Mutant OmpF porins of Yersinia pseudotuberculosis with deletions of external loops: Structure–functional and immunochemical properties

Sidorova, O. V.; Khomenko, V. A.; Portnyagina, O. Yu.; Likhatskaya, G. N.; Vakorina, T. I.; Kim, N. Yu; Chistyulin, D. K.; Соловьева, Т. Ф.; Novikova, O. D.

doi:10.1016/j.bbrc.2014.02.018

Cited by 7 publications

(3 citation statements)

References 17 publications

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“…As expected, BALB/c mice vaccinated with the renatured and purified rOmpF protein elicited a significant immunogenic response, which was consistent with the previous report (Sidorova et al 2014). The iELISA results showed that the antiserum not only had high affinity against rOmpF (1: 240,000 dilution) but also against the whole cell (1:27,000 dilution) (Fig.…”

Section: Discussionsupporting

confidence: 93%

“…Liu et al demonstrated that the recombinant OmpC and OmpF proteins from E. coli stimulated strong immunoglobulin G (IgG) antibody responses, and provided 62.5 and 87.5% protection against E. coli PCN033, respectively (Liu et al 2012). Immunization with OmpF of Yersinia pseudotuberculosis not only resulted in production of high-avidity antibodies, but also stimulated bactericidal activity of peritoneal macrophages (Sidorova et al 2014). Sharma et al suggested that the OmpF epitope (66–80) in fusion with a carrier protein is a promising vaccine candidate against A. hydrophila (Sharma and Dixit 2015).…”

Section: Introductionmentioning

confidence: 99%

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Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella

et al. 2017

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Diarrhea caused by pathogenic Escherichia coli (E. coli) is one of the most serious infectious diseases in humans and animals. Due to antibiotics resistance and the lack of efficient vaccine, more attention should be paid to find potential versatile vaccine candidates to prevent diseases. In this study, the sequence homology analysis indicated that OmpF from E. coli CVCC 1515 shares a high identity (90−100%) with about half of the E. coli (46.7%) and Shigella (52.8%) strains. Then the recombinant OmpF was supposed to be developed as a versatile vaccine to prevent E. coli infection. OmpF was expressed in E. coli BL21 (DE3) using the auto-induction method. The recombinant OmpF (rOmpF) protein had an average molecular weight of 40 kDa with the purity of 90%. Immunological analysis indicated that the titers of anti-rOmpF sera against rOmpF and whole cells were 1:240,000 and 1:27,000, respectively. The opsonophagocytosis result showed that 72.21 ± 11.39 and 11.04 ± 3.90% of bacteria were killed in the rOmpF immunization and control groups, respectively. The survival ratio of mice immunized with rOmpF ranged between 40 and 60% as observed within 36 h after challenge, indicating mice were partially protected from E. coli CVCC 1515 infection. The expressed rOmpF protein induced an effective immune response, but only provide a weak protection against pathogenic E. coli CVCC 1515 and a small reduction in E. coli CICC 21530 (O157:H7) excretion in a mouse infection model. Native forms of the OmpF antigen may be studied for immunogenicity and potential protective efficacy.

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Section: Discussionsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella

et al. 2017

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“…As the major components and one of the most abundant proteins in the outer membrane, bacterial porin proteins play a critical role in bacterial pathogenesis and interactions with the host immune system ( 68 , 69 ). OmpF, as one of the best-studied bacterial porins on structural and functional characteristics ( 70 – 74 ), has been reported to be a protective antigen against some bacterial infections ( 40 , 74 – 77 ) and been predicted to be a conserved porin located on the surface of Yersinia ( 42 ), which suggests it is possible to use as an immunogen candidate providing immunoprotection against Yersinia infection.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization, Phylogenetic, Expression, and Protective Immunity Analysis of OmpF, a Promising Candidate Immunogen Against Yersinia ruckeri Infection in Channel Catfish

Wang

Qin

et al. 2018

Front. Immunol.

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Outer membrane porins, as the major components of Gram-negative bacterial membrane proteins, have been proven to be involved in interactions with the host immune system and potent protective antigen candidates against bacterial infection in fish. Outer membrane porin F (OmpF) is one of the major porins of Yersinia ruckeri (Y. ruckeri), the causative agent of enteric red mouth disease of salmonid and non-salmonid fish. In the present study, the molecular characterization and phylogenetic analysis of OmpF gene was studied, heterogenous expression, immunogenicity and protective immunity of OmpF were systemically evaluated as a subunit vaccine for channel catfish against Y. ruckeri infection. The results showed that OmpF gene was highly conserved among 15 known Yersinia species based on the analysis of conserved motifs, sequences alignment and phylogenetic tree, and was subjected to negative/purifying selection with global dN/dS ratios value of 0.649 throughout the evolution. Besides, OmpF was also identified to have immunogenicity by western blotting and was verified to be located on the surface of Y. ruckeri using cell surface staining and indirect immunofluorescence assays. Moreover, recombinant OmpF (rtOmpF) as a subunit vaccine was injected with commercial adjuvant ISA763, significantly enhanced the immune response by increasing serum antibody levels, lysozyme activity, complement C3 activity, total protein content, SOD activity, immune-related genes expression in the head kidney and spleen, and survival percent of channel catfish against Y. ruckeri infection. Thus, our present results not only enriched the information of molecular characterization and phylogenetics of OmpF, but also demonstrated that OmpF holds promise to be used as a potential antigen against Y. ruckeri infection in fish.

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Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential

Novikova

Uversky

Zelepuga

2021

Progress in Molecular Biology and Translational Science

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Mutant OmpF porins of Yersinia pseudotuberculosis with deletions of external loops: Structure–functional and immunochemical properties

Cited by 7 publications

References 17 publications

Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella

Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella

Molecular Characterization, Phylogenetic, Expression, and Protective Immunity Analysis of OmpF, a Promising Candidate Immunogen Against Yersinia ruckeri Infection in Channel Catfish

Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential

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