Peptide Cross-Links in Bacterial Cell Wall Peptidoglycans Studied with Specific Endopeptidases from Streptomyces albus G

Petit, Jean‐François; Muñoz, Emilio; Ghuysen, Jean‐Marie

doi:10.1021/bi00872a037

Cited by 86 publications

(69 citation statements)

References 28 publications

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“…cross-linked by L-alanyl-L-alanine to form a matrix (15). The mucopeptides of the various bacteria differ primarily in the amino acid content of the tetrapeptides and the cross-link peptides.…”

Section: Resultsmentioning

confidence: 99%

Biological Properties of Cell Wall Mucopeptide of Hemolytic Streptococci

Rotta

Bednáŕ

1969

The Journal of Experimental Medicine

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Although the mucopeptide ~ of hemolytic streptococci is not chemically similar to the endoto~n~ of Gram-negative bacteria, both substances have several biological properties in common. For example, streptococcal mucopeptide, when injected into mice, either intraperitoneaUy or intravenously, enhances the resistance to subsequent challenge with virulent Group A streptococci. Mucopeptide produces fever in the rabbit and may initiate shock and death (1). A necrotic skin lesion develops in rabbits after local injection of mucopeptide (2). In this report, the febrile response after injection of mucopeptide has been studied in greater detail, and mucopeptide has been used to prepare and provoke the local Shwartzman reaction. Special attention has been given to pathologic alterations which occur in the myocardium of rabbits after the intravenous administration of mucopeptide, a finding which was reported earlier as a preliminary observation (3). Throughout the whole procedure for the preparation of mucopeptide and carbohydrate, from the growth of the bacteria to the final lyophifization of the products, care was taken to * The prellmlna~ studies of this work were begun at the time the senior author was a visitiag investigator in the laboratory of Dr. Materials and Methods Streptococcal Strains.--Group

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Section: Resultsmentioning

confidence: 99%

Biological Properties of Cell Wall Mucopeptide of Hemolytic Streptococci

Rotta

Bednáŕ

1969

The Journal of Experimental Medicine

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“…This branched anchor peptide is linked to N-acetylmuramic acid, thereby attaching surface proteins to the glycan chains of the staphylococcal cell wall. We think that surface proteins may be linked to a precursor molecule of peptidoglycan synthesis rather than to the mature, assembled cell wall, because the staphylococcal peptidoglycan is highly cross-linked and has very few free pentaglycine amino groups (11,23,(32)(33)(34). During the biosynthesis of bacterial peptidoglycans, a membrane-bound disaccharide-precursor molecule cytoplasm (35, 36) and translocated across the membrane to serve as a substrate for transglycosylation and Table III for a complete listing of observed ions, proposed structures, and calculated masses.…”

Section: Discussionmentioning

confidence: 99%

Anchor Structure of Staphylococcal Surface Proteins

Ton‐That¹,

Faull

Schneewind³

1997

Journal of Biological Chemistry

123

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Surface proteins of Staphylococcus aureus are anchored to the cell wall by a mechanism requiring a COOH-terminal sorting signal. Previous work demonstrated that the sorting signal is cleaved at the conserved LPXTG motif and that the carboxyl of threonine (T) is linked to the staphylococcal cell wall. By employing different cell wall lytic enzymes, surface proteins were released from the staphylococcal peptidoglycan and their COOH-terminal anchor structure was revealed by a combination of mass spectrometry and chemical analysis. The results demonstrate that surface proteins are linked to a branched peptide (NH 2 -Ala-␥-Gln-Lys-(NH 2 -Gly 5 )-Ala-COOH) by an amide bond between the carboxyl of threonine and the amino of the pentaglycine cross-bridge that is attached to the ⑀-amino of lysyl. This branched anchor peptide is amidelinked to the carboxyl of N-acetylmuramic acid, thereby tethering the COOH-terminal end of surface proteins to the staphylococcal peptidoglycan.

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“…The carboxylpeptidase and ␤-lactamase members of the PBP family resolve the acyl-enzyme by the nucleophilic attack of water, followed by the release of cleaved substrate (20). PBP transpeptidases bind cell-wall crossbridges, NH 2 -Gly 5 in S. aureus (21,22), and the nucleophilic attack of their amino group at the acyl-enzyme ester regenerates the active site, thereby linking the carboxyl group of D-Ala within wall peptides to the amino group of the crossbridge (10,23). Penicillin and other ␤-lactam antibiotics act as a molecular mimic of D-Ala-D-Ala (24).…”

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confidence: 99%

Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus

Ilangovan

Ton‐That

Iwahara

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

285

366

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Surface proteins of Gram-positive bacteria play important roles during the pathogenesis of human infections and require sortase for anchoring to the cell-wall envelope. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine (T) and the amino group of cell-wall crossbridges. The NMR structure of sortase reveals a unique ␤-barrel structure, in which the active-site sulfhydryl of cysteine-184 is poised for ionization by histidine-120, presumably enabling the resultant thiolate to attack the LPXTG peptide. Calcium binding near the active site stimulates catalysis, possibly by altering the conformation of a surface loop that recognizes newly translocated polypeptides. The structure suggests a mechanistic relationship to the papain͞cathepsin proteases and should facilitate the design of new antiinfective agents.

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Peptide Cross-Links in Bacterial Cell Wall Peptidoglycans Studied with Specific Endopeptidases from Streptomyces albus G

Cited by 86 publications

References 28 publications

Biological Properties of Cell Wall Mucopeptide of Hemolytic Streptococci

Biological Properties of Cell Wall Mucopeptide of Hemolytic Streptococci

Anchor Structure of Staphylococcal Surface Proteins

Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus

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