Matching Items (4)
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Description

A 3-D fate map of the chicken (Gallus gallus) embryo with the prospective point of ingression and yolk. The area where the primitive streak will form during gastrulation is shown. The anterior- posterior axis is shown by labeling the anterior and posterio ends (A) and (P). Different colors indicate prospective

A 3-D fate map of the chicken (Gallus gallus) embryo with the prospective point of ingression and yolk. The area where the primitive streak will form during gastrulation is shown. The anterior- posterior axis is shown by labeling the anterior and posterio ends (A) and (P). Different colors indicate prospective fates of different regions of the epiblast after gastrulation. The turquoise shaded region represents the prospective ectoderm, the lavender shaded region represents the prospective mesoderm, the dark blue shaded region represents the prospective endoderm, and the white shaded region represents the prospective extraembryonic area.

Created2014-02-26
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Description

This image shows a chicken (Gallus gallus) embryo undergoing gastrulation in stage four (18-19 hrs after laying) according to the Hamburger-Hamilton staging series. At this point in time the chicken embryo is a blastoderm (shown in blue). The first magnification of the embryo shows that the blastoderm cell layers have

This image shows a chicken (Gallus gallus) embryo undergoing gastrulation in stage four (18-19 hrs after laying) according to the Hamburger-Hamilton staging series. At this point in time the chicken embryo is a blastoderm (shown in blue). The first magnification of the embryo shows that the blastoderm cell layers have thickened to form the primitive streak and Hensen's node. The primitive streak extends from the posterior (P) region to the anterior (A) region. The second rectangular magnification shows the blastoderm cross-sectioned through the primitive streak. The cross-section shows the blastoderm's two cell layers, the epiblast and the hypoblast. The fluid filled cavity between the two cell layers is the blastocoel. The space left between the hypoblast cell layer and the yolk is called the subgerminal cavity.

Created2014-02-26
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Description
Necrotic enteritis (NE) is caused by type A strains of the bacterium Clostridium perfringens, leading to an estimated 2 billion dollar global economic loss in the poultry industry annually. Traditionally, NE has been effectively controlled by antibiotics added to the diet of poultry. Concerns about increasing antibiotic resistance of poultry

Necrotic enteritis (NE) is caused by type A strains of the bacterium Clostridium perfringens, leading to an estimated 2 billion dollar global economic loss in the poultry industry annually. Traditionally, NE has been effectively controlled by antibiotics added to the diet of poultry. Concerns about increasing antibiotic resistance of poultry and human based pathogens have led to the consideration of alternative approaches for controlling disease, such as vaccination. NE causing strains of C. perfringens produce two major toxins, α-toxin and NetB. Immune responses against either toxin can provide partial protection against NE. We have developed a fusion protein combining a non-toxic carboxy-terminal domain of the α-toxin (PlcC) and an attenuated, mutant form of NetB (NetB-W262A) for use as a vaccine antigen to immunize poultry against NE. We utilized a DNA sequence that was codon-optimized for Nicotiana benthamiana to enable high levels of expression. The 6-His tagged PlcC-NetB fusion protein was synthesized in N. benthamiana using a geminiviral replicon transient expression system. The fusion protein was purified by metal affinity chromatography and used to immunize broiler birds. Immunized birds produced a strong serum IgY response against both the plant produced PlcC-NetB protein and against bacterially produced His-PlcC and His-NetB. However, the PlcC-NetB fusion had antibody titers four times that of the bacterially produced toxoids alone. Immunized birds were significantly protected against a subsequent in-feed challenge with virulent C. perfringens when treated with the fusion protein. These results indicate that a plant-produced PlcC-NetB is a promising vaccine candidate for controlling NE in poultry.
ContributorsHunter, Joseph G (Author) / Mason, Hugh (Thesis advisor) / Mor, Tsafrir (Committee member) / Blattman, Joseph (Committee member) / Arizona State University (Publisher)
Created2018
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Description
The glycation of plasma proteins leading to the production of advanced glycation end products (AGEs) and subsequent damage is a driving factor in the pathophysiology of diabetic complications. The overall research objective was to elucidate the mechanisms by which birds prevent protein glycation in the presence of naturally high plasma

The glycation of plasma proteins leading to the production of advanced glycation end products (AGEs) and subsequent damage is a driving factor in the pathophysiology of diabetic complications. The overall research objective was to elucidate the mechanisms by which birds prevent protein glycation in the presence of naturally high plasma glucose concentrations. This was accomplished through the specific purpose of examining the impact of temperature and glucose concentration on the percent glycation of chicken serum albumin (CSA) in comparison to human serum albumin (HSA). Purified CSA and HSA solutions prepared at four different glucose concentrations (0 mM, 5.56 mM, 11.11 mM, and 22.22 mM) were incubated at three different temperatures (37.0°C, 39.8°C, and 41.4°C) on separate occasions for seven days with aliquots extracted on days 0, 3, and 7. Samples were analyzed by LC-ESI-MS for percent glycation of albumin. The statistically significant interaction between glucose concentration, temperature, albumin type, and time as determined by four-way repeated measures ANOVA (p = 0.032) indicated that all independent variables interacted to affect the mean percent glycation of albumin. As glucose concentration increased, the percent glycation of both HSA and CSA increased over time at all temperatures. In addition, HSA was glycated to a greater extent than CSA at the two higher glucose concentrations examined for all temperature conditions. Temperature differentially affected percent glycation of HSA and CSA wherein glycation increased with rising temperatures for HSA but not CSA. The results of this study suggest an inherent difference between the human and chicken albumin that contributes to the observed differences in glycation. Further research is needed to characterize this inherent difference in an effort to elucidate the mechanism by which birds protect plasma proteins from glycation. Future related work has the potential to lead to the development of novel therapies to prevent or reverse protein glycation prior to the formation of AGEs in humans, thus preventing the development and devastating effects of numerous diabetic complications.
ContributorsZuck, Jessica (Author) / Sweazea, Karen (Thesis advisor) / Johnston, Carol (Committee member) / Lespron, Christy (Committee member) / Arizona State University (Publisher)
Created2016