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Article ; Online: Binding of Mucin by E. coli from Human Gut.

Vakhrusheva, T V / Baikova, Yu P / Balabushevich, N G / Gusev, S A / Lomakina, G Yu / Sholina, E A / Moshkovskaya, M A / Shcherbakov, P L / Pobeguts, O V / Mikhal'chik, E V

Bulletin of experimental biology and medicine

2018 Volume 165, Issue 2, Page(s) 235–238

Abstract: Cells of E. coli isolates from the gut of healthy volunteers (N=5) and patients ... with Crohn's disease (N=5) and laboratory E. coli strain DH5α bound mucin in vitro in similar amounts ranging from 0.02 ...

Abstract	Cells of E. coli isolates from the gut of healthy volunteers (N=5) and patients with Crohn's disease (N=5) and laboratory E. coli strain DH5α bound mucin in vitro in similar amounts ranging from 0.02 to 0.12 mg/mg of bacterial dry weight. Binding was evaluated by the decrease in optical absorption of mucin solution at 214 nm after incubation with bacteria. Detailed analysis of mucin binding by one of isolates showed that during incubation of 0.09 mg/ml bacteria in 0.15 M NaCl containing 0.1 mg/ml mucin at 25
MeSH term(s)	Bacterial Adhesion ; Crohn Disease/metabolism ; Crohn Disease/microbiology ; Crohn Disease/pathology ; Escherichia coli/isolation & purification ; Escherichia coli/metabolism ; Feces/microbiology ; Gastrointestinal Microbiome ; Healthy Volunteers ; Humans ; Intestines/microbiology ; Intestines/pathology ; Mucins/metabolism ; Protein Binding
Chemical Substances	Mucins
Language	English
Publishing date	2018-06-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	390407-6
ISSN	1573-8221 ; 0007-4888 ; 0365-9615
ISSN (online)	1573-8221
ISSN	0007-4888 ; 0365-9615
DOI	10.1007/s10517-018-4137-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Mucin adsorbed by E. coli can affect neutrophil activation in vitro.

Mikhalchik, Elena / Balabushevich, Nadezhda / Vakhrusheva, Tatiana / Sokolov, Alexey / Baykova, Julia / Rakitina, Daria / Scherbakov, Petr / Gusev, Sergey / Gusev, Alexander / Kharaeva, Zaira / Bukato, Olga / Pobeguts, Olga

FEBS open bio

2019 Volume 10, Issue 2, Page(s) 180–196

Abstract: ... Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro ...

Abstract	Bacteria colonizing human intestine adhere to the gut mucosa and avoid the innate immune system. We previously demonstrated that Escherichia coli isolates can adsorb mucin from a diluted solution in vitro. Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro. Activation was evaluated based on the detection of reactive oxygen species production by a chemiluminescent reaction (ChL), observation of morphological alterations in neutrophils and detection of exocytosis of myeloperoxidase and lactoferrin. We report that mucin adsorbed by cells of SharL1 isolate from Crohn's disease patient's inflamed ileum suppressed the potential for the activation of neutrophils in whole blood. Also, the binding of plasma complement proteins and immunoglobulins to the bacteria was reduced. Desialylated mucin, despite having the same adsorption efficiency to bacteria, had no effect on the blood ChL response. The effect of mucin suggests that it shields epitopes that interact with neutrophils and plasma proteins on the bacterial outer membrane. Potential candidates for these epitopes were identified among the proteins within the bacterial outer membrane fraction by 2D-PAGE, fluorescent mucin binding on a blot and HPLC-MS/MS. In vitro, the following proteins demonstrated mucin adsorption: outer membrane porins (OmpA, OmpC, OmpD and OmpF), adhesin OmpX, the membrane assembly factor OmpW, cobalamine transporter, ferrum uptake protein and the elongation factor Ef Tu-1. In addition to their other functions, these proteins are known to be bacterial surface antigens. Therefore, the shielding of epitopes by mucin may affect the dynamics and intensity of an immune response.
MeSH term(s)	Adsorption ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Humans ; Mucins/metabolism ; Neutrophil Activation/physiology ; Neutrophils/metabolism ; Porins ; Tandem Mass Spectrometry
Chemical Substances	Escherichia coli Proteins ; Mucins ; OmpC protein ; Porins
Language	English
Publishing date	2019-12-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2651702-4
ISSN	2211-5463 ; 2211-5463
ISSN (online)	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.12770
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Mucin adsorbed by E. coli can affect neutrophil activation in vitro

FEBS Open Bio. 2020 Feb., v. 10, no. 2

2020

Abstract: ... Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro ...

