Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin
2016 Summer. Includes bibliographical references. Transmissible Spongiform Encephalopathies (TSEs) are a group of diseases caused by an abnormal version, PrPRES, of the normal cellular host protein prion protein (Prnp) termed PrPC. Disease is fatal resulting in amyloid deposits and spongiform degene...
Main Author: | |
---|---|
Other Authors: | , , , |
Format: | Text |
Language: | English |
Published: |
Colorado State University. Libraries
2016
|
Subjects: | |
Online Access: | http://hdl.handle.net/10217/176603 |
id |
ftcolostateunidc:oai:mountainscholar.org:10217/176603 |
---|---|
record_format |
openpolar |
spelling |
ftcolostateunidc:oai:mountainscholar.org:10217/176603 2023-06-11T04:03:18+02:00 Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin Ortega, Aimee Elise Zabel, Mark Mathiason, Candace Leach, Jan Wilusz, Jeffrey 2016-08-18T23:10:03Z born digital masters theses application/pdf http://hdl.handle.net/10217/176603 English eng eng Colorado State University. Libraries 2000-2019 - CSU Theses and Dissertations Ortega_colostate_0053N_13631.pdf http://hdl.handle.net/10217/176603 Copyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright. Text 2016 ftcolostateunidc 2023-05-04T17:39:26Z 2016 Summer. Includes bibliographical references. Transmissible Spongiform Encephalopathies (TSEs) are a group of diseases caused by an abnormal version, PrPRES, of the normal cellular host protein prion protein (Prnp) termed PrPC. Disease is fatal resulting in amyloid deposits and spongiform degeneration in the brain in most but not all cases. Clinical signs can include wasting, increases in salivation, and general motor impairment but many other clinical signs exist and can vary between TSEs. PrPRES is incredibly resistant to inactivation and can withstand radiation, formalin treatment, and autoclaving to name a few tried decontamination methods whereas PrPC is degraded normally. This difference in degradation allows for differentiation between the two protein forms as PrPRES is resistant to degradation by Proteinase K. In the early 1980s this abnormal protein was discovered to be the sole causative agent of the various TSEs which at the time was a novel finding and a novel method of disease transmission. It is thought that slightly misfolded forms of PrPC occur which can then misfold further eventually forming PrPRES. PrPRES then has the ability to act as a template for conversion, converting PrPC. Numerous TSEs exist that affect both humans and a variety of animals. One of the animal TSEs is Chronic Wasting Disease (CWD) which affects cervids such as elk, deer, and moose (Cervus candensis, Odocoileus hemionus, Alces alces) and has become endemic in both free-ranging and captive herds. The exact mechanisms behind spread of CWD are unknown but research has shown that environmental reservoirs play a role in transmission dynamics. We chose to explore whether PrPRES can be detected on or inside grasses and plants naturally exposed to prions in CWD endemic areas by use of Protein Misfolding Cyclic Amplification (PMCA). Here we present novel environmental evidence showing that PrPRES can be found on the surface of multiple plants from Rocky Mountain National Park and mice inoculated with these samples are ... Text Alces alces Digital Collections of Colorado (Colorado State University) |
institution |
Open Polar |
collection |
Digital Collections of Colorado (Colorado State University) |
op_collection_id |
ftcolostateunidc |
language |
English |
description |
2016 Summer. Includes bibliographical references. Transmissible Spongiform Encephalopathies (TSEs) are a group of diseases caused by an abnormal version, PrPRES, of the normal cellular host protein prion protein (Prnp) termed PrPC. Disease is fatal resulting in amyloid deposits and spongiform degeneration in the brain in most but not all cases. Clinical signs can include wasting, increases in salivation, and general motor impairment but many other clinical signs exist and can vary between TSEs. PrPRES is incredibly resistant to inactivation and can withstand radiation, formalin treatment, and autoclaving to name a few tried decontamination methods whereas PrPC is degraded normally. This difference in degradation allows for differentiation between the two protein forms as PrPRES is resistant to degradation by Proteinase K. In the early 1980s this abnormal protein was discovered to be the sole causative agent of the various TSEs which at the time was a novel finding and a novel method of disease transmission. It is thought that slightly misfolded forms of PrPC occur which can then misfold further eventually forming PrPRES. PrPRES then has the ability to act as a template for conversion, converting PrPC. Numerous TSEs exist that affect both humans and a variety of animals. One of the animal TSEs is Chronic Wasting Disease (CWD) which affects cervids such as elk, deer, and moose (Cervus candensis, Odocoileus hemionus, Alces alces) and has become endemic in both free-ranging and captive herds. The exact mechanisms behind spread of CWD are unknown but research has shown that environmental reservoirs play a role in transmission dynamics. We chose to explore whether PrPRES can be detected on or inside grasses and plants naturally exposed to prions in CWD endemic areas by use of Protein Misfolding Cyclic Amplification (PMCA). Here we present novel environmental evidence showing that PrPRES can be found on the surface of multiple plants from Rocky Mountain National Park and mice inoculated with these samples are ... |
author2 |
Zabel, Mark Mathiason, Candace Leach, Jan Wilusz, Jeffrey |
format |
Text |
author |
Ortega, Aimee Elise |
spellingShingle |
Ortega, Aimee Elise Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin |
author_facet |
Ortega, Aimee Elise |
author_sort |
Ortega, Aimee Elise |
title |
Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin |
title_short |
Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin |
title_full |
Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin |
title_fullStr |
Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin |
title_full_unstemmed |
Metabolic engineering of the cyanobacterium Synechocystis sp. PCC 6803 for the production of astaxanthin |
title_sort |
metabolic engineering of the cyanobacterium synechocystis sp. pcc 6803 for the production of astaxanthin |
publisher |
Colorado State University. Libraries |
publishDate |
2016 |
url |
http://hdl.handle.net/10217/176603 |
genre |
Alces alces |
genre_facet |
Alces alces |
op_relation |
2000-2019 - CSU Theses and Dissertations Ortega_colostate_0053N_13631.pdf http://hdl.handle.net/10217/176603 |
op_rights |
Copyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright. |
_version_ |
1768378495701876736 |