A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization.

Abstract

The Tn551 insertion site of the autolysisdeficient Staphylococcus aureus mutant RUSAL2 was cloned and used to identify the autolysis gene ati in the parent strain,RN450. The open reading frame for atl was 3768 bp in length, encoding a deduced protein of 1256 amino acids and molecular size of 137,381 Da. The atl gene product is a bifunctional protein that has an amidase domain and an endo-13-Nacetylglucosaminidase domain which must undergo proteolytic processing to generate the two extraceliular lytic enzymes found in the culture broth of S. aureus.

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

“…Its C-terminal cell wall-anchoring (CWA) domain contains eight glycine-tryptophan (GW) modules, through which Ami associates to the bacterial surface, putatively by interaction with lipoteichoic acids (LTAs). [35][36][37] The CWA domain of Ami has been shown to mediate bacterial adhesion to human epithelial cells. 38,39 In addition, an ami mutant is attenuated in the liver of intravenously infected mice, suggesting a role in L. monocytogenes virulence.…”

Dual Targeting of Cell Wall Precursors by Teixobactin Leads to Cell Lysis

“…It was also shown that mutation of tarO results in delocalization of amidase (21). Atl possesses three repeat sequences, each about 150 amino acids long (R 1-3 ), which bind to peptidoglycan (19,35). We examined the localization of Atl using a fluorescently labeled R 1-3 repeat domain (Cy3-R 1-3 ) (21).…”

Tracking adhesion factors in Staphylococcus caprae strains responsible for human bone infections following implantation of orthopaedic material

“…Three similar genes in S. aweits, S. epidermidis and S. saprophyticus en c od i n g ce 1 1 -w a 11 -ass o c i at ed auto 1 y s i n s have been sequenced: at1 (Oshida et al, 1995(Oshida et al, , 1998, at1E and aas (Hell et al, 1998), respectively. T h e three proteins encoded by these genes have two enzymic domains (amidase and glucosaminidase) in common.…”

“…4, lane 5) was sequenced. T h e amino acid sequence obtained was AEETQDQTKN, which is 80% identical to the Nterminal part of S. aurezts At1 ( A E T T Q D Q T T N ) (Oshida et al, 1995), 7 0 % identical to the N-terminal part of Staphvlococczts saprophvticus Aas (ASNT-Q D Q T P N ) (Hell et al, 1998) and 50% identical to the same part of S. epidermidis AtlE (AEQPQNQSHN) (Heilmann et a/., 1997).…”