Abstract	Bacteria colonizing human intestine adhere to the gut mucosa and avoid the innate immune system. We previously demonstrated that Escherichia coli isolates can adsorb mucin from a diluted solution in vitro. Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro. Activation was evaluated based on the detection of reactive oxygen species production by a chemiluminescent reaction (ChL), observation of morphological alterations in neutrophils and detection of exocytosis of myeloperoxidase and lactoferrin. We report that mucin adsorbed by cells of SharL1 isolate from Crohn's disease patient's inflamed ileum suppressed the potential for the activation of neutrophils in whole blood. Also, the binding of plasma complement proteins and immunoglobulins to the bacteria was reduced. Desialylated mucin, despite having the same adsorption efficiency to bacteria, had no effect on the blood ChL response. The effect of mucin suggests that it shields epitopes that interact with neutrophils and plasma proteins on the bacterial outer membrane. Potential candidates for these epitopes were identified among the proteins within the bacterial outer membrane fraction by 2D‐PAGE, fluorescent mucin binding on a blot and HPLC‐MS/MS. In vitro, the following proteins demonstrated mucin adsorption: outer membrane porins (OmpA, OmpC, OmpD and OmpF), adhesin OmpX, the membrane assembly factor OmpW, cobalamine transporter, ferrum uptake protein and the elongation factor Ef Tu‐1. In addition to their other functions, these proteins are known to be bacterial surface antigens. Therefore, the shielding of epitopes by mucin may affect the dynamics and intensity of an immune response.
Keywords	Crohn disease ; Escherichia coli ; adhesins ; adsorption ; bacterial outer membranes ; chemiluminescence ; complement ; digestive tract mucosa ; epitopes ; exocytosis ; fluorescence ; humans ; ileum ; immune response ; immunoglobulins ; innate immunity ; lactoferrin ; mucins ; myeloperoxidase ; neutrophils ; patients ; peptide elongation factors ; porins ; reactive oxygen species
Language	English
Dates of publication	2020-02
Size	p. 180-196.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	2651702-4
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.12770
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Mucin adsorbed by E. coli can affect neutrophil activation in vitro

Elena Mikhalchik / Nadezhda Balabushevich / Tatiana Vakhrusheva / Alexey Sokolov / Julia Baykova / Daria Rakitina / Petr Scherbakov / Sergey Gusev / Alexander Gusev / Zaira Kharaeva / Olga Bukato / Olga Pobeguts

FEBS Open Bio, Vol 10, Iss 2, Pp 180-

2020 Volume 196

Abstract: ... Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro ...

Abstract	Bacteria colonizing human intestine adhere to the gut mucosa and avoid the innate immune system. We previously demonstrated that Escherichia coli isolates can adsorb mucin from a diluted solution in vitro. Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro. Activation was evaluated based on the detection of reactive oxygen species production by a chemiluminescent reaction (ChL), observation of morphological alterations in neutrophils and detection of exocytosis of myeloperoxidase and lactoferrin. We report that mucin adsorbed by cells of SharL1 isolate from Crohn's disease patient's inflamed ileum suppressed the potential for the activation of neutrophils in whole blood. Also, the binding of plasma complement proteins and immunoglobulins to the bacteria was reduced. Desialylated mucin, despite having the same adsorption efficiency to bacteria, had no effect on the blood ChL response. The effect of mucin suggests that it shields epitopes that interact with neutrophils and plasma proteins on the bacterial outer membrane. Potential candidates for these epitopes were identified among the proteins within the bacterial outer membrane fraction by 2D‐PAGE, fluorescent mucin binding on a blot and HPLC‐MS/MS. In vitro, the following proteins demonstrated mucin adsorption: outer membrane porins (OmpA, OmpC, OmpD and OmpF), adhesin OmpX, the membrane assembly factor OmpW, cobalamine transporter, ferrum uptake protein and the elongation factor Ef Tu‐1. In addition to their other functions, these proteins are known to be bacterial surface antigens. Therefore, the shielding of epitopes by mucin may affect the dynamics and intensity of an immune response.
Keywords	E. coli ; mucin ; neutrophils ; outer membrane proteins ; plasma proteins ; reactive oxygen species ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2020-02-01T00:00:00Z
Publisher	Wiley
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Nanotoxicity of ZrS 3 Probed in a Bioluminescence Test on E. coli Bacteria

Olga V. Zakharova / Alexander A. Gusev / Jehad Abourahma / Nataliia S. Vorobeva / Dmitry V. Sokolov / Dmitry S. Muratov / Denis V. Kuznetsov / Alexander Sinitskii

Nanomaterials, Vol 10, Iss 1401, p

The Effect of Evolving H 2 S

2020 Volume 1401

Abstract: ... TMTC material, toward photoluminescent E. coli bacteria in a bioluminescence test. We found ... intrinsically nontoxic to photoluminescent E. coli bacteria, it may exhibit high toxicity in aqueous media ...

