1) My long standing interest is the mechanism of viral nucleic acid packaging: Nucleic acid packaging into viral precursors is highly conserved biologically among phages and viruses. Although translocation is known to result from the ATPase activity of a packaging enzyme that interacts with a dodecameric portal vertex of the procapsid, the energetic mechanism remains to be established. We have studied intensively the phage T4 proteins (portal dodecamer and two subunit packaging enzyme) that package DNA.

2) Phage Display and encapsidation: We have developed the two protein phage T4 SOC and HOC capsid display system to reveal protein interactions important for viral packaging. These proteins enable display of full length biologically and immunologically active proteins for binding studies and development of vaccines. A phage T4 capsid targeting sequence also allows virtually any protein to be encapsidated with the DNA.

3) Phage exclusion and anti-exclusion mechanisms: A novel type IV modification dependent restriction enzyme that targets glycosylated hydroxymethyl cytosine modified DNAs has been isolated and characterized from pathogenic E. coli CT596 prophage exclusion genes ibegs and gibeg. The T-evens have evolved a diverse family of capsid-targeted internal proteins injected into the host with the DNA to shield the diverse sugar modifications of their hydroxymethyl cytosine residues from the IBEG family of MDS enzymes.