The tape measure protein of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has an active muramidase domain.
Tailed double-stranded DNA (dsDNA) bacteriophages frequently harbor structural proteins displaying peptidoglycan hydrolytic activities. The tape measure protein from Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has a lysozyme-like and a peptidase_M23 domain. This report shows that the lysozyme-like domain (TG1) has muramidase activity and exhibits in vitro lytic activity against live S. aureus cells, an activity that could eventually find use in the treatment of infections.
Instituto de Productos Lácteos de Asturias (IPLA-CSIC), Department of Technology and Biotechnology of Dairy Products, Asturias, Spain.
Lorena
L
Rodríguez-Rubio
Dolores
D
Gutiérrez
Beatriz
B
Martínez
Ana
A
Rodríguez
Friedrich
F
Götz
Pilar
P
García
D001433:Bacteriolysis; D009113:Muramidase / Q000235:genetics*; D017434:Protein Structure, Tertiary; D013204:Staphylococcus Phages / Q000235:genetics*; D013211:Staphylococcus aureus / Q000821:virology*; D014764:Viral Proteins / Q000235:genetics*
D014764:Viral Proteins; D009113:Muramidase