EBV type 1 (DAG3069)

EBV type 1 (aa 340), recombinant protein from P. pastoris

Product Overview
Recombinant Epstein-Barr Virus Antigen
Specificity
Truncated to 340 aa, glycine-alanine repeats removed
Nature
Recombinant
Tag/Conjugate
Unconjugated
Procedure
None
Purity
95% by SDS-PAGE
Buffer
PBS, pH 7.2
Preservative
0.1% Sodium Azide
Storage
2-8°C short term, -20°C long term
Introduction
The Epstein–Barr virus (EBV), also called human herpesvirus 4 (HHV-4), is a virus of the herpes family, and is one of the most common viruses in humans. It is best known as the cause of infectious mononucleosis (glandular fever). It is also associated with particular forms of cancer, such as Hodgkin's lymphoma, Burkitt's lymphoma, nasopharyngeal carcinoma, and conditions associated with human immunodeficiency virus (HIV) such as hairy leukoplakia and central nervous system lymphomas. There is evidence that infection with the virus is associated with a higher risk of certain autoimmune diseases, especially dermatomyositis, systemic lupus erythematosus, rheumatoid arthritis and multiple sclerosis.
Antigen Description
Epstein-Barr virus (EBV) nuclear antigen 1 (EBNA1) is the one EBV antigen that is expressed in all EBV associated malignancies. It has long been thought to go undetected by the cell mediated immune system. However, recent studies show that EBNA1 can be pr
Keywords
Epstein-Barr virus nuclear antigen 1; EBV EBNA-1

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References


ROLE OF SURGERY IN TREATING EPSTEIN-BARR VIRUS-ASSOCIATED SMOOTH MUSCLE TUMOR (EBV-SMT) WITH CENTRAL NERVOUS SYSTEM INVASION: A SYSTEMIC REVIEW

NEURO-ONCOLOGY

Authors: Chen, Ko-Ting; Lau, Ka-Wei; Hsu, Yu-Wei; Lin, Yin-Ting

HLA-DPB1 and Epstein-Barr virus gp42 protein jointly contribute to the development of Hodgkin lymphoma

TRANSLATIONAL CANCER RESEARCH

Authors: Li, Hongyu; Liu, Dan; Li, Xun

Background: Epstein-Barr virus (EBV) glycoprotein 42 (gp42) enters B lymphocytes by binding to the human leukocyte antigen II (HLA-II) on their surface, in a process involving other EBV proteins (e.g., gH/gL and gp350). From a latent state of infection, the virus may reactivate and enter into a rapid proliferation phase, which enables the further entry of EBV into B lymphocytes and epithelial cells, leading to tumor development. EBV is an oncogenic virus associated with Hodgkin lymphoma (HL), and gp42 is a key protein in EBV infection of B lymphocytes. However, the exact binding pattern and capacity of gp42 are unclear. Methods: The patterns and morphologies of gp42 binding to HLA-DPB1 were obtained through molecular dynamics simulation. The binding efficiency of gp42 and HLA-DPB1 was verified by plasmid construction and flow cytometry. Results: The beta-chain of HLA-DPB1 and the a-chain of gp42 formed a hydrogen-bonded complex, which was a hydrophilic protein with a resolution of 3.25. The binding efficiency between HLA-DPB1 and gp42 reached its peak (range, 26-31.3%) at a gp42 protein concentration of 80 mu g. Conclusions: We can inhibit the binding of gp42 to HLA-DPB1 by reducing the concentration of gp42. In the subsequent experiments, we will verify whether the binding of gp42 to HLA-DPB1 can be prevented by breaking hydrogen bonds and destroying hydrophilicity. These data may provide certain reference value for the development and treatment of Hodgkin's lymphoma.

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