scholarly journals First insights of peptidoglycan amidation in Gram-positive bacteria - the high-resolution crystal structure of Staphylococcus aureus glutamine amidotransferase GatD

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Francisco Leisico ◽  
Diana V. Vieira ◽  
Teresa A. Figueiredo ◽  
Micael Silva ◽  
Eurico J. Cabrita ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
High Resolution ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Glutamine Amidotransferase

scholarly journals A structural study of TatD from Staphylococcus aureus elucidates a putative DNA-binding mode of a Mg2+-dependent nuclease

IUCrJ ◽  
2020 ◽  
Vol 7 (3) ◽  
pp. 509-521
Author(s):  
Kyu-Yeon Lee ◽  
Seung-Ho Cheon ◽  
Dong-Gyun Kim ◽  
Sang Jae Lee ◽  
Bong-Jin Lee
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Dna Binding ◽  
Catalytic Mechanism ◽  
Nuclease Activity ◽  
Binding Mode ◽  
Functional Study ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Key Residues

TatD has been thoroughly investigated as a DNA-repair enzyme and an apoptotic nuclease, and still-unknown TatD-related DNases are considered to play crucial cellular roles. However, studies of TatD from Gram-positive bacteria have been hindered by an absence of atomic detail and the resulting inability to determine function from structure. In this study, an X-ray crystal structure of SAV0491, which is the TatD enzyme from the Gram-positive bacterium Staphylococcus aureus (SaTatD), is reported at a high resolution of 1.85 Å with a detailed atomic description. Although SaTatD has the common TIM-barrel fold shared by most TatD-related homologs, and PDB entry 2gzx shares 100% sequence identity with SAV0491, the crystal structure of SaTatD revealed a unique binding mode of two phosphates interacting with two Ni2+ ions. Through a functional study, it was verified that SaTatD has Mg2+-dependent nuclease activity as a DNase and an RNase. In addition, structural comparison with TatD homologs and the identification of key residues contributing to the binding mode of Ni2+ ions and phosphates allowed mutational studies to be performed that revealed the catalytic mechanism of SaTatD. Among the key residues composing the active site, the acidic residues Glu92 and Glu202 had a critical impact on catalysis by SaTatD. Furthermore, based on the binding mode of the two phosphates and structural insights, a putative DNA-binding mode of SaTatD was proposed using in silico docking. Overall, these findings may serve as a good basis for understanding the relationship between the structure and function of TatD proteins from Gram-positive bacteria and may provide critical insights into the DNA-binding mode of SaTatD.

scholarly journals In Vitro and In Vivo Activities of DA-7867, a New Oxazolidinone, against Aerobic Gram-Positive Bacteria

2005 ◽  
Vol 49 (6) ◽  
pp. 2498-2500 ◽  
Author(s):  
Eun Jeong Yoon ◽  
Yeong Woo Jo ◽  
Sung Hak Choi ◽  
Tae Ho Lee ◽  
Jae Keol Rhee ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Streptococcus Pneumoniae ◽  
Gram Positive ◽  
Methicillin Resistant ◽  
Gram Positive Bacteria ◽  
Vancomycin Resistant Enterococci ◽  
Infection Models ◽  
Vancomycin Resistant

ABSTRACT In vitro and in vivo activities of DA-7867 were assessed against methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and penicillin-resistant Streptococcus pneumoniae. All isolates were inhibited by DA-7867 at ≤0.78 μg/ml, a four-times-lower concentration than that of inhibition by linezolid. For murine infection models, DA-7867 also exhibited greater efficacy than linezolid against all isolates tested.

scholarly journals Antimicrobial Activity of Gardenia jasminoides Callus and Crude Leaf Extracts for some Organic Solvents against some Pathogenic Bacteria and Yeasts

2014 ◽  
Vol 8 (3) ◽  
pp. 40-45
Author(s):  
Zina Hashem Shehab ◽  
Huda Suhail Abid ◽  
Sumaya Fadhil Hamad ◽  
Sara Haitham
Keyword(s):  
Staphylococcus Aureus ◽  
Candida Albicans ◽  
Pathogenic Bacteria ◽  
Saccharomyces Boulardii ◽  
Gram Negative Bacteria ◽  
Proteus Vulgaris ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria ◽  
Gardenia Jasminoides

The study was conducted to evaluate the inhibitory activity of methanol extract of Gardenia jasminoides leaves compared with leaf crude extracts for some organic solvents namely Methanol, Ethanol, Petroleum ether, Asetone and Chloroform on growth of some pathogenic bacteria and yeast, which included four gram positive isolates Staphylococcus aureus, Enterococcus faecalis, Streptococcus pyogenes and Bacillus cereus and gram negative isolates Escherichia coli, Salmonella typhi, Proteus vulgaris and Pseudomonas aeruginosa and some yeasts Candida albicans and Saccharomyces boulardii, by using well diffusion method. The inhibitory activity of extracts in the tested bacterial strains and yeasts was varied according to the type of extracting solvents and are tested microorganisms. The methanol callus extract which grown on Murashige and Skoog (MS) media by using (Naphthalen acitic acid) NAA and (Benzyle adenine) BA as growth regulator highly effective as compared to the other extracts as for inhibition of three gram positive bacteria and three gram negative bacteria,which include Staphylococcus aureus and, Proteus vulgaris, followed by acetone and ethanolic extracts which include two gram positive bacteria and two gram negative bacteria. All extracts had highly effect in growth of Candida albicans while all crude extracts didn’t show any sensitivity against Saccharomyces boulardii, and when we’d done (High Performance Liquid Chromatography) HPLC test for detection of some active compound we found Quinic acid, Iridiods glycosides and Crocin which its rate in fresh callus was higher than fresh leaves.

