Submitted to: Evergreen International Phage Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 6/10/2007
Publication Date: 8/15/2007
Citation: Donovan, D.M., Stodola, A.J., Annacker, D. 2007. A summary of staphylococcal C-terminal SH3b_5 cell wall binding domains.. Evergreen International Phage Meeting.
Technical Abstract: Staphylococcal peptidoglycan hydrolases are a potential new source of antimicrobials. A large subset of these proteins contain a C-terminal SH3b_5 cell wall binding domain that has been shown for some to be essential for accurate cell wall recognition and subsequent staphylolytic activity, properties that could enhance the antimicrobial qualities of the protein. Fifty proteins of staphylococcal (or phage) origin, harboring these C-terminal sequences have been aligned and homologues identified. Five highly repetitive groups of proteins with >90% identity have been defined. Representative C-termini from each of these five groups and another six staphylococcal proteins, for which conserved homologues have not yet been identified, are aligned and sequence conservation presented. A hypothesis and premise behind this work was that there might be specie-specific conservation of cell wall binding regions that could be used to target a variety of antimicrobials to specific pathogens. C-terminal domain alignment identifies a staphylococcal binding region consensus sequence. There are two distinct sub-groups with over-lapping but differentially conserved residues. Unexpectedly, the subgroup with the higher degree of conservation is comprised of proteins originating from a variety of staphylococcal species (or their phage), rather than the group reportedly from S. aureus alone. Three new putative intron containing phage endolysin genes have also been identified for the phages G1, X2 and 85. The phage X2 and phage 85 endolysin genes are the only ones with introns within this group of 15 nearly identical genes.