Evolution of Phage Tail Sheath Protein
Sheath proteins comprise a part of the contractile molecular machinery present in bacteriophages with myoviral morphology, contractile injection systems, and the type VI secretion system (T6SS) found in many Gram-negative bacteria. Previous research on sheath proteins has demonstrated that they shar...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-05-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/14/6/1148 |
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| author | Peter Evseev Mikhail Shneider Konstantin Miroshnikov |
| author_facet | Peter Evseev Mikhail Shneider Konstantin Miroshnikov |
| author_sort | Peter Evseev |
| collection | DOAJ |
| description | Sheath proteins comprise a part of the contractile molecular machinery present in bacteriophages with myoviral morphology, contractile injection systems, and the type VI secretion system (T6SS) found in many Gram-negative bacteria. Previous research on sheath proteins has demonstrated that they share common structural features, even though they vary in their size and primary sequence. In this study, 112 contractile phage tail sheath proteins (TShP) representing different groups of bacteriophages and archaeal viruses with myoviral morphology have been modelled with the novel machine learning software, AlphaFold 2. The obtained structures have been analysed and conserved and variable protein parts and domains have been identified. The common core domain of all studied sheath proteins, including viral and T6SS proteins, comprised both N-terminal and C-terminal parts, whereas the other parts consisted of one or several moderately conserved domains, presumably added during phage evolution. The conserved core appears to be responsible for interaction with the tail tube protein and assembly of the phage tail. Additional domains may have evolved to maintain the stability of the virion or for adsorption to the host cell. Evolutionary relations between TShPs representing distinct viral groups have been proposed using a phylogenetic analysis based on overall structural similarity and other analyses. |
| first_indexed | 2024-03-09T22:15:46Z |
| format | Article |
| id | doaj.art-e8e50f504c814c00b65600c201a4bd81 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-09T22:15:46Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-e8e50f504c814c00b65600c201a4bd812023-11-23T19:24:24ZengMDPI AGViruses1999-49152022-05-01146114810.3390/v14061148Evolution of Phage Tail Sheath ProteinPeter Evseev0Mikhail Shneider1Konstantin Miroshnikov2Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, RussiaSheath proteins comprise a part of the contractile molecular machinery present in bacteriophages with myoviral morphology, contractile injection systems, and the type VI secretion system (T6SS) found in many Gram-negative bacteria. Previous research on sheath proteins has demonstrated that they share common structural features, even though they vary in their size and primary sequence. In this study, 112 contractile phage tail sheath proteins (TShP) representing different groups of bacteriophages and archaeal viruses with myoviral morphology have been modelled with the novel machine learning software, AlphaFold 2. The obtained structures have been analysed and conserved and variable protein parts and domains have been identified. The common core domain of all studied sheath proteins, including viral and T6SS proteins, comprised both N-terminal and C-terminal parts, whereas the other parts consisted of one or several moderately conserved domains, presumably added during phage evolution. The conserved core appears to be responsible for interaction with the tail tube protein and assembly of the phage tail. Additional domains may have evolved to maintain the stability of the virion or for adsorption to the host cell. Evolutionary relations between TShPs representing distinct viral groups have been proposed using a phylogenetic analysis based on overall structural similarity and other analyses.https://www.mdpi.com/1999-4915/14/6/1148sheath proteintail contractionphage tail assembly |
| spellingShingle | Peter Evseev Mikhail Shneider Konstantin Miroshnikov Evolution of Phage Tail Sheath Protein Viruses sheath protein tail contraction phage tail assembly |
| title | Evolution of Phage Tail Sheath Protein |
| title_full | Evolution of Phage Tail Sheath Protein |
| title_fullStr | Evolution of Phage Tail Sheath Protein |
| title_full_unstemmed | Evolution of Phage Tail Sheath Protein |
| title_short | Evolution of Phage Tail Sheath Protein |
| title_sort | evolution of phage tail sheath protein |
| topic | sheath protein tail contraction phage tail assembly |
| url | https://www.mdpi.com/1999-4915/14/6/1148 |
| work_keys_str_mv | AT peterevseev evolutionofphagetailsheathprotein AT mikhailshneider evolutionofphagetailsheathprotein AT konstantinmiroshnikov evolutionofphagetailsheathprotein |