Catalog No.
RVV15103
Species reactivity
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4), Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4)
Host species
Human
Isotype
IgG1, kappa
Clonality
Monoclonal
Target
Envelope glycoprotein H, gH, BXLF2
Concentration
1.55 mg/ml
Endotoxin level
Please contact with the lab for this information.
Purity
>95% as determined by SDS-PAGE.
Purification
Protein A/G purified from cell culture supernatant.
Accession
P03231, K9US75
Applications
ELISA, FCM, IF
Form
Liquid
Storage buffer
0.01M PBS, pH 7.4.
Stability and Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4°C short term (1-2 weeks). Store at -20°C 12 months. Store at -80°C long term.
Clone ID
769B10
The structural basis of herpesvirus entry. PMID: 33087881
Immunization with a self-assembling nanoparticle vaccine displaying EBV gH/gL protects humanized mice against lethal viral challenge. PMID: 35705092
Immunization with Components of the Viral Fusion Apparatus Elicits Antibodies That Neutralize Epstein-Barr Virus in B Cells and Epithelial Cells. PMID: 30979688
gH/gL supercomplexes at early stages of herpesvirus entry. PMID: 26849495
Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition. PMID: 36306784
Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells. PMID: 9621012
Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion. PMID: 16973550
Functional analysis of glycoprotein L (gL) from rhesus lymphocryptovirus in Epstein-Barr virus-mediated cell fusion indicates a direct role of gL in gB-induced membrane fusion. PMID: 19457993
Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus. PMID: 27094060
Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry. PMID: 23107819
The large groove found in the gH/gL structure is an important functional domain for Epstein-Barr virus fusion. PMID: 23325693
Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex. PMID: 21149717
Functional homology of gHs and gLs from EBV-related gamma-herpesviruses for EBV-induced membrane fusion. PMID: 17477951
Epstein-Barr Virus Fusion with Epithelial Cells Triggered by gB Is Restricted by a gL Glycosylation Site. PMID: 28956769
Epstein-Barr virus gH is essential for penetration of B cells but also plays a role in attachment of virus to epithelial cells. PMID: 10864642
The KGD motif of Epstein-Barr virus gH/gL is bifunctional, orchestrating infection of B cells and epithelial cells. PMID: 22215569
The Epstein-Barr virus (EBV) BZLF2 gene product associates with the gH and gL homologs of EBV and carries an epitope critical to infection of B cells but not of epithelial cells. PMID: 7539502
The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment. PMID: 27935841
Plxdc family members are novel receptors for the rhesus monkey rhadinovirus (RRV). PMID: 33657166
Antibody Generation and Immunogenicity Analysis of EBV gp42 N-Terminal Region. PMID: 34960650
An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus. PMID: 29669253
Binding-site interactions between Epstein-Barr virus fusion proteins gp42 and gH/gL reveal a peptide that inhibits both epithelial and B-cell membrane fusion. PMID: 17581996
Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies. PMID: 28939750
Comparative Mutagenesis of Pseudorabies Virus and Epstein-Barr Virus gH Identifies a Structural Determinant within Domain III of gH Required for Surface Expression and Entry Function. PMID: 26656711
Immunoinformatic and systems biology approaches to predict and validate peptide vaccines against Epstein-Barr virus (EBV). PMID: 30679646
The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cells. PMID: 25231307
The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells. PMID: 16160168
Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry. PMID: 19217393
Cleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes. PMID: 19369343
Gammaherpesvirus entry and fusion: A tale how two human pathogenic viruses enter their host cells. PMID: 31439152
Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins. PMID: 15583133
Assembly and architecture of the EBV B cell entry triggering complex. PMID: 25144748
Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacers. PMID: 25564465
The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope protein whose processing is dependent on coexpression with the BMRF2 protein. PMID: 18995876
Coreceptor restriction within the HLA-DQ locus for Epstein-Barr virus infection. PMID: 10908662
Epstein-Barr virus entry utilizing HLA-DP or HLA-DQ as a coreceptor. PMID: 10666279
Alternate replication in B cells and epithelial cells switches tropism of Epstein-Barr virus. PMID: 12042810
Epstein-Barr virus infection of polarized epithelial cells via the basolateral surface by memory B cell-mediated transfer infection. PMID: 21573183
Epstein-Barr virus lacking glycoprotein gp42 can bind to B cells but is not able to infect. PMID: 9420211
Epstein-Barr virus uses HLA class II as a cofactor for infection of B lymphocytes. PMID: 9151859
Capacity of Epstein-Barr virus to infect monocytes and inhibit their development into dendritic cells is affected by the cell type supporting virus replication. PMID: 15448337
For research use only. Not for human or drug use.
