Optimization of a lysis method to isolate periplasmic proteins from Gram‐negative bacteria for clinical mass spectrometry

2021 ◽  
pp. 2100044
Author(s):  
Dong Huey Cheon ◽  
Saeyoung Lee ◽  
Won Suk Yang ◽  
Seohyun Hwang ◽  
Heejung Jang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Periplasmic Proteins

scholarly journals Direct detection of lipid A on intact Gram-negative bacteria by MALDI-TOF mass spectrometry

2016 ◽  
Vol 120 ◽  
pp. 68-71 ◽  
Author(s):  
Gerald Larrouy-Maumus ◽  
Abigail Clements ◽  
Alain Filloux ◽  
Ronan R. McCarthy ◽  
Serge Mostowy
Keyword(s):  
Mass Spectrometry ◽  
Lipid A ◽  
Direct Detection ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof

scholarly journals Fusaricidins, Polymyxins and Volatiles Produced by Paenibacillus polymyxa Strains DSM 32871 and M1

2021 ◽  
Author(s):  
Pascal Mülner ◽  
Elisa Schwarz ◽  
Kristin Dietel ◽  
Stefanie Herfort ◽  
Jennifer Jähne ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Characteristic Feature ◽  
Fungal Pathogens ◽  
Paenibacillus Polymyxa ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Antifungal Activities ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof ◽  
Volatile Organic

Paenibacilli are efficient producers of potent agents against bacterial and fungal pathogens, which are of great interest both for therapeutic applications in medicine as well as in agrobiotechnol-ogy. Lipopeptides produced by such organisms play a major role in their inactivation potential. In this work we investigated two lipopeptide complexes, the fusaricidins and the polymyxins, produced by Paenibacillus polymyxa strains DSM 32871 and M1 by MALDI-TOF mass spectrometry. The fusaricidins show potent antifungal activities and are distinguished by an unusual variabil-ity. For strain DSM 32871 we identified numerous yet unknown variants mass spectrometrically. DSM 32871 produces polymyxins of type E (colistins), while M1 forms polymyxins P. For both strains novel, but not yet completely characterized polymyxin species were detected, which pos-sibly are glycosylated. These compounds may be of interest therapeutically, because polymyxins attain increasing attention as last-resort antibiotics against multiresistant pathogenic Gram-negative bacteria. In addition, the volatilomes of DSM 32781 and M1 were investigated with a GC-MS approach using different cultivation media. Production of volatile organic com-pounds (VOCs) was strain and medium dependent. In particular, strain M1 manifested as an effi-cient VOC-producer that exhibited formation of 25 volatiles in total. A characteristic feature of Paenibacilli is the formation of volatile pyrazine derivatives.

scholarly journals Discrimination of Some Gram-negative Bacteria by Direct Probe Mass Spectrometry

Microbiology ◽  
1982 ◽  
Vol 128 (4) ◽  
pp. 721-730
Author(s):  
C. S. Gutteridge ◽  
D. J. Puckey
Keyword(s):  
Mass Spectrometry ◽  
Gram Negative Bacteria ◽  
Gram Negative

Glycosides from Cephalaria Species

2010 ◽  
Vol 65 (11) ◽  
pp. 1384-1392 ◽  
Author(s):  
Erkan Halay ◽  
Süheyla Kırmızıgül
Keyword(s):  
Mass Spectrometry ◽  
Oleanolic Acid ◽  
2D Nmr ◽  
Spectroscopic Methods ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Nmr Techniques ◽  
Basic Hydrolysis ◽  
Hydrolysis Of ◽  
Chemical Evidence

Three novel triterpene glycosides (1 - 3), namely lycicoside I, II and cilicicoside I, were isolated from two different Cephalaria (Dipsacaceae) species along with one known oleanane- and one iridoit- type of glycoside. The structures of these compounds were established as 3-O-[β -D-glucopyranosyl( 1→3)-α-L-rhamnopyranosyl(1→4)-β -D-xylopyranosyl(1→4)-β -D-xylopyranosyl]-28-O-[β -Dglucopyranosyl( 1→6)-β -D-glucopyranosyl]-oleanolic acid (1), 3-O-[β -D-xylopyranosyl(1→3)-α- L-rhamnopyranosyl(1→4)-β -D-xylopyranosyl]-28-O-[β -D-glucopyranosyl]-oleanolic acid (2) from Cephalaria lycica Matthew and 3-O-{β -D-glucopyranosyl(1→4)-β -D-xylopyranosyl(1→3)-α-Lrhamnopyranosyl( 1→2)-[β -D-glucopyranosyl(1→3)]-α -L-rhamnopyranosyl}-28-O-[β -D-glucopyranosyl( 1→6)-β -D-glucopyranosyl]-hederagenin (3) from Cephalaria cilicica Boiss. & Kotschy, on the basis of spectroscopic methods (1D and 2D NMR techniques, mass spectrometry) and chemical evidence. In addition, three new prosapogenins, 1B - 3B, were obtained from the basic hydrolysis of 1 - 3. The antimicrobial activity of 1 - 3 was tested against some Gram-positive and Gram-negative bacteria strains.

Use of Glycol Ethers for Selective Release of Periplasmic Proteins from Gram-Negative Bacteria

2007 ◽  
Vol 0 (0) ◽  
pp. 0-0 ◽  
Author(s):  
J.R. Allen ◽  
A.Y. Patkar ◽  
T.C. Frank ◽  
F.A. Donate ◽  
Y. ChunChiu ◽  
...  
Keyword(s):  
Gram Negative Bacteria ◽  
Glycol Ethers ◽  
Gram Negative ◽  
Periplasmic Proteins

scholarly journals Secretin channel-interactors prevent antibiotic influx during type IV pili assembly in P. aeruginosa

2021 ◽  
Author(s):  
Hongbaek Cho ◽  
Oh Hyun Kwon ◽  
Joel W Sher ◽  
Bi-o Kim ◽  
You-Hee Cho
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Virulence Factors ◽  
Bacterial Pathogenesis ◽  
Type Iv Pili ◽  
Permeability Barrier ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Type Iv ◽  
Periplasmic Proteins ◽  
And Function

Type IV pili (T4P) are important virulence factors involved in host attachment and other aspects of bacterial pathogenesis. In Gram-negative bacteria, the T4P filament is polymerized from pilin subunits at the platform complex in the inner membrane (IM) and exits the outer membrane (OM) through the OM secretin channel. Although it is essential for T4P assembly and function, the OM secretin complexes can potentially impair the permeability barrier function of the OM and allow the entry of antibiotics and other toxic molecules. The mechanism by which Gram-negative bacteria prevent secretin-mediated OM leakage is currently not well understood. Here, we report a discovery of SlkA and SlkB (PA5122 and PA5123) that prevent permeation of several classes of antibiotics through the secretin channel of Pseudomonas aeruginosa type IV pili. We found these periplasmic proteins interact with the OM secretin complex and prevent toxic molecules from entering through the channel when there is a problem in the assembly of the T4P IM subcomplexes or when docking between the OM and IM complexes is defective.

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