scholarly journals Immunochemical Properties of Recombinant Ompf Porin from Outer Membrane of Yersinia pseudotuberculosis

10.5772/35207 ◽  
2012 ◽  
Author(s):  
Olga Portnyagina ◽  
Olga Sidorova ◽  
Valentina Khomenko ◽  
Olga Novikova ◽  
Marina Issaeva ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Yersinia Pseudotuberculosis ◽  
Ompf Porin

Influence of cultivation conditions on spatial structure and functional activity of OmpF-like porin from outer membrane of Yersinia pseudotuberculosis

2008 ◽  
Vol 73 (2) ◽  
pp. 139-148 ◽  
Author(s):  
O. D. Novikova ◽  
T. I. Vakorina ◽  
V. A. Khomenko ◽  
G. N. Likhatskaya ◽  
N. Yu. Kim ◽  
...  
Keyword(s):  
Spatial Structure ◽  
Outer Membrane ◽  
Functional Activity ◽  
Yersinia Pseudotuberculosis ◽  
Cultivation Conditions

The Colicin E3 Outer Membrane Translocon:  Immunity Protein Release Allows Interaction of the Cytotoxic Domain with OmpF Porin†

Biochemistry ◽  
2006 ◽  
Vol 45 (34) ◽  
pp. 10199-10207 ◽  
Author(s):  
Stanislav D. Zakharov ◽  
Mariya V. Zhalnina ◽  
Onkar Sharma ◽  
William A. Cramer
Keyword(s):  
Outer Membrane ◽  
Protein Release ◽  
Immunity Protein ◽  
Ompf Porin ◽  
Colicin E3

Inclusion Bodies of Recombinant OmpF Porin from Yersinia pseudotuberculosis: Properties and Structural Characterization

2019 ◽  
Vol 84 (6) ◽  
pp. 672-685
Author(s):  
V. A. Khomenko ◽  
E. V. Sidorin ◽  
S. I. Bakholdina ◽  
G. A. Naberezhnykh ◽  
N. Yu. Kim ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Inclusion Bodies ◽  
Yersinia Pseudotuberculosis ◽  
Ompf Porin

scholarly journals Comparative aspects of the diffusion of norfloxacin, cefepime and spermine through the F porin channel of Enterobacter cloacae

2000 ◽  
Vol 348 (1) ◽  
pp. 223-227 ◽  
Author(s):  
Jacqueline CHEVALIER ◽  
Monique MALLÉA ◽  
Jean-Marie PAGÈS
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Clinical Isolate ◽  
Initial Rate ◽  
Enterobacter Cloacae ◽  
Ompf Porin ◽  
Rate Of Penetration ◽  
Cephalosporin Antibiotics ◽  
Pore Forming Proteins

In Enterobacteriaceae, the permeability of the outer membrane to hydrophilic antibiotics is associated with the presence of pore-forming proteins. We tested the diffusion of the fluoroquinolone norfloxacin in four Enterobacter cloacae strains: a clinical isolate and three derivatives variously producing or lacking the D and F porins. We analysed the entry of norfloxacin into E. cloacae cells in the presence of either the polyamine spermine or the recently developed cefepime, which are known to penetrate through the Escherichia coli OmpF porin. Uptake of the fluoroquinolone was decreased in both cases; the initial rate of penetration decreased as more spermine blocked the channel. Our results indicate that, like β-lactam molecules, fluoroquinolones translocate through the outer membrane via the F porin and that cefepime and norfloxacin entries are polyamine-sensitive. This suggests that the closure of the F porin channel by polyamines might modulate the susceptibility of E. cloacae to both fluoroquinolone and cephalosporin antibiotics.

Recombinant phospholipase A1 of the outer membrane of psychrotrophic Yersinia pseudotuberculosis: Expression, purification, and characterization

2016 ◽  
Vol 81 (1) ◽  
pp. 47-57 ◽  
Author(s):  
S. I. Bakholdina ◽  
N. M. Tischenko ◽  
E. V. Sidorin ◽  
M. P. Isaeva ◽  
G. N. Likhatskaya ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Yersinia Pseudotuberculosis ◽  
Purification And Characterization ◽  
Phospholipase A1

scholarly journals Immunogenicity and Protective Activity of a Chimeric Protein Based on the Domain III of the Tick-Borne Encephalitis Virus E Protein and the OmpF Porin of Yersinia pseudotuberculosis Incorporated into the TI-Complex

