Structure of the Cell Wall of Staphylococcus aureus, Strain Copenhagen. VII. Mode of Action of the Bacteriolytic Peptidase from Myxobacter and the Isolation of Intact Cell Wall Polysaccharides<sup>*</sup>

Tipper, Donald J.; Strominger, Jack L.; Ensign, Jerald C.

doi:10.1021/bi00855a035

Cited by 94 publications

(91 citation statements)

References 27 publications

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“…Fraction IIb was predominantly glycine, presumably derived from the polyglycine bridge. Similar split products have been isolated by others (17,19). The components of interest isolated from the lysostaphin digest included a hexosamine-rich fraction and a peptide moiety.…”

Section: Isolation Of Haptenic Inhibitors From An Enzymatic Digest Ofsupporting

confidence: 64%

“…Recent studies have shown that AL-proteinase preparations contain activities which hydrolyze N-acetyl muramyl-L-alanine, D-alanyl-glycine, and glycyl-glycine (17). The lysostaphin preparation has the enzyme specificities similar to AL-proteinase, with the exception that it lacks the capacity to split D-alanyl-glycine (18,19).…”

Section: Isolation Of Haptenic Inhibitors From An Enzymatic Digest Ofmentioning

confidence: 99%

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Immunochemical Studies on the Cross-Reactivity Between Streptococcal and Staphylococcal Mucopeptide

Karakawa

Braun

Lackland

et al. 1968

The Journal of Experimental Medicine

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Previous studies on the immunology of streptococcal mucopeptidO indicate that the peptide moiety isolated by enzymatic means is a dominant antigenic determinant (1). More recently, it has also been shown that the hexosamine polymer may be antigenic (2). In an extension of these observations, immunologic cross-reactions between streptococcal and staphylococcal mucopeptides were noted, but the immunochemical basis for this cross-reactivity was not defined (3).The mucopeptides of streptococci and staphylococci consist of repeating units of N-acetylglucosamine and N-acetyl muramic acid. In each case, tetrapeptides, composed of L-alanine, D-glutamic acid, lysine, and D-alanine, are linked to the hexosamine polymer through the carboxyl group of the muramic acid, and in turn the tetrapeptides of adjacent hexosamine polymers are covalently cross-linked to form a matrix (4, 5, 6). The cross-link extends from the carboxyl group of n-alanine of one tetrapeptide to the free amino group of the lysine of another tetrapeptide. The major chemical difference between the mucopeptides of streptococci and staphylococci is the composition of the peptide bridge spanning the tetrapeptides. The peptide bridge of hemolytic streptococci consists of L-alanyl-L-alanine (7), whereas that of staphylococci is a peptide of glycine (4).Other studies have now directed attention to the antigenic properties of the mucopeptides of Staphylococcus aureus. Hisatsune et al. (8) isolated from a

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Section: Isolation Of Haptenic Inhibitors From An Enzymatic Digest Ofsupporting

confidence: 64%

Section: Isolation Of Haptenic Inhibitors From An Enzymatic Digest Ofmentioning

confidence: 99%

Immunochemical Studies on the Cross-Reactivity Between Streptococcal and Staphylococcal Mucopeptide

Karakawa

Braun

Lackland

et al. 1968

The Journal of Experimental Medicine

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“…S. aureus peptidoglycan (murein) comprises glycan strands with the repeating disaccharide N-acetylmuramic acid (␤1-4)-N-acetylglucosamine (MurNac-GlcNac) units of various lengths (18,19). Short wall peptides, composed of L-Ala-D-iGln-L-Lys-D-Ala, are linked via an amide bond to the D-lactyl moiety of MurNac (20,44,70). Neighboring wall peptides are cross-linked between the ε-amino group of L-Lys in one peptide and the carboxyl group of D-Ala in another via pentaglycine cross bridges.…”

