OmpA—FMDV VP1 fusion proteins: production, cell surface exposure and immune responses to the major antigenic domain of foot-and-mouth disease virus

Ruppert, Andreas; Arnold, Norbert; Hobom, Gerd

doi:10.1016/0264-410x(94)90305-0

Cited by 28 publications

(7 citation statements)

References 42 publications

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“…Model proteins, such as GFP [106] or β-galactosidase [107], have been displayed successfully on the surface of E. coli. Furthermore, relevant foot-and-mouth disease viral antigens [108] and malarial antigens [109] have been fused to OmpA and these fusions elicited antigen-specific immune responses. This principle has previously been employed for the production of recombinant BGs displaying the hepatitis B core antigen on their surface [110].…”

Section: Bgs As Carriersmentioning

confidence: 99%

Bacterial ghosts as adjuvant particles

Riedmann

Kyd

Cripps

et al. 2007

Expert Review of Vaccines

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The development of more advanced and effective vaccines is of great interest in modern medicine. These new-generation vaccines, based on recombinant proteins or DNA, are often less reactogenic and immunogenic than traditional vaccines. Thus, there is an urgent need for the development of new and improved adjuvants. Besides many other immunostimulatory components, the bacterial ghost (BG) system is currently under investigation as a potent vaccine delivery system with intrinsic adjuvant properties. BGs are nonliving cell envelope preparations from Gram-negative cells, devoid of cytoplasmic contents, while their cellular morphology and native surface antigenic structures remain preserved. Owing to the particulate nature of BGs and the fact that they contain many well known immune-stimulating compounds, BGs have the potential to enhance immune responses against ghost-delivered target antigens.

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Section: Bgs As Carriersmentioning

confidence: 99%

Bacterial ghosts as adjuvant particles

Riedmann

Kyd

Cripps

et al. 2007

Expert Review of Vaccines

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“…It is considered that co-infection of viable E. coli O157:H7 organism and toxins is general, and a novel vaccine which could provide the co-prevention of bacterial adhesion and toxic damage is imminent. In this study, the linear Stx2Am-Stx1B antigen was displayed on the surface of E. coli O157:H7 BGs based on a sandwich vector pSOmpA 28 29 30 31 which was constructed by the partial out membane protein A (OmpA) of Shigella dysenteriae and partial OmpA of E. coli to construct a novel candidate vaccine named rSOBGs. The immunogenicity, protection ability and immunologic mechanism against the challenge of E. coli O157:H7 were described subsequently.…”

mentioning

confidence: 99%

Novel fusion antigen displayed-bacterial ghosts vaccine candidate against infection of Escherichia coli O157:H7

Cai

Liu

et al. 2015

Sci Rep

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Infection with Escherichia coli O157:H7 may develop into hemorrhagic colitis, or hemolytic uremic syndrome (HUS), which usually causes kidney failure or even death. The adhesion and toxins are the important virulent factors. In this study, a novel vaccine candidate rSOBGs was constructed based on the bacterial ghost (BG). rSOBGs maintained the integrity of cellular morphology and displayed the linear Stx2Am-Stx1B antigen on the surface of outer membrane. rSOBGs induced Stxs-specific IgA/IgG antibodies and stronger intimin-specific IgA/IgG antibodies effectively in sera in this study. In vivo, the rSOBGs provided the higher protection rate (52%) than native bacterial ghost-OBGs (12%) when challenged intragastricly with high dose (500 LD50) viable E. coli O157:H7. Meanwhile, the rSOBGs provided higher protection rate (73.33%) than OBGs when challenged with 2 LD50 even to 5 LD50 lysed E. coli O157:H7. In vitro, the rSOBGs-immunized sera possessed neutralizing activity to lysed pathogenic bacteria. Furthermore, the results of histopathology also displayed that the administration of rSOBGs have the ability to reduce or inhibit the adhesion lesions and toxins damages of organs. The novel vaccine candidate rSOBGs induced both anti-toxin and anti-adhesion immune protection, suggesting the possibility to prevent the infectious diseases caused by Escherichia coli O157:H7.

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“…Before comparing our prediction to the competing models for OmpA, we first used experimental data on the localization of specific residues to assess the reliability of the NN output (Chen et al, 1980;Morona et al, 1984Morona et al, , 1985Freud1 et al, 1986Freud1 et al, , 1989Ried et al, 1994;Ruppert et al, 1994;Georgiou et al, 1996). Experimental and predicted localizations are in agreement in the majority of cases (13 out of 19; see Table I in the supplementary material).…”

Section: Ompa From Escherichia Colimentioning

confidence: 99%

Prediction by a neural network of outer membrane β‐strand protein topology

Diederichs¹,

Freigang²,

Umhau³

et al. 1998

Protein Science

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An artificial neural network (NN) was trained to predict the topology of bacterial outer membrane (OM) beta-strand proteins. Specifically, the NN predicts the z-coordinate of Calpha atoms in a coordinate frame with the outer membrane in the xy-plane, such that low z-values indicate periplasmic turns, medium z-values indicate transmembrane beta-strands, and high z-values indicate extracellular loops. To obtain a training set, seven OM proteins (porins) with structures known to high resolution were aligned with their pores along the z-axis. The relationship between Calpha z-values and topology was thereby established. To predict the topology of other OM proteins, all seven porins were used for the training set. Z-values (topologies) were predicted for two porins with hitherto unknown structure and for OM proteins not belonging to the porin family, all with insignificant sequence homology to the training set. The results of topology prediction compare favorably with experimental topology data.

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OmpA—FMDV VP1 fusion proteins: production, cell surface exposure and immune responses to the major antigenic domain of foot-and-mouth disease virus

Cited by 28 publications

References 42 publications

Bacterial ghosts as adjuvant particles

Bacterial ghosts as adjuvant particles

Novel fusion antigen displayed-bacterial ghosts vaccine candidate against infection of Escherichia coli O157:H7

Prediction by a neural network of outer membrane β‐strand protein topology

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