@phdthesis{105346,
  author = {Jolie Jean},
  title = {Construction and Characterization of a novel PRV recombinant expressing a C Terminal VP26-mCherry fusion protein},
  abstract = { Fluorescent protein-based methodologies have revolutionized the field of virology, allowing us to visualize the location and activity of pseudorabies virus (PRV) particles in vitro (G. A. Smith \&amp; Enquist, 2002). Several limitations, including brightness and stability have limited such tools for microscopy analysis (Hogue et al., 2015). While N terminal fusions of fluorescent proteins to capsid proteins like VP26 (pUL35) have been well utilized, little is known about the effectiveness of C Terminal fusions. Included in this study are the first recombinant PRV strains expressing C terminal VP26-mCherry. The properties of this reporter virus, PRV 1028, were compared to previously constructed N terminal recombinants containing either mRFP or mCherry. PRV 1028 had similar single-step replication kinetics compared to wild-type PRV Becker and traditional FP{\textendash} VP26 strains. Despite slightly reduced plaque diameter, we find that our newly synthesized PRV 1028 incorporates more fluorescent VP26 fusion proteins in progeny virus particles. As a result, PRV 1028 capsids have a higher fluorescent intensity in comparison to their N terminal counterparts. Based on these findings, our novel PRV recombinant will allow for optimized fluorescent-based methodologies.<br>http://arks.princeton.edu/ark:/88435/dsp019s161861k },
  year = {2016},
  journal = {Molecular Biology},
  language = {eng},
}