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<p class="publishdate"><span property="dc:date" datatype="xsd:dateTime" content="2024-07-23T00:00:00-04:00" class="date-display-single">July 23, 2024</span></p><div class='syndicate'><h1>Developing treatments for prion diseases</h1><div class="callout callout-with-border"><h3>At a Glance</h3>
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<ul>
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<li>Researchers developed a novel method to turn off prion protein production in mice.</li>
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<li>The technique could lead to treatments for prion diseases such as mad cow disease.</li>
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</ul></div><div class="media-float-right"><div class="ds-1col file file-image file-image-jpeg view-mode-floated_media clearfix">
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<picture title="Colorized electron micrograph of prion protein fibrils.">
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<!--[if IE 9]><video style="display: none;"><![endif]-->
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-large/public/news-events/research-matters/2024/8656058266_94c1dafae3_o.jpg?itok=027_IYe1&timestamp=1721745694 1x" media="screen and (min-width: 960px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium/public/news-events/research-matters/2024/8656058266_94c1dafae3_o.jpg?itok=LIKzUQZs&timestamp=1721745694 1x" media="screen and (min-width: 800px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium-small/public/news-events/research-matters/2024/8656058266_94c1dafae3_o.jpg?itok=hkVSnj3I&timestamp=1721745694 1x" media="screen and (min-width: 600px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-small/public/news-events/research-matters/2024/8656058266_94c1dafae3_o.jpg?itok=vk54vReq&timestamp=1721745694 1x" media="screen and (min-width: 480px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-tiny/public/news-events/research-matters/2024/8656058266_94c1dafae3_o.jpg?itok=PUmkkaeN&timestamp=1721745694 1x" media="screen and (min-width: 0)" />
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<!--[if IE 9]></video><![endif]-->
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<img src="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium/public/news-events/research-matters/2024/8656058266_94c1dafae3_o.jpg?itok=LIKzUQZs&timestamp=1721745694" alt="Colorized electron micrograph of prion protein fibrils." title="Colorized electron micrograph of prion protein fibrils." />
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</picture><span class="caption">Purified prion protein fibrils.</span><span class="credit">NIAID</span></div>
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</div><p>When normal prion proteins misfold in the brain, they cause a chain reaction of prion protein misfolding. These form toxic clumps that kill brain cells and eventually lead to death. Prion diseases include Creutzfeldt-Jacob disease and familial fatal insomnia in people, mad cow disease in cattle, scrapie in sheep, and chronic wasting disease in deer, elk, and moose.</p>
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||
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||
<p>Prion misfolding can be spontaneous or the result of genetic changes. It can also result from infection with misfolded prion protein, such as from contact with infected animals.</p>
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||
<p>No treatments for prion diseases yet exist. But prion protein isn’t essential for survival. Previous research has shown that mice completely lacking the gene for prion protein resist infectious prions. And reducing prion protein in neurons after infection can halt and even reverse disease in mice with minimal side effects. This suggests that reducing prion protein levels in neurons is a potential strategy for treating prion diseases.</p>
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||
<p>One way to reduce prion protein levels is to turn off the gene coding for the prion protein. This can be done via a DNA modification called methylation. This is a type of epigenetic modification—one that affects how DNA is used without changing the genetic sequence itself. In a new NIH-funded study, a research team led by Drs. Sonia Vallabh at the Broad Institute and Jonathan Weissman at MIT and the Whitehead Institute developed an improved method to target the prion gene. Their results appeared in <em>Science </em>on June 28, 2024.</p>
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||
|
||
