López Ramsés, Urquiza Mauricio, Patino Helena, Suárez Jorge, Reyes Claudia, Patarroyo Manuel A, Patarroyo Manuel E
Fundación Instituto de Inmunología de Colombia (FIDIC), Universidad Nacional de Colombia, Avenida Carrera 50 No. 26-00, Bogotá, Colombia.
Biochimie. 2005 Nov;87(11):985-92. doi: 10.1016/j.biochi.2005.04.009.
Epstein-Barr virus (EBV) infects human target cells mainly through gp350/220-CD21 and gp42-MHCII interactions; however, it has been shown that these interactions are dispensable for EBV-invasion of susceptible cells, suggesting that other viral proteins are involved in this process. It is probable that tegument BNRF1/p140 protein is involved in EBV-invasion of target cells, since anti-p140 antibodies inhibit EBV-infection of B-lymphocytes and there is evidence that part of the protein is located on virus surface. Sixty-six peptides, covering the entire BNRF1/p140 sequence, were synthesised and tested in lymphoblastoid cell line binding assays. Peptides 11465 and 11521 bound with high affinity to Raji, Ramos and P3HR-1 cells but not to erythrocytes, showing cell-binding behaviour similar to EBV. These two peptides induced antibodies recognising live EBV-infected cells. Interestingly, peptide-11521 (YVLQNAHQIACHFHSNGTDA) or antibodies induced by this peptide inhibited EBV-binding to B-lymphocytes, suggesting that this p140-region could be involved in EBV and B-lymphocyte interaction.
