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Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses
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Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins

Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Unit-3125. Storrs, CT 06029-3125, USA
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Authors to whom correspondence should be addressed.
Viruses 2020, 12(10), 1163; https://doi.org/10.3390/v12101163
Received: 18 September 2020 / Revised: 9 October 2020 / Accepted: 11 October 2020 / Published: 14 October 2020
(This article belongs to the Special Issue In Memory of Michael Rossmann)
Decoration proteins are viral accessory gene products that adorn the surfaces of some phages and viral capsids, particularly tailed dsDNA phages. These proteins often play a “cementing” role, reinforcing capsids against accumulating internal pressure due to genome packaging, or environmental insults such as extremes of temperature or pH. Many decoration proteins serve alternative functions, including target cell recognition, participation in viral assembly, capsid size determination, or modulation of host gene expression. Examples that currently have structures characterized to high-resolution fall into five main folding motifs: β-tulip, β-tadpole, OB-fold, Ig-like, and a rare knotted α-helical fold. Most of these folding motifs have structure homologs in virus and target cell proteins, suggesting horizontal gene transfer was important in their evolution. Oligomerization states of decoration proteins range from monomers to trimers, with the latter most typical. Decoration proteins bind to a variety of loci on capsids that include icosahedral 2-, 3-, and 5-fold symmetry axes, as well as pseudo-symmetry sites. These binding sites often correspond to “weak points” on the capsid lattice. Because of their unique abilities to bind virus surfaces noncovalently, decoration proteins are increasingly exploited for technology, with uses including phage display, viral functionalization, vaccination, and improved nanoparticle design for imaging and drug delivery. These applications will undoubtedly benefit from further advances in our understanding of these versatile augmenters of viral functions. View Full-Text
Keywords: structure-function relationships; virus surfaces; bacteriophage; host-pathogen interactions; quasi-symmetry; innate immunity; biomimetics; nanomedicine structure-function relationships; virus surfaces; bacteriophage; host-pathogen interactions; quasi-symmetry; innate immunity; biomimetics; nanomedicine
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Dedeo, C.L.; Teschke, C.M.; Alexandrescu, A.T. Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins. Viruses 2020, 12, 1163.

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