gp42 is a type II transmembrane glycoprotein essential for EBV’s dual-tropic infection of B cells and epithelial cells . Key functional attributes include:
Tropism Regulation: gp42 binds to HLA-II on B cells, triggering membrane fusion via interactions with viral gH/gL complexes .
Conformational Switching: Its N-terminal domain (residues 36–81) mediates high-affinity binding to gH/gL, while the C-terminal lectin domain engages HLA-II .
Epithelial Cell Entry: Virions lacking gp42 preferentially infect epithelial cells due to reduced HLA-II binding .
| Domain | Residues | Binding Partner | Role in Infection |
|---|---|---|---|
| N-terminal | 36–81 | gH/gL | Membrane fusion initiation |
| C-terminal (CTLD) | 159–206 | HLA-II | B cell entry triggering |
Recent studies describe human and murine monoclonal antibodies (mAbs) neutralizing EBV by targeting gp42:
2B7 and 2C1: Human mAbs isolated via single B cell cloning. Both neutralize EBV in B cells and epithelial cells by binding distinct gp42 epitopes outside the HLA-II interface .
F-2-1: Murine mAb blocking HLA-II binding, effective only against B cell infection .
| Antibody | Species | Neutralization Scope | Key Epitope | Efficacy in Humanized Mice |
|---|---|---|---|---|
| 2C1 | Human | B cells, epithelial | Hydrophobic patch (aa 159–206) | 95% infection reduction |
| 2B7 | Human | B cells, epithelial | N-terminal (aa 44–81) | 80% infection reduction |
| F-2-1 | Murine | B cells | HLA-II interface | Limited data |
Spp42 antibody plays a crucial role in pre-mRNA splicing. It may also participate in endoplasmic reticulum-associated protein degradation (ERAD) and is essential for growth under both low and high temperatures. Spp42 is required for pre-spliceosome formation, the initial step in pre-mRNA splicing. This protein interacts with snRNP U5 and plays a significant role in branch site-3' splice site selection. It associates with the branch site-3' splice 3'-exon region.
KEGG: spo:SPAC4F8.12c
STRING: 4896.SPAC4F8.12c.1