scholarly journals Activities of Oxadiazole Antibacterials against Staphylococcus aureus and Other Gram-Positive Bacteria

2018 ◽  
Vol 62 (8) ◽  
Author(s):  
Sara Ceballos ◽  
Choon Kim ◽  
Derong Ding ◽  
Shahriar Mobashery ◽  
Mayland Chang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Gram Positive ◽  
Methicillin Resistant ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Vancomycin Resistant Enterococci ◽  
Vancomycin Resistant ◽  
Mrsa Strains

ABSTRACT The activities of four oxadiazoles were investigated with 210 methicillin-resistant Staphylococcus aureus (MRSA) strains. MIC50 and MIC90 values of 1 to 2 and 4 μg/ml, respectively, were observed. We also evaluated the activity of oxadiazole ND-421 against other staphylococci and enterococci and in the presence of oxacillin for selected MRSA strains. The MIC for ND-421 is lowered severalfold in combination with oxacillin, as they synergize. The MIC90 of ND-421 against vancomycin-resistant enterococci is ≤1 μg/ml.

Covalent Sortase A Inhibitor ML346 Prevents Staphylococcus aureus Infection of Galleria mellonella

2021 ◽  
Author(s):  
Xiang-Na Guan ◽  
Tao Zhang ◽  
Teng Yang ◽  
Ze Dong ◽  
Song Yang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Galleria Mellonella ◽  
Surface Proteins ◽  
Sortase A ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Aureus Infection ◽  
Cell Wall Peptidoglycan

The housekeeping sortase A (SrtA), a membrane-associated cysteine transpeptidase, is responsible for anchoring surface proteins to the cell wall peptidoglycan in Gram-positive bacteria. This process is essential for the regulation...

scholarly journals Chemical Composition and Antibacterial Activity of the Essential Oil of Espeletia nana

2012 ◽  
Vol 7 (5) ◽  
pp. 1934578X1200700 ◽  
Author(s):  
Alexis Peña ◽  
Luis Rojas ◽  
Rosa Aparicio ◽  
Libia Alarcón ◽  
José Gregorio Baptista ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Chemical Composition ◽  
Essential Oil ◽  
Diffusion Method ◽  
Gram Negative Bacteria ◽  
Gram Positive ◽  
Disk Diffusion Method ◽  
Gram Negative ◽  
Gram Positive Bacteria

The essential oil of the leaves of Espeletia nana Cuatrec, obtained by hydrodistillation, was analyzed by GC-MS, which allowed the identification of 24 components, which made up 99.9% of the oil. The most abundant compounds were α-pinene (38.1%), β-pinene (17.2%), myrcene (15.0%), spathulenol (4.2%), bicyclogermacrene (4.0%), α-zingiberene (4.0%), and γhimachalene (3.7%). Antibacterial activity was tested against Gram-positive and Gram-negative bacteria using the agar disk diffusion method. Activity was observed only against Gram-positive bacteria. MIC values were determined for Staphylococcus aureus ATCC 25923(200 μg/mL) and Enterococcus faecalis ATCC 29212 (600 μg/mL).

scholarly journals A Comparative Genome Analysis Identifies Distinct Sorting Pathways in Gram-Positive Bacteria

2004 ◽  
Vol 72 (5) ◽  
pp. 2710-2722 ◽  
Author(s):  
David Comfort ◽  
Robert T. Clubb
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Surface Proteins ◽  
Sequence Motifs ◽  
Comparative Genome Analysis ◽  
Gram Positive ◽  
Microbial Genomes ◽  
Searchable Database ◽  
Gram Positive Bacteria ◽  
Related Proteins

ABSTRACT Surface proteins in gram-positive bacteria are frequently required for virulence, and many are attached to the cell wall by sortase enzymes. Bacteria frequently encode more than one sortase enzyme and an even larger number of potential sortase substrates that possess an LPXTG-type cell wall sorting signal. In order to elucidate the sorting pathways present in gram-positive bacteria, we performed a comparative analysis of 72 sequenced microbial genomes. We show that sortase enzymes can be partitioned into five distinct subfamilies based upon their primary sequences and that most of their substrates can be predicted by making a few conservative assumptions. Most bacteria encode sortases from two or more subfamilies, which are predicted to function nonredundantly in sorting proteins to the cell surface. Only ∼20% of sortase-related proteins are most closely related to the well-characterized Staphylococcus aureus SrtA protein, but nonetheless, these proteins are responsible for anchoring the majority of surface proteins in gram-positive bacteria. In contrast, most sortase-like proteins are predicted to play a more specialized role, with each anchoring far fewer proteins that contain unusual sequence motifs. The functional sortase-substrate linkage predictions are available online (http://www.doe-mbi.ucla.edu/Services/Sortase/ ) in a searchable database.

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