Disease relevance of EBNA1BP2

• EBNA1 partitions Epstein-Barr virus plasmids in yeast cells by attaching to human EBNA1-binding protein 2 on mitotic chromosomes [1].

High impact information on EBNA1BP2

• EBNA1 expression alone did not enable the stable segregation of FR-containing plasmids in yeast, but segregation was rescued by human EBP2 [2].
• When expressed in yeast, hEBP2 undergoes the same cell cycle-regulated association with the mitotic chromatin as in human cells, and using yeast temperature-sensitive mutant strains, we found that the attachment of hEBP2 to mitotic chromosomes was dependent on the Ipl1 kinase [3].
• We have previously identified a mitotic chromosomal protein, human EBNA1 binding protein 2 (hEBP2), which binds to EBNA1 and enables EBNA1 to partition EBV-based plasmids in Saccharomyces cerevisiae [3].
• P40 was not detected in normal human kidney, liver, and leukocytes but was readily demonstrable in a variety of human malignant tissues [4].
• EBNA1BP2, involved in ribosome biogenesis, is an example of such a gene, with its depletion arresting MCF10A at G1/S in a p53-dependent manner [5].

Biological context of EBNA1BP2

• The human p40/EBP2 gene is located in chromosome 1 with nine exons and eight introns [6].
• An EBNA1 mutant (delta325-376) disrupted for EBP2 binding and segregation function was nuclear but failed to attach to the cellular chromosomes in mitosis [7].
• Hybridization analyses demonstrate that the amount of RcC/EBP-2 mRNAs in tadpole liver remains constant throughout metamorphosis, whereas RcC/EBP-1 mRNAs are up-regulated during both spontaneous and TH-induced metamorphosis [8].

Anatomical context of EBNA1BP2

• A novel Plasmodium falciparum erythrocyte binding protein-2 (EBP2/BAEBL) involved in erythrocyte receptor binding [9].
• Maintenance of Epstein-Barr virus-derived episomal vectors in the murine Sp2/0 myeloma cell line is dependent upon exogenous expression of human EBP2 [10].
• When the lesions were located primarily in the ventro-posterior thalamus, the SEP changes consisted of the following combination: absence of response; decrease in response amplitude; delay in peak latency; and attenuation of median N20-P25 and tibial P40 [11].

Associations of EBNA1BP2 with chemical compounds

• Similar to EBA-175, the binding of EBP2/BAEBL to human erythrocytes was dependent on sialic acids because neuraminidase treatment of those erythrocytes rendered them incapable of binding, but differed from EBA-175 in that trypsin treatment decreased EBP2/BAEBL binding by only twofold compared to a 10-fold reduction in EBA-175 binding [9].

Analytical, diagnostic and therapeutic context of EBNA1BP2

• However, we were able to obtain long-term episome maintenance in Sp2/0 cells after exogenously expressing human EBP2 by genetic engineering [10].

References