Line 5: | Line 5: | ||
<html> | <html> | ||
<head> | <head> | ||
− | + | <!-- fonts below are also referred to as a redundancy in the css file --> | |
− | + | ||
− | + | ||
<link href="https://fonts.googleapis.com/css?family=Cabin" rel="stylesheet"> | <link href="https://fonts.googleapis.com/css?family=Cabin" rel="stylesheet"> | ||
<link href="https://fonts.googleapis.com/css?family=Lato" rel="stylesheet"> | <link href="https://fonts.googleapis.com/css?family=Lato" rel="stylesheet"> | ||
Line 15: | Line 13: | ||
</head> | </head> | ||
<body> | <body> | ||
+ | <br><br> | ||
+ | |||
+ | <h1>MODEL</h1> | ||
+ | <br><br> | ||
+ | |||
+ | <div class="oneText-Wrapper"> | ||
+ | <div class="oneText-Text"> | ||
+ | <p>While VLPs will be useful components of VINCEnT, we wanted to focus on development of a novel non-immunogenic PNC with RNA packaging capabilities. Such a tool could enable simpler transfection of mammalian cell lines for fellow iGEMers and other researchers. | ||
+ | To do this, we identified the Rattus norvegicus Arc protein as a candidate for modelling a minimal packaging protein. Arc is an activity-regulated cytoskeletal-associated protein that has recently been recognized as a repurposed Ty3/Gypsy retrotransposon. A bi-lobar domain within Arc has significant homology to Gag proteins, which are the major capsid proteins of many viruses including Human Immunodeficiency Virus type 1 (HIV-1), Rous-Sarcoma Virus (RSV), and Bovine Leukemia Virus (BLV). In response to synaptic activity in neurons, Arc proteins self-assemble via this Gag domain (similar to the related viral particles) to encapsulate Arc mRNA and shuttle it to neighbouring cells (Pastuzyn et al., 2018; Ashley et al., 2018). | ||
− | </ | + | To ensure we would not retain any native Arc functionality that might impact cellular activity, we designed a “minimal” Arc Gag protein based on homology with other known Gag domains. We used template-based structural predictions to model this minimal Arc Gag and its predicted assembly into higher-order structures. |
− | </ | + | </p> |
+ | </div> | ||
+ | </div> |
Revision as of 16:11, 13 October 2018
MODEL
While VLPs will be useful components of VINCEnT, we wanted to focus on development of a novel non-immunogenic PNC with RNA packaging capabilities. Such a tool could enable simpler transfection of mammalian cell lines for fellow iGEMers and other researchers. To do this, we identified the Rattus norvegicus Arc protein as a candidate for modelling a minimal packaging protein. Arc is an activity-regulated cytoskeletal-associated protein that has recently been recognized as a repurposed Ty3/Gypsy retrotransposon. A bi-lobar domain within Arc has significant homology to Gag proteins, which are the major capsid proteins of many viruses including Human Immunodeficiency Virus type 1 (HIV-1), Rous-Sarcoma Virus (RSV), and Bovine Leukemia Virus (BLV). In response to synaptic activity in neurons, Arc proteins self-assemble via this Gag domain (similar to the related viral particles) to encapsulate Arc mRNA and shuttle it to neighbouring cells (Pastuzyn et al., 2018; Ashley et al., 2018). To ensure we would not retain any native Arc functionality that might impact cellular activity, we designed a “minimal” Arc Gag protein based on homology with other known Gag domains. We used template-based structural predictions to model this minimal Arc Gag and its predicted assembly into higher-order structures.