![]() This structure has allowed us to compare our findings with the structure of the human alphacoronavirus NL63 spike as well as another recently published PEDV spike structure ( Walls et al., 2016b Wrapp and McLellan, 2019). Here we used cryoelectron microscopy (cryo-EM) to determine the structure of the PEDV spike protein at 3.5 Å resolution. High-resolution structural studies of coronavirus spike proteins have the potential to shed light on the molecular mechanisms of spike prefusion stability, and the lessons learned can be utilized in the production of stabilized spike proteins as vaccine immunogens. However, the use of pAPN as a receptor for PEDV has been called into question ( Li et al., 2017b). By analogy with transmissible gastroenteritis virus, PEDV spikes were also proposed to recognize porcine aminopeptidase N (pAPN) ( Li et al., 2007). PEDV has been shown to bind to sialic acid glycans using its S1 domain 0 ( Li et al., 2016). Receptors include both host glycans and host proteins and vary widely between coronaviruses. Coronavirus S1 regions of the spike contain domains contributing to receptor binding. ![]() However, this site is lacking in many alphacoronavirus spikes, including PEDV. In betacoronavirus spikes, the S1 and S2 regions are often demarcated by a protease cleavage site ( Millet and Whittaker, 2015). However, a structural mapping of PEDV antibody epitopes targeted during viral infection is lacking.Ĭoronavirus spikes adopt a shared domain arrangement where the N-terminal S1 regions of the homotrimeric spike surround and cap the C-terminal S2 regions. These antibodies primarily target the PEDV S1 region and some epitopes have been found to be neutralizing ( Li et al., 2017a Okda et al., 2017 Sun et al., 2007). As the major surface glycoprotein on the enveloped virions, spikes are also the target of neutralizing antibodies ( Okda et al., 2017). For coronavirus spikes, this transition of conformations has been proposed to be triggered by progressive destabilization of the prefusion structure through receptor binding and host proteolytic cleavage ( Belouzard et al., 2009 Millet and Whittaker, 2015 Taguchi and Matsuyama, 2002). This class of proteins proceeds from a metastable prefusion conformation to a highly stable postfusion conformation ( Bullough et al., 1994). Coronavirus spikes are class I viral fusion proteins ( Bosch et al., 2003 Chambers et al., 1990), possessing structural and functional parallels to influenza hemagglutinin ( Wilson et al., 1981) and HIV-1 Env ( Julien et al., 2013 Lyumkis et al., 2013). Like all coronaviruses, PEDV possesses a spike glycoprotein (S) responsible for cell attachment and virus-host membrane fusion mediating viral entry into host cells. Although mortality due to PEDV infection is lower in older pigs, infection can still result in decreased growth performance. Mortality due to viral infection varies with age, with mortalities of 1–3 day old piglets in naive herds approaching 100% ( Lee, 2015). PEDV was first identified in the United States in 2013 ( Stevenson et al., 2013), and it swept through pig populations, causing several million piglet deaths ( Sawyer and Sherwell, 2014). Originally identified in England ( Wood, 1977), PEDV is now a global pathogen. Identified as a viral agent distinct from transmissible gastroenteritis virus ( Wood, 1977) and as a coronavirus ( Pensaert and de Bouck, 1978), this virus is responsible for an enteric infection in pigs. As a result, your scientists can switch entirely to SnapGene without losing data, or can continue using legacy software together with SnapGene without conflict.Īs a service to the research community, SnapGene provides tutorial videos along with a library of carefully annotated plasmids, along with guides to popular cloning methods.Porcine epidemic diarrhea virus (PEDV) is a coronavirus of the Alphacoronavirus genus. SnapGene supports a host of file formats.SnapGene automatically generates a record of every sequence edit and cloning procedure, so you won’t lose track of how a construct was made, even after a lab member leaves.dna files can be opened by the free cross-platform SnapGene Viewer, enabling you to share richly annotated maps and sequences with colleagues. Every DNA manipulation in SnapGene is automatically recorded, so you can see exactly what you did and retrieve the sequences of ancestral constructs.SnapGene makes your DNA manipulations easy to visualize and simulate, and alerts you to errors before they happen.The software also enables documentation and sharing of data. With an intuitive interface, the software enables DNA sequence visualization, sequence annotation, sequence editing, cloning, protein visualization, and simulating common cloning methods. ![]() SnapGene enables an easy and secure way to plan, visualize, and document everyday molecular biology procedures.
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