Characteristics of Epstein-Barr virus envelope protein gp42

• Published in: Virus genes Vol. 40; no. 3; pp. 307 - 319
• Main Authors: Shaw, Pamela L, Kirschner, Austin N, Jardetzky, Theodore S, Longnecker, Richard
• Format: Journal Article
• Language: English
• Published: Boston Boston : Springer US 01.06.2010; Springer US; Springer Nature B.V
• Subjects: Amino Acid Sequence; Biomedical and Life Sciences; Biomedicine; Calcium - metabolism; Computational Biology; Epstein-Barr virus; Glycoproteins - genetics; Glycoproteins - physiology; Herpesvirus 4, Human - genetics; Herpesvirus 4, Human - physiology; Medical Microbiology; Models, Molecular; Molecular Sequence Data; Phylogeny; Plant Sciences; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology; Viral Proteins - genetics; Viral Proteins - physiology; Virology; Virus Internalization; EBV; Viral entry; Gp42; Epstein–Barr virus; Glycoprotein; Herpesvirus
• ISSN: 0920-8569; 1572-994X
• DOI: 10.1007/s11262-010-0455-x

Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a membrane protein essential for fusion and entry of EBV into host B-lymphocytes. Gp42 is a member of the protein-fold family C-type lectin or lectin-like domains (CLECT or CTLD) and specifically is classified as a natural-killer receptor (NKR)-like CLECT. Literature review and phylogenetic comparison show that EBV gp42 shares a common structure with other NKR-like CLECTs and possibly with many viral CTLDs, but does not appear to exhibit some common binding characteristics of many CTLDs, such as features required for calcium binding. The flexible N-terminal region adjacent to the CTLD fold is important for binding to other EBV glycoproteins and for a cleavage site that is necessary for infection of host cells. From structural studies of gp42 unbound and bound to receptor and extensive mutational analysis, a general model of how gp42 triggers membrane fusion utilizing both the flexible N-terminal region and the CTLD domain has emerged.