2018 ◽  
Vol 19 (10) ◽  
pp. 2988
Author(s):  
Nina Sanina ◽  
Natalia Chopenko ◽  
Andrey Mazeika ◽  
Ludmila Davydova ◽  
Galina Leonova ◽  
...  
Keyword(s):  
Yersinia Pseudotuberculosis ◽  
Chimeric Protein ◽  
Encephalitis Virus ◽  
Protective Activity ◽  
Ompf Porin ◽  
E Protein ◽  
Tick Borne Encephalitis ◽  
Tick Borne Encephalitis Virus ◽  
Domain Iii ◽  
Ti Complexes

Tick-borne encephalitis (TBE) is a widespread, dangerous infection. Unfortunately, all attempts to create safe anti-TBE subunit vaccines are still unsuccessful due to their low immunogenicity. The goal of the present work was to investigate the immunogenicity of a recombinant chimeric protein created by the fusion of the EIII protein, comprising domain III and a stem region of the tick-borne encephalitis virus (TBEV) E protein, and the OmpF porin of Yersinia pseudotuberculosis (OmpF-EIII). Adjuvanted antigen delivery systems, the tubular immunostimulating complexes (TI-complexes) based on the monogalactosyldiacylglycerol from different marine macrophytes, were used to enhance the immunogenicity of OmpF-EIII. Also, the chimeric protein incorporated into the most effective TI-complex was used to study its protective activity. The content of anti-OmpF-EIII antibodies was estimated in mice blood serum by enzyme-linked immunosorbent assay (ELISA). To study protective activity, previously immunized mice were infected with TBEV strain Dal’negorsk (GenBank ID: FJ402886). The animal survival was monitored daily for 21 days. OmpF-EIII incorporated into the TI-complexes induced about a 30–60- and 5–10-fold increase in the production of anti-OmpF-EIII and anti-EIII antibodies, respectively, in comparison with the effect of an individual OmpF-EIII. The most effective vaccine construction provided 60% protection. Despite the dramatic effect on the specific antibody titer, the studied TI-complex did not provide a statistically significant increase in the protection of OmpF-EIII protein. However, our results provide the basis of the future search for approaches to design and optimize the anti-TBEV vaccine based on the OmpF-EIII protein.

scholarly journals Immunotropic and Immunogenic Properties of Nonspecific Yersinia Porins

2019 ◽  
Vol 3 (4) ◽  
pp. 350-372
Keyword(s):  
Outer Membrane ◽  
Yersinia Pseudotuberculosis ◽  
Molecular Mimicry ◽  
Receptor Activation ◽  
Eukaryotic Cell ◽  
Elisa Test ◽  
Multiple Organ ◽  
Laboratory Animals ◽  
Cell Functions ◽  
Protective Antigens

The purpose of the study is to summarize our own data and literature data on the signifi cance of poreforming proteins of the outer membrane of Yersinia as factors of their pathogenicity and as diagnostic and protective antigens, and their role in pathological processes considered non-infectious. In the last decades of the last century, the epidemic signifi cance of intestinal yersiniosis caused by the bacteria of Yersinia genus, Yersinia pseudotuberculosis and Yersinia enterocolitica, which are the «doubles» of the plague pathogen (Yersinia pestis) by genetic, cultural, biochemical, and other properties, has signifi cantly increased. It has been established that acute yersiniosis infections without eff ective treatment can pass into secondary focal forms, leading to the development of systemic diseases that were not previously considered infectious (for example, Grave’s disease). Th ey are characterized by multiple organ lesions, dysfunctions of the cardiovascular and nervous systems, musculoskeletal system, urinary system and gastrointestinal tract, which is a consequence of autoimmune processes based on the ability of Yersinia to molecular mimicry. Th e paper shows that porins play a signifi cant role in the development of the infectious process and can be considered as pathogenic factors of bacteria. Together with other components of the outer membrane of gram negative bacteria, they provide adhesion, invasion and colonization of the cells of the host organism by bacteria. Porins can aff ect a number of eukaryotic cell functions, including cytokine expression, receptor activation, apoptosis induction, and regulation of the actin cytoskeleton. It has been established that pore-forming Yersinia proteins are protective antigens. The administration of them to laboratory animals induces the formation of species-specifi c immunity, which allows us to recommend porin protein as a component of chemical and genetic engineering vaccines. Porins are promising for the development of ELISA test systems for the diagnosis of pseudotuberculosis and intestinal yersiniosis, as well as immunopathologies caused by Yersinia bacteria. Given the high degree of similarity of the primary structures of Yersinia porins, it can be assumed that protective preparations created on their basis will protect against infections caused by intestinal yersiniosis, pseudotuberculosis and plague pathogens

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