J Bacteriol 2004,186(14):4543–4555.PubMedCrossRef 44. Clewell DB, Tomich PK, Gawron-Burke MC, Franke AE, Yagi Y, An FY: Mapping of Streptococcus faecalis plasmids pAD1 and pAD2 and studies relating to transposition of Tn917. J Bacteriol 1982,152(3):1220–1230.PubMed 45. Jacob AE, Hobbs SJ: Conjugal Transfer of Plasmid-Borne Multiple Antibiotic Resistance in Streptococcus

faecalis var. zymogenes. J Bacteriol 1974,117(2):360–372.PubMed 46. Maguin E, Prevost H, Ehrlich S, Gruss A: Efficient click here insertional mutagenesis in lactococci and other gram-positive bacteria. J Bacteriol 1996,178(3):931–935.PubMed Authors’ contributions CAS carried out the molecular genetic studies, participated in the β-galactosidase activities and protein purification. VSB carried out the molecular genetic studies, participated in the band shift assay and helped to draft the manuscript. SP participated in the purification of the proteins and Band shift assay. JD participated in the coordination and helped to draft the https://www.selleckchem.com/autophagy.html manuscript and CM participated in experiment design, coordination and helped to draft the manuscript. All authors read and approved the final manuscript.”
“Background Peptidoglycan-degrading enzymes or murein hydrolases have the ability to digest bacterial cell walls. Such enzymes from bacteriophages represent a unique class of antibacterial

agents because of their ability to cleave bacterial peptidoglycan in a species-specific or genus-specific manner. Thus, they provide a means to selectively target pathogens [1–3]. At the end of the bacteriophage infection process, progeny are released from the host

cell by lysis, which is mediated by two phage-encoded gene products, endolysins selleck and holins [4]. Holins are transmembrane proteins that create lesions in the cytoplasmic membrane through which peptidoglycan-degrading enzymes (endolysins) gain access to the peptidoglycan layer [4, 5]. Bacteriophages encode another peptidoglycan-degrading enzyme involved in the initial stages of infection that facilitates phage DNA injection into the host cell. These proteins, which are distinct from endolysins, aid in the rapid lysis of host cells by a phenomenon referred to as “”lysis from without”" upon infection with high multiplicities of phage [6]. Enzymes involved in DNA injection are an integral component of the virion structure of many phages [7–9]. Examples of these phage structure-associated peptidoglycan-degrading enzymes include GP16 (phage T7), GP5 (phage T4), GP4 (Salmonella phage P22), GP3 (Bacillus phage Φ29), ORF50 (Lactococcus lactis bacteriophage Tuc2009), protein 17 (Staphylococcus aureus phage P68), and GP61 (S. aureus phage PhiMR11) [8–15]. S. aureus is an important human pathogen responsible for a wide variety of diseases and is a common cause of nosocomial and community-acquired infections. The emergence of antibiotic-resistant S.