New targets for antibiotic development: biogenesis of surface adherence structures

Jones, C. Hal; Hruby, Dennis E.

doi:10.1016/s1359-6446(98)01261-6

Cited by 9 publications

(8 citation statements)

References 66 publications

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Section: Sortasementioning

confidence: 99%

“…[100][101][102][103][104][105][106] Cell wall sorting is the covalent attachment of surface proteins to the peptidoglycan via a C-terminal sorting signal that contains a consensus LeuProXThrGly (LPXTG-X may be any of the 20 natural amino acids) sequence. [100][101][102][103][104][105][106][107] Sortase participates in the pathways involved in secretion and anchoring of cell wall proteins, by a mechanism conserved in almost the entire class of the gram-positive bacteria. Sortase catalyzes the scission of the Thr # Gly bond of the above-mentioned motif, liberating the carboxyl moiety of the threonine, which subsequently forms an amide bond with the amino groups of some amino acid residues present in the bacterial cell wall peptidoglycan, which in turn are crosslinked to the E-amino group of lysine residues (for S. aureus it is the amino moiety of a pentaglycine motif that cross-bridge with the COOH moiety of the above-mentioned Thr residue; in S. pyogenes this motif is constituted by two alanines, whereas Listeria monocytogenes has a meso-diaminopimelic acid moiety in place of the lysine residue of the peptidoglycan, and no amino acid in the bridge).…”

Section: Sortasementioning

confidence: 99%

“…Sortase catalyzes the scission of the Thr # Gly bond of the above-mentioned motif, liberating the carboxyl moiety of the threonine, which subsequently forms an amide bond with the amino groups of some amino acid residues present in the bacterial cell wall peptidoglycan, which in turn are crosslinked to the E-amino group of lysine residues (for S. aureus it is the amino moiety of a pentaglycine motif that cross-bridge with the COOH moiety of the above-mentioned Thr residue; in S. pyogenes this motif is constituted by two alanines, whereas Listeria monocytogenes has a meso-diaminopimelic acid moiety in place of the lysine residue of the peptidoglycan, and no amino acid in the bridge). [100][101][102][103][104][105][106][107] Sortase is a 206-amino acid protein with a potential amino-terminal signal peptide that may act as membrane anchor. The conserved Cys 184 is considered critical for catalysis, since the enzyme is sensitive to agents that modify SH groups.…”

Section: Sortasementioning

confidence: 99%

“…105,106 These data clearly showed that cell wall anchoring of surface proteins is a critical parameter for the development of staphylococcal infection, and that sortase is a very promising target for the development of novel types of antibiotics, effective against gram-positive bacteria. [100][101][102][103][104][105][106][107] For the moment, few inhibitors of this enzyme have been reported, maybe also due to the fact that the target has only recently been purified and demonstrated as critically important for the life cycle of gram-positive bacteria. Thus, Schneewind's group 103 showed that sulfhydryl reducing agents (dithiothreitol, mercaptoethanol, etc.…”

Section: Sortasementioning

confidence: 99%

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Bacterial protease inhibitors

Supuran

Scozzafava

Clare

2002

Medicinal Research Reviews

149

120

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Serine-, cysteine-, and metalloproteases are widely spread in many pathogenic bacteria, where they play critical functions related to colonization and evasion of host immune defenses, acquisition of nutrients for growth and proliferation, facilitation of dissemination, or tissue damage during infection. Since all the antibiotics used clinically at the moment share a common mechanism of action, acting as inhibitors of the bacterial cell wall biosynthesis or affecting protein synthesis on ribosomes, resistance to these pharmacological agents represents a serious medical problem, which might be resolved by using new generation of antibiotics, possessing a different mechanism of action. Bacterial protease inhibitors constitute an interesting such possibility, due to the fact that many specific as well as ubiquitous proteases have recently been characterized in some detail in both gram-positive as well as gram-negative pathogens. Few potent, specific inhibitors for such bacterial proteases have been reported at this moment except for some signal peptidase, clostripain, Clostridium histolyticum collagenase, botulinum neurotoxin, and tetanus neurotoxin inhibitors. No inhibitors of the critically important and ubiquitous AAA proteases, degP or sortase have been reported, although such compounds would presumably constitute a new class of highly effective antibiotics. This review presents the state of the art in the design of such enzyme inhibitors with potential therapeutic applications, as well as recent advances in the use of some of these proteases in therapy.

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Section: Sortasementioning

confidence: 99%

Section: Sortasementioning

confidence: 99%

Section: Sortasementioning

confidence: 99%

Section: Sortasementioning

confidence: 99%

See 2 more Smart Citations

Bacterial protease inhibitors

Supuran

Scozzafava

Clare

2002

Medicinal Research Reviews

149

120

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“…Before the age of penicillin and antibiotic discovery, medicinal plants were frequently used to treat microbial infections. In view of the worldwide recurrence of multidrug-resistant bacterial strains 2 , it becomes an urgency to search for next-generation antimicrobial compounds. Since plants produce diverse polyphenolic compounds as parts of their self-defence mechanism against microbial infection, medicinal plants represent a promising reservoir in the search for novel antimicrobial compounds 3 .…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the antibacterial activities of selected medicinal plants and determination of their phenolic constituents

Wong

Yong²,

Ong³

et al. 2013

ScienceAsia

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The purpose of this investigation was to determine the antibacterial activities of five medicinal plants, against both Gram-positive and Gram-negative bacteria. The levels of phenolic constituents in these medicinal plants were also quantified and compared. Minimum inhibitory concentrations (MIC) were determined colorimetrically using 96-well sterile microtitre plates and treatment with p-iodonitrotetrazolium chloride (violet). Concentrations of selected phenolic constituents were determined using HPLC methods, by comparison to standard plots prepared using catechin, caffeic acid, gallic acid, and quercetin standards. MIC tests indicated that Callicarpa formosana and Melastoma candidum possessed the strongest bacterial inhibitory activities, with MIC values ranging between 12.5 and 37.5 mg/ml and 0.80-8.3 mg/ml, respectively. M. candidum also demonstrated inhibitory activities against Gram-negative bacteria, with MIC value of 8.3 mg/ml. Quercetin was detected in all medicinal plants tested, with concentrations ranging between 0.25 and 0.47 µg per mg of dried sample. Caffeic acid, catechin and gallic acid were detected in only some of the medicinal plants. Our results suggested that C. formosana and M. candidum could potentially be used for the isolation of potent antibacterial compounds.

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