Abstract	Materials from a large family of transition metal trichalcogenides (TMTCs) attract considerable attention because of their potential applications in electronics, optoelectronics and energy storage, but information on their toxicity is lacking. In this study, we investigated the toxicity of ZrS 3 , a prominent TMTC material, toward photoluminescent E. coli bacteria in a bioluminescence test. We found that freshly prepared ZrS 3 suspensions in physiological saline solution with concentrations as high as 1 g/L did not exhibit any toxic effects on the bacteria. However, ZrS 3 suspensions that were stored for 24 h prior to the bioluminescence tests were very toxic to the bacteria and inhibited their emission, even at concentrations down to 0.001 g/L. We explain these observations by the aqueous hydrolysis of ZrS 3 , which resulted in the formation of ZrO x on the surface of ZrS 3 particles and the release of toxic H 2 S. The formation of ZrO x was confirmed by the XPS analysis, while the characteristic H 2 S smell was noticeable for the 24 h suspensions. This study demonstrates that while ZrS 3 appears to be intrinsically nontoxic to photoluminescent E. coli bacteria, it may exhibit high toxicity in aqueous media. The results of this study can likely be extended to other transition metal chalcogenides, as their toxicity in aqueous solutions may also increase over time due to hydrolysis and the formation of H 2 S. The results of this study also demonstrate that since many systems involving nanomaterials are unstable and evolve over time in various ways, their toxicity may evolve as well, which should be considered for relevant toxicity tests.
Keywords	zirconium trisulfide ; nanotoxicity ; antibacterial properties ; bioluminescence test ; Escherichia coli ; Chemistry ; QD1-999
Subject code	290
Language	English
Publishing date	2020-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Effects of Non-Opiate Analogue of Leu-Enkephalin on the Ion Currents, Number of Nucleoli, and p53 Expression in Isolated Cardiomyocytes of Albino Rats.

Sazonova, E N / Gusev, I A / Filatova, T S

Bulletin of experimental biology and medicine

2023 Volume 175, Issue 4, Page(s) 544–548

Abstract: Acute exposure of isolated ventricular cardiomyocytes to non-opiate analogue of leu-enkephalin (NALE peptide: Phe-D-Ala-Gly-Phe-Leu-Arg) in a concentration of 100 μg/liter and 6-h incubation in NALE solution did not significantly change ATP-dependent ... ...

Abstract	Acute exposure of isolated ventricular cardiomyocytes to non-opiate analogue of leu-enkephalin (NALE peptide: Phe-D-Ala-Gly-Phe-Leu-Arg) in a concentration of 100 μg/liter and 6-h incubation in NALE solution did not significantly change ATP-dependent K
Language	English
Publishing date	2023-09-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	390407-6
ISSN	1573-8221 ; 0007-4888 ; 0365-9615
ISSN (online)	1573-8221
ISSN	0007-4888 ; 0365-9615
DOI	10.1007/s10517-023-05902-2
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 56: Show issues

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Article: (E,Z)-1-(4-Chloro-phen-yl)-5-phenyl-5-(phenyl-sulfan-yl)penta-2,4-dien-1-one.

Vologzhanina, Anna V / Gusev, Dmitry M / Golovanov, Alexander A / Pisareva, Valentina S

Acta crystallographica. Section E, Structure reports online

2013 Volume 69, Issue Pt 9, Page(s) o1479

Abstract: The penta-2,4-dien-1-one fragment of the title compound, C23H17ClOS, is twisted by 20.0 (3)°, as measured by the dihedral angle between the planes of the carbonyl group and its attached C atom and the distant C=C double bond and its attached C atom. The ... ...

