EBV (LMP1) Peptide Pool

Peptide pool of 59 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Trans-activator protein BZLF1 (UniProt ID: P03206) of Epstein-Barr virus (HHV4) for T cell assays. One unit allows the stimulation of 2,5 x 108 cells.

The EBV (EBNA-3a) Peptide Pool from peptides&elephants is designed for in vitro T cell stimulation and epitope analysis in research on Epstein-Barr virus (EBV, HHV-4). This pool contains 234 synthetic 15-mer peptides, overlapping by 11 amino acids, and spans the complete sequence of EBNA-3a (Epstein-Barr nuclear antigen 3a; UniProt ID: P12977). Each unit enables the stimulation of up to 2.5 × 10⁸ peripheral blood mononuclear cells (PBMCs) and is ideal for use in ELISpot, intracellular cytokine staining (ICS), and flow cytometry-based T cell assays. Scientific Background EBV is a ubiquitous herpesvirus that infects more than 90% of the global population. It is the causative agent of infectious mononucleosis and is closely associated with several B cell malignancies, including post-transplant lymphoproliferative disease (PTLD), diffuse large B cell lymphoma (DLBCL), Burkitt lymphoma, and Hodgkin lymphoma. During latency, EBV can enter different gene expression programs. Latency type III, in which all nine latent proteins are expressed, is the only form capable of transforming B cells in vitro, resulting in lymphoblastoid cell lines (LCLs). Among these latency proteins, EBNA-3a plays a supportive but non-essential role in B cell transformation: EBV mutants lacking EBNA-3a can still transform B cells, but with significantly reduced efficiency. EBNA-3a–deficient LCLs proliferate more slowly and show increased apoptosis compared to wild-type virus–derived LCLs. EBNA-3a appears to regulate a subset of cellular genes, some of which overlap with those regulated by EBNA2. The two proteins can act antagonistically or cooperatively to control gene expression. These findings position EBNA-3a as a key modulator of B cell proliferation and survival during EBV latency, and as a relevant CD8⁺ T cell target in both basic immunological studies and translational research.

Peptide pool of 234 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Epstein-Barr nuclear antigen 4 (EBNA3b) (UniProt ID: Q1HVG4) of Epstein-Barr virus (HHV4) for T cell assays. One unit allows the stimulation of 2,5 x 108 cells.

Peptide pool of 224 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Envelope glycoprotein GP350/GP340 (UniProt ID: P03200) of Epstein-Barr virus (EBV, Humanes Herpesvirus 4, HHV4). One unit allows the stimulation of 2,5 x 108 cells. gp350/gp340 versus gp350/220 The EBV envelope glycoprotein gp350/gp340 (or gp350/220) is encoded by the BLLF1 gene and represents one of the most abundant surface proteins of the virion. The protein exists in multiple isoforms generated by alternative splicing. While gp350 denotes the full-length form, gp340 and gp220 refer to truncated isoforms of the same glycoprotein, which retain identical biological function. Differences in naming (gp340 vs. gp220) arise from historical nomenclature, experimental detection methods, and variations in glycosylation state.  Initial attachment and endocytosis Gp350/gp340 belongs to the core set of EBV glycoproteins that define viral tropism and host cell interaction – together with gp42, BMRF2, gH/gL, and gB. Gp350/gp340 plays a central role in viral attachment and entry into B lymphocytes. Through molecular mimicry of complement components, gp350/gp340 specifically recognizes complement receptor 1 (CR1/CD35) and complement receptor 2 (CR2/CD21) on B cells. This interaction mediates the initial attachment of EBV particles and triggers endocytosis of the immobilized virion, marking the first step of EBV infection in B lymphocytes. Major target of immune responses Due to its surface exposure, high abundance, and essential role in viral entry, gp350/gp340 represents a major target of humoral and cellular immune responses. Peptides derived from gp350/gp340 are widely used to study EBV-specific T cell immunity, epitope recognition, and immune monitoring in the context of EBV infection, EBV-associated malignancies, and vaccine development. The EBV (gp350/gp340) Peptide Pool from peptides&elephants provides comprehensive sequence coverage of this key viral glycoprotein and is ideally suited for applications such as T cell stimulation assays, epitope mapping, and immunological profiling in EBV research.

Peptide pool of 27 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Latent membrane protein 2A (LMP2A) (UniProt ID: A8CDV5) of Epstein-Barr virus (HHV4) for T cell assays. One unit allows the stimulation of 2,5 x 108 cells.

Peptide pool of 53 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Secreted protein BARF1 (UniProt: P03225) of Homo sapiens Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4). One unit allows the stimulation of 2,5 x 108 cells.

This peptide pool consists of 26 peptides, each corresponding to a defined HLA class I-restricted T cell epitope from Epstein-Barr virus (EBV). One unit allows the stimulation of 2,5 x 108 cells.

Peptide pool of 158 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Epstein-Barr nuclear antigen 1 (EBNA1) (Uniprot ID: P03211) of Epstein-Barr virus (HHV4) for T cell assays. One unit allows the stimulation of 2,5 x 108 cells.

The EBV EBNA-2 Peptide Pool from peptides&elephants is designed for reliable stimulation and detection of EBV-specific T-cell responses in immunological research. The pool consists of 119 overlapping peptides (15-mers with an 11-amino-acid overlap) spanning Epstein–Barr nuclear antigen 2 (EBNA2) from Epstein–Barr virus strain B95-8 (UniProt ID: P12978). The Epstein-Barr virus is also known as Human herpesvirus 4 (HHV-4).  EBNA2 is one of the earliest viral proteins expressed after infection of B cells and acts as a central transcriptional regulator that reprograms host and viral gene expression. Through interactions with numerous sites in the host genome, EBNA2 cooperates with EBNA-LP to activate key cellular pathways, including transient activation of the MYC proto-oncogene, which drives early B-cell proliferation and supports survival during the establishment of EBV latency. EBNA2 activity also contributes to the transition from the initial Wp promoter–driven transcription toward the Cp promoter–controlled latency program IIb, in which multiple EBV nuclear antigens are expressed from a polycistronic transcript. This shift allows the virus to balance rapid proliferation with controlled persistence. Learn more about EBNA2-mediated transcriptional reprogramming and MYC regulation during early EBV infection in the Peptide Insights section of peptides&elephants. Applications Suitable for multiple T-cell–based assays, including: ELISpot assays Intracellular cytokine staining (ICS) FluoroSpot assays T-cell proliferation assays Immune monitoring in EBV research Capacity One unit allows the stimulation of 2.5 × 10⁸ cells. The EBV EBNA-2 Peptide Pool provides a comprehensive tool for studying EBV-specific immune responses, latency establishment, and virus-host interactions in basic and translational research.