Physicochemical Analysis of the Interaction between Epstein - Barr Virus Glycoprotein gp 350 and Complement Receptor 2 using AESOP ( Analysis of Electrostatic Similarities Of Proteins )

Epstein-Barr Virus (EBV) infects a large percentage of the world’s population and is responsible for infectious mononucleosis and, in rare cases, Burkitt’s lymphoma and nasopharyngeal carcinoma. EBV’s primary means of infection is the association of the viral surface glycoprotein gp350 with Complement Receptor 2 (CR2) of the immune system. Various mutagenesis studies have identified key residues on both gp350 and CR2 necessary for binding. These mutagenesis studies have recently been used to derive constraints for a computational docking study in order to generate a putative three-dimensional structure for the gp350-CR2 complex, using the soft-docking program HADDOCK (High-Ambiguity Driven biomolecular DOCKing). We have applied our own AESOP (Analysis of Electrostatic Similarities Of Proteins) protocol to analyze the electrostatic contributions to complex formation, using the HADDOCK-derived structure of the gp350-CR2 complex. Our atomic-detail studies using AESOP suggest that the original HADDOCK structure may not be optimized and warrant a re-evaluation of the docking process.