Characteristics of Epstein-Barr virus envelope protein gp42.
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.
Shaw
Pamela L
PL
Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Kirschner
Austin N
AN
Jardetzky
Theodore S
TS
Longnecker
Richard
R
D000595:Amino Acid Sequence; D002118:Calcium / Q000378:metabolism; D019295:Computational Biology; D006023:Glycoproteins / Q000235:genetics / Q000502:physiology*; D004854:Herpesvirus 4, Human / Q000235:genetics / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017385:Sequence Homology; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*; D053586:Virus Internalization
C101688:BZLF2 protein, Herpesvirus 4, Human; D006023:Glycoproteins; D014764:Viral Proteins; D002118:Calcium