycoprotein D (gD) to different cell surface receptors. Equine herpesvirus type 1 (EHV-1) and EHV-4 gDs interact with equine major histocompatibility complex I (MHC-I) to initiate entry into equine cells. We have characterized the gD-MHC-I interaction by solving the crystal structures of EHV-1 and EHV-4 gDs (gD1, gD4), performing protein-protein docking simulations, surface plasmon resonance (SPR) analysis, and biological assays. The structures of gD1 and gD4 revealed the existence of a common V-set immunoglobulin-like (IgV-like) core comparable to those of other gD homologs. Molecular modeling yielded plausible binding hypotheses and identified key residues (F213 and D261) that are important for virus binding. Altering the key residues resulted in impaired virus growth in cells, which highlights the important role of these residues in the gD-MHC-I interaction. Taken together, our results add to our understanding of the initial herpesvirus-cell interactions and will contribute to the targeted design of antiviral drugs and vaccine development.

PubMed: 37250020
DOI: 10.3389/fmicb.2023.1197120

Experimental method

X-RAY DIFFRACTION (1.9 Å)