Abstract	The penta-2,4-dien-1-one fragment of the title compound, C23H17ClOS, is twisted by 20.0 (3)°, as measured by the dihedral angle between the planes of the carbonyl group and its attached C atom and the distant C=C double bond and its attached C atom. The 4-chloro-phenyl group forms a dihedral angle of 4.0 (3)° with the adjacent carbonyl group. Conjugation between the phenyl ring and the C=C double bond is absent; the dihedral angle between the phenyl ring and the C-C=C fragment is 34.3 (2)°. In the crystal, mol-ecules are linked via C-H⋯O hydrogen bonds, forming chains parallel to the b-axis direction.
Language	English
Publishing date	2013-08-31
Publishing country	United States
Document type	Journal Article
ZDB-ID	2041947-8
ISSN	1600-5368
ISSN	1600-5368
DOI	10.1107/S160053681302312X
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Article: Contra-Intuitive Features of Time-Domain Brillouin Scattering in Collinear Paraxial Sound and Light Beams.

Gusev, Vitalyi E

Photoacoustics

2020 Volume 20, Page(s) 100205

Abstract: Time-domain Brillouin scattering is an opto-acousto-optical probe technique for the evaluation of transparent materials. Via optoacoustic conversion, ultrashort pump laser pulses launch coherent acoustic pulses in the sample. Time-delayed ultrashort ... ...

Abstract	Time-domain Brillouin scattering is an opto-acousto-optical probe technique for the evaluation of transparent materials. Via optoacoustic conversion, ultrashort pump laser pulses launch coherent acoustic pulses in the sample. Time-delayed ultrashort probe laser pulses monitor the propagation of the coherent acoustic pulses via the photo-elastic effect, which induces light scattering. A photodetector collects both the acoustically scattered light and the probe light reflected by the sample structure for the heterodyning. The scattered probe light carries information on the acoustical, optical and acousto-optical parameters of the material for the current position of the coherent acoustic pulse. Thus, among other applications, time-domain Brillouin scattering is a technique for three-dimensional imaging. Sharp focusing of coherent acoustic pulses and probe laser pulses could increase lateral spatial resolution of imaging, but could potentially diminish the depth of imaging. However, the theoretical analysis presented in this manuscript contra-intuitively demonstrates that the depth and spectral resolution of the time-domain Brillouin scattering imaging, with collinearly propagating paraxial sound and light beams, do not depend on the focusing/diffraction of sound. The variations of the amplitude of the time-domain Brillouin scattering signal are only due to the variations of the probe light amplitude caused by light focusing/diffraction. Although the amplitude of the acoustically scattered light is proportional to the product of the local acoustical and probe light field amplitudes, the temporal dynamics of the time-domain Brillouin scattering signal amplitude is independent of the dynamics of the coherent acoustic pulse amplitude.
Language	English
Publishing date	2020-09-04
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2716706-9
ISSN	2213-5979
ISSN	2213-5979
DOI	10.1016/j.pacs.2020.100205
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Book: Rassejannyj skleroz

Gusev, E. I.

(Žurnal nevrologii i psichiatrii imeni S. S. Korsakova ; 2002, Spec. vypusk)

2002

Author's details	glavnyj red. E. I. Gusev
Series title	Žurnal nevrologii i psichiatrii imeni S. S. Korsakova ; 2002, Spec. vypusk Žurnal nevrologii i psichiatrii imeni S. S. Korsakova
Collection	Žurnal nevrologii i psichiatrii imeni S. S. Korsakova
Language	Russian
Size	80 S. : Ill., graph. Darst.
Publisher	Media Sphera
Publishing place	Moskva
Publishing country	Russian Federation
Document type	Book
HBZ-ID	HT013382317
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

Shelf mark	Loan status	Location
Zs B 746 -2002,Spec.vypusk-	verfügbar in Königswinter	Königswinter

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Book: Insul't

Gusev, E. I.

(Žurnal nevrologii i psichiatrii imeni S. S. Korsakova ; 2001, Vypusk 2)

2001

Author's details	glavnyj red. E. I. Gusev
Series title	Žurnal nevrologii i psichiatrii imeni S. S. Korsakova ; 2001, Vypusk 2 Žurnal nevrologii i psichiatrii imeni S. S. Korsakova
Collection	Žurnal nevrologii i psichiatrii imeni S. S. Korsakova
Language	Russian
Size	72 S. : graph. Darst.
Publisher	Media Sphera
Publishing place	Moskva
Publishing country	Russian Federation
Document type	Book
HBZ-ID	HT013083201
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

Shelf mark	Loan status	Location
Zs B 746 -2001,Vyp.2-	verfügbar in Königswinter	Königswinter

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