<p>Earlier, Weissman’s group had developed a genetic tool for turning genes off in cultured cells. The tool, called CRISPRoff, combined the Cas9 protein from CRISPR gene editing technology, which guides the tool to a target gene, with an enzyme that methylates DNA. But CRISPRoff is not well-suited to therapeutic use. CRISPRoff is too big to fit into the harmless virus, called adeno-associated virus (AAV), that’s typically used to deliver gene therapies into the brain.</p>
|
||
|
||
<p>To design a system for therapies, the team replaced Cas9 with a zinc finger protein. Like Cas9, zinc finger proteins can be designed to target specific DNA sequences. But zinc finger proteins are much smaller than Cas9. They also occur naturally in human cells and so are less likely to trigger an immune response.</p>
|
||
|
||
<p>The next challenge the team faced is that too much of the DNA-methylating enzyme can be toxic to cells. So they designed the tool to recruit and activate a DNA-methylating enzyme already found in cells, instead of bringing in an outside enzyme. They called the new tool Coupled Histone tail for Autoinhibition Release of Methyltransferase (CHARM).</p>
|
||
|
||
<p>When the team injected mice with AAV carrying CHARM, the prion protein gene was turned off throughout the mouse brains. Prion protein levels decreased by up to 80% after six weeks. This is much more than earlier studies found was needed for a therapeutic effect. To further reduce the chance of side effects, the team modified CHARM so that it would turn itself off after turning off the prion protein gene.</p>
|
||
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||
<p>The results suggest that CHARM can safely suppress prion protein levels in brain cells. It thus could form the basis for potential prion disease treatments. Other neurodegenerative diseases, such as Huntington’s, are also caused by a buildup of toxic misfolded proteins. CHARM might help with treating these diseases as well.</p>
|
||
|
||
<p>“CHARMs are an elegant solution to the problem of silencing disease genes,” Weissman says, “and they have the potential to have an important position in the future of genetic medicines.”</p>
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<p>—by Brian Doctrow, Ph.D.</p></div><h2 class="label-above">Related Links</h2><ul class="spaced print-urls"><li><a href="https://www.nih.gov/news-events/nih-research-matters/gene-therapy-chronic-pain-relief" target="_top">Gene Therapy for Chronic Pain Relief</a></li><li><a href="https://www.nih.gov/news-events/nih-research-matters/detecting-prions-eyes" target="_top">Detecting Prions in Eyes</a></li><li><a href="https://www.nih.gov/news-events/nih-research-matters/prions-found-skin-people-creutzfeldt-jakob-disease" target="_top">Prions Found in Skin of People with Creutzfeldt-Jakob Disease</a></li><li><a href="https://www.nih.gov/news-events/nih-research-matters/treatment-shows-promise-models-fatal-neurological-disorders" target="_top">Treatment Shows Promise in Models of Fatal Neurological Disorders</a></li><li><a href="https://www.nih.gov/news-events/nih-research-matters/new-method-accurately-detects-prions-blood" target="_top">New Method Accurately Detects Prions in Blood</a></li><li><a href="https://www.niaid.nih.gov/diseases-conditions/prion-diseases" target="_top">Prion Diseases</a></li><li><a href="https://www.niehs.nih.gov/health/topics/science/epigenetics" target="_top">Epigenetics</a></li><li><a href="https://www.cdc.gov/prions/about/index.html" target="_top">About Prion Diseases (CDC)</a></li></ul><p class="footnote"><strong class="label-inline">References: </strong><a href="https://pubmed.ncbi.nlm.nih.gov/38935715/">Brainwide silencing of prion protein by AAV-mediated delivery of an engineered compact epigenetic editor.</a> Neumann EN, Bertozzi TM, Wu E, Serack F, Harvey JW, Brauer PP, Pirtle CP, Coffey A, Howard M, Kamath N, Lenz K, Guzman K, Raymond MH, Khalil AS, Deverman BE, Minikel EV, Vallabh SM, Weissman JS. <em>Science</em>. 2024 Jun 28;384(6703):ado7082. doi: 10.1126/science.ado7082. Epub 2024 Jun 28. PMID: 38935715.</p><p class="footnote"><strong class="label-inline">Funding: </strong>NIH’s National Institute of Neurological Disorders and Stroke (NINDS), Office of the Director (OD) Office of Strategic Coordination’s Somatic Cell Genome Editing Program, National Human Genome Research Institute (NHGRI), and National Institute of Biomedical Imaging and Bioengineering (NIBIB); Jane Coffin Childs Memorial Fund for Medical Research; United States Department of Defense; Schmidt Sciences; Howard Hughes Medical Institute.</p>
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