نتایج جستجو برای: heat labile enterotoxin b subunit ltb
تعداد نتایج: 1171501 فیلتر نتایج به سال:
The ecotoxicological effects of transgenic maize-expressed vaccine protein, Escherichia coli heat-labile enterotoxin subunit B (LTB), on two soil invertebrates were studied under laboratory settings. After being reared for 28 days on LTB-maize-treated soils, no apparent mortality of the springtail, Folsomia candida , or the earthworm, Eisenia fetida , was observed at levels well above conservat...
Citation: Kumar A (2015) Commentary: Incorporation of membrane-anchored flagellin or Escherichia coli heat-labile enterotoxin B subunit enhances the immunogenicity of rabies virus-like particles in mice and dogs. Front. Microbiol. 6:1039. doi: 10.3389/fmicb.2015.01039 Commentary: Incorporation of membrane-anchored flagellin or Escherichia coli heat-labile enterotoxin B subunit enhances the immu...
We expressed the heat-labile enterotoxin B (LTB) subunit from enterotoxigenic Escherichia coli and the cholera toxin B (CTB) subunit from Vibrio cholerae under the control of the rice (Oryza sativa) globulin (Glb) promoter. Binding of recombinant LTB and CTB proteins was confirmed based on GM1-ganglioside binding enzyme-linked immunosorbent assays (GM1-ELISA). Real-time PCR of three generations...
Rotavirus is the leading cause of severe diarrheal disease among newborns. Plant-based rotavirus vaccines have been developed in recent years and have been proven to be effective in animal models. In the present study, we report a bivalent vaccine candidate expressing rotavirus subunits VP6 and NSP4 fused with the adjuvant subunit B of E. coli heat-labile enterotoxin (LTB) in maize seeds. The R...
We used the Salmonella typhi galactose epimerase (galE) mutant strain Ty21a, shown to be a safe, effective, living, attenuated oral typhoid vaccine, as a recipient for a recombinant plasmid containing the gene for production of the nontoxic B subunit of the heat-labile enterotoxin of Escherichia coli. The S. typhi derivative, strain SE12, produced heat-labile enterotoxin subunit B that was stru...
Heat-labile enterotoxin subunit B (LTB) is a non-catalytic protein from a pentameric subunit of Escherichia coli. Based on its function of binding specifically to ganglioside GM1 on the surface of cells, a novel nanoparticle (NP) composed of a mixture of bovine serum albumin (BSA) and LTB was designed for targeted delivery of 5-fluorouracil to tumor cells. BSA-LTB NPs were characterized by dete...
Mycoplasma hyopneumoniae is the etiological agent of porcine enzootic pneumonia (EP), leading to a mild and chronic in swine. Relative control has been attained through active vaccination programs, but remains significant economic challenge swine industry. Cellular immunity plays key role prevention pneumonia. Therefore, development more efficient vaccine that confers strong against M. necessar...
A novel nontoxic form of chimeric mucosal adjuvant that combines the A subunit of mutant cholera toxin E112K with the pentameric B subunit of heat-labile enterotoxin from enterotoxigenic Escherichia coli was constructed by use of the Brevibacillus choshinensis expression system (mCTA/LTB). Nasal immunization of mice with tetanus toxoid (TT) plus mCTA/LTB elicited significant TT-specific immunog...
Background: Enterotoxigenic Escherichia coli (ETEC) strains are the major causes of diarrheal disease in humans and animals. Colonization factors and enterotoxins are the major virulence factors in ETEC pathogenesis. For the broad-spectrum protection against ETEC, one could focus on colonization factors and non-toxic heat labile as a vaccine candidate. Methods: A fusion protein is composed of a...
Although most enteropathogenic Escherichia coli strains do not produce recognized enterotoxins, we wished to examine whether they produce any factors like heat-stable enterotoxin b or cholera toxin active subunits that might be missed by conventional assay methods. E. coli strains E851 (O142) and E2348 (O127) that had caused diarrhea in volunteers were negative for heat-labile enterotoxin and h...
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