Inhibition of the Bacterial Surface Protein Anchoring Transpeptidase Sortase by Isoquinoline Alkaloids

Kim, Soo-Hwan; Shin, Dong Chun; Oh, Min-A; Chung, Soon‐Chun; Lee, Jang-Suk; Oh, Ki‐Bong

doi:10.1271/bbb.68.421

Cited by 87 publications

(39 citation statements)

References 18 publications

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“…As sitosterol alone does not inhibit sortase, it was concluded that the inhibitory effect must reside within the glucopyranoside moiety of the molecule. A similar experimental approach for extracts of Coptis chinensis identified the isoquinoline alkaloid berberine chloride as a sortase inhibitor (94). Both compounds exhibit a lower MIC than p-hydroxymercuribenzoic acid (see above) and were able to inhibit binding of S. aureus to fibronectin-coated surfaces (143), an interaction mediated by the sortase A substrates fibronectin binding proteins A and B (FnbpA and FnbpB) (see above).…”

Section: Sortase a Inhibitorsmentioning

confidence: 96%

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Marraffini

DeDent²,

Schneewind³

2006

Microbiol Mol Biol Rev

608

600

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SUMMARY The cell wall envelopes of gram-positive bacteria represent a surface organelle that not only functions as a cytoskeletal element but also promotes interactions between bacteria and their environment. Cell wall peptidoglycan is covalently and noncovalently decorated with teichoic acids, polysaccharides, and proteins. The sum of these molecular decorations provides bacterial envelopes with species- and strain-specific properties that are ultimately responsible for bacterial virulence, interactions with host immune systems, and the development of disease symptoms or successful outcomes of infections. Surface proteins typically carry two topogenic sequences, i.e., N-terminal signal peptides and C-terminal sorting signals. Sortases catalyze a transpeptidation reaction by first cleaving a surface protein substrate at the cell wall sorting signal. The resulting acyl enzyme intermediates between sortases and their substrates are then resolved by the nucleophilic attack of amino groups, typically provided by the cell wall cross bridges of peptidoglycan precursors. The surface protein linked to peptidoglycan is then incorporated into the envelope and displayed on the microbial surface. This review focuses on the mechanisms of surface protein anchoring to the cell wall envelope by sortases and the role that these enzymes play in bacterial physiology and pathogenesis.

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Section: Sortase a Inhibitorsmentioning

confidence: 96%

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Marraffini

DeDent²,

Schneewind³

2006

Microbiol Mol Biol Rev

608

600

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“…The anti-biofilm action of curcumin was attributed to a reduction in the cell wall-anchored adhesin PAc that mediates attachment of S. mutans to the tooth surface [57]. The isoquinoline alkaloid berberine chloride extracted from the Coptis chinensis rhizome, was reported as a potent inhibitor of sortase (IC 50 ¼ 8.7 mg/ml) with a moderate antibacterial activity against Gram-positive bacteria (MIC range of 50e400 mg/ml) [58]. Recently, Oh et al described a series of flavonoids isolated from the roots of Sophora flavescens that acted as S. aureus SrtA inhibitors [59].…”

Section: Natural Productsmentioning

confidence: 99%

Sortase A: An ideal target for anti-virulence drug development

Cascioferro¹,

Totsika²,

Schillaci³

2014

Microbial Pathogenesis

165

142

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“…33,34 The mechanism of antimicrobial activity of berberine is attributed to its ability to intercalate with DNA and suppress DNA and protein synthesis in microorganism cells. 34,35 Synthesizing our data and literature reports, 33,34 we propose that berberine may be used to treat PPI induced by Staphylococcus (S. epidermidis and S. aureus) and other bacteria. Berberine may, at least, inhibit biofilm formation by reducing bacterial adhesion and proliferation.…”

Section: Discussionmentioning

confidence: 60%

Berberine inhibits Staphylococcus Epidermidis adhesion and biofilm formation on the surface of titanium alloy

Wang

Qiu

Xiao

et al. 2009

Journal Orthopaedic Research

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Biofilm formed by Staphylococcus epidermidis (S. epidermidis) is a common cause of periprosthetic infection. Recently, we have discovered that berberine is bacteriostatic for S. epidermidis. The purpose of the present study was to examine the effect of berberine on S. epidermidis adhesion and biofilm formation on the surface of titanium alloy, which is a popular material for orthopedic joint prostheses. Three strains of S. epidermidis (ATCC 35984, ATCC 12228, and SE 243) were used for in vitro experiment. Direct colony counting showed that berberine significantly inhibited S. epidermidis adhesion on the titanium alloy disk in 2 h at the concentration of 45 mg/mL. When examined with crystal violet staining, confocal laser scanning microscopy, and scanning electron microscopy, we found that higher concentrations (>30 mg/mL) of berberine effectively prevented the formation of S. epidermidis biofilm on the surface of the titanium disk in 24 h. These findings suggest that berberine is a potential agent for the treatment of periprosthetic infection. ß

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Inhibition of the Bacterial Surface Protein Anchoring Transpeptidase Sortase by Isoquinoline Alkaloids

Cited by 87 publications

References 18 publications

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Sortase A: An ideal target for anti-virulence drug development

Berberine inhibits Staphylococcus Epidermidis adhesion and biofilm formation on the surface of titanium alloy

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