Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/12/10/1163 |
| _version_ | 1797550937582075904 |
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| author | Corynne L. Dedeo Carolyn M. Teschke Andrei T. Alexandrescu |
| author_facet | Corynne L. Dedeo Carolyn M. Teschke Andrei T. Alexandrescu |
| author_sort | Corynne L. Dedeo |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T15:37:33Z |
| format | Article |
| id | doaj.art-7d7a2bfe8e574a3f9d17233909fd9ec6 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T15:37:33Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-7d7a2bfe8e574a3f9d17233909fd9ec62023-11-20T17:06:30ZengMDPI AGViruses1999-49152020-10-011210116310.3390/v12101163Keeping It Together: Structures, Functions, and Applications of Viral Decoration ProteinsCorynne L. Dedeo0Carolyn M. Teschke1Andrei T. Alexandrescu2Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Unit-3125. Storrs, CT 06029-3125, USADepartment of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Unit-3125. Storrs, CT 06029-3125, USADepartment of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Unit-3125. Storrs, CT 06029-3125, USADecoration 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.https://www.mdpi.com/1999-4915/12/10/1163structure-function relationshipsvirus surfacesbacteriophagehost-pathogen interactionsquasi-symmetryinnate immunity |
| spellingShingle | Corynne L. Dedeo Carolyn M. Teschke Andrei T. Alexandrescu Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins Viruses structure-function relationships virus surfaces bacteriophage host-pathogen interactions quasi-symmetry innate immunity |
| title | Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins |
| title_full | Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins |
| title_fullStr | Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins |
| title_full_unstemmed | Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins |
| title_short | Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins |
| title_sort | keeping it together structures functions and applications of viral decoration proteins |
| topic | structure-function relationships virus surfaces bacteriophage host-pathogen interactions quasi-symmetry innate immunity |
| url | https://www.mdpi.com/1999-4915/12/10/1163 |
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