title: Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site.
abstract: Staphylococcus aureus is a notorious pathogen highly successful at developing resistance to virtually all antibiotics to which it is exposed. Staphylococcal phage 2638A endolysin is a peptidoglycan hydrolase that is lytic for S. aureus when exposed externally, making it a new candidate antimicrobial. It shares a common protein organization with more than 40 other reported staphylococcal peptidoglycan hydrolases. There is an N-terminal M23 peptidase domain, a mid-protein amidase 2 domain (N-acetylmuramoyl-L-alanine amidase), and a C-terminal SH3b cell wall-binding domain. It is the first phage endolysin reported with a secondary translational start site in the inter-lytic-domain region between the peptidase and amidase domains. Deletion analysis indicates that the amidase domain confers most of the lytic activity and requires the full SH3b domain for maximal activity. Although it is common for one domain to demonstrate a dominant activity over the other, the 2638A endolysin is the first in this class of proteins to have a high-activity amidase domain (dominant over the N-terminal peptidase domain). The high activity amidase domain is an important finding in the quest for high-activity staphylolytic domains targeting novel peptidoglycan bonds.
authors: State Research Center for Applied Microbiology and Biotechnology (SRCAMB), Obolensk, Moscow Region 142279, Russia.
authors: Igor
authors: I
authors: Abaev
authors: Juli
authors: J
authors: Foster-Frey
authors: Olga
authors: O
authors: Korobova
authors: Nina
authors: N
authors: Shishkova
authors: Natalia
authors: N
authors: Kiseleva
authors: Pavel
authors: P
authors: Kopylov
authors: Sergey
authors: S
authors: Pryamchuk
authors: Mathias
authors: M
authors: Schmelcher
authors: Stephen C
authors: SC
authors: Becker
authors: David M
authors: DM
authors: Donovan
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D018387:Codon, Initiator; D004252:DNA Mutational Analysis; D010450:Endopeptidases / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010442:Peptide Chain Initiation, Translational; D017434:Protein Structure, Tertiary; D017384:Sequence Deletion; D013204:Staphylococcus Phages / Q000201:enzymology* / Q000235:genetics; D013211:Staphylococcus aureus / Q000821:virology*
chemical_list: D018387:Codon, Initiator; D010450:Endopeptidases; C001143:endolysin