mentioning

confidence: 99%

Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope ofStaphylococcus aureus

2006

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Staphylococcus simulans bv. staphylolyticus secretes lysostaphin, a bacteriocin that cleaves pentaglycine cross bridges in the cell wall of Staphylococcus aureus. The C-terminal cell wall-targeting domain (CWT) of lysostaphin is required for selective binding of this bacteriocin to S. aureus cells; however, the molecular target for this was unknown. We used purified green fluorescent protein fused to CWT (GFP-CWT) to reveal speciesspecific association of the reporter with staphylococci. GFP-CWT bound S. aureus cells as well as purified peptidoglycan sacculi. The addition of cross-linked murein, disaccharides linked to interconnected wall peptides, blocked GFP-CWT binding to staphylococci, whereas murein monomers or lysostaphin-solubilized cell wall fragments did not. S. aureus strain Newman variants lacking the capacity for synthesizing polysaccharide capsule (capFO), poly-N-acetylglucosamine (icaAC), lipoprotein (lgt), cell wall-anchored proteins (srtA), or the glycolipid anchor of lipoteichoic acid (ypfP) bound GFP-CWT similar to wild-type staphylococci. A tagO mutant strain, defective in the synthesis of polyribitol wall teichoic acid attached to the cell wall envelope, displayed increased GFP-CWT binding. In contrast, a femAB mutation, reducing both the amount and the length of peptidoglycan cross-linking (monoglycine cross bridges), showed a dramatic reduction in GFP-CWT binding. Thus, the CWT domain of lysostaphin directs the bacteriocin to cross-linked peptidoglycan, which also serves as the substrate for its glycyl-glycine endopeptidase domain.

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“…After reduction, 0.3 ml of conc. HC1 was added to it and the mixture was heated at 100 C for 3 hr in sealed tubes [22]. The hydrolysate was dried in vacuo over NaOH pellets.…”

Section: Methodsmentioning

confidence: 99%

“…A portion (3-4 mg) of the disaccharide fraction (DFF-III) was reduced with sodium borohydride according to the method of Tipper et al [22]. The reduced disaccharide was subjected to acid hydrolysis and the resulting material was analyzed by onedimensional paper chromatography in solvents (A) and (B).…”

Section: Characterization Of the Isolated Disaccharidementioning

confidence: 99%

Autolytic Enzyme System of Clostridium botulinum

Takumi

Kawata

Hisatsune

1971

Japanese Journal of Microbiology

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The mode of action of the autolytic enzymes of Clostridium botulinum type A strain 190L was investigated using a partially purified autolysin. The autolysin completely solubilized SDS‐treated cell walls of the organism, liberating 1.2 moles of NH2‐terminal‐L‐alanine and 0.6 moles of reducing groups per mole of glutamic acid. Neither the NH2‐termini of other amino acids nor COOH‐termini of any amino acids were released. These results show that the autolysin contains an N‐acetylmuramyl‐L‐alanine amidase and a hexosaminidase. A disaccharide and peptides were isolated from the wall lysate in a chromatographically homogeneous state. The reducing end of the disaccharide was elucidated to be N‐acetylglucosamine by borohydride reduction. This fact indicates that the hexosaminidase is likely to be an endo‐β‐N‐acetylglucosaminidase. A possible structure of the cell wall peptidoglycan is proposed.

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Structure of the Cell Wall of Staphylococcus aureus, Strain Copenhagen. VII. Mode of Action of the Bacteriolytic Peptidase from Myxobacter and the Isolation of Intact Cell Wall Polysaccharides^*

Cited by 94 publications

References 27 publications

Immunochemical Studies on the Cross-Reactivity Between Streptococcal and Staphylococcal Mucopeptide

Immunochemical Studies on the Cross-Reactivity Between Streptococcal and Staphylococcal Mucopeptide

Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope ofStaphylococcus aureus

Autolytic Enzyme System of Clostridium botulinum

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Structure of the Cell Wall of Staphylococcus aureus, Strain Copenhagen. VII. Mode of Action of the Bacteriolytic Peptidase from Myxobacter and the Isolation of Intact Cell Wall Polysaccharides*

Cited by 94 publications

References 27 publications

Immunochemical Studies on the Cross-Reactivity Between Streptococcal and Staphylococcal Mucopeptide

Immunochemical Studies on the Cross-Reactivity Between Streptococcal and Staphylococcal Mucopeptide

Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope ofStaphylococcus aureus

Autolytic Enzyme System of Clostridium botulinum

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Product

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Structure of the Cell Wall of Staphylococcus aureus, Strain Copenhagen. VII. Mode of Action of the Bacteriolytic Peptidase from Myxobacter and the Isolation of Intact Cell Wall Polysaccharides^*