Identification of structural and morphogenesis genes of Pseudoalteromonas phage φRIO-1 and placement within the evolutionary history of Podoviridae
Abstract The virion proteins of Pseudoalteromonas phage φRIO-1 were identified and quantitated by mass spectrometry and gel densitometry. Bioinformatic methods customized to deal with extreme divergence defined a φRIO-1 tail structure homology group of phages, which was further related to T7 tail an...
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description | Abstract The virion proteins of Pseudoalteromonas phage φRIO-1 were identified and quantitated by mass spectrometry and gel densitometry. Bioinformatic methods customized to deal with extreme divergence defined a φRIO-1 tail structure homology group of phages, which was further related to T7 tail and internal virion proteins (IVPs). Similarly, homologs of tubular tail components and internal virion proteins were identified in essentially all completely sequenced podoviruses other than those in the subfamily Picovirinae. The podoviruses were subdivided into several tail structure homology groups, in addition to the RIO-1 and T7 groups. Molecular phylogeny indicated that these groups all arose about the same ancient time as the φRIO-1/T7 split. Hence, the T7-like infection mechanism involving the IVPs was an ancestral property of most podoviruses. The IVPs were found to variably host both tail lysozyme domains and domains destined for the cytoplasm, including the N4 virion RNA polymerase embedded within an IVP-D homolog. |
doi_str_mv | 10.1016/j.virol.2015.12.005 |
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Bioinformatic methods customized to deal with extreme divergence defined a φRIO-1 tail structure homology group of phages, which was further related to T7 tail and internal virion proteins (IVPs). Similarly, homologs of tubular tail components and internal virion proteins were identified in essentially all completely sequenced podoviruses other than those in the subfamily Picovirinae. The podoviruses were subdivided into several tail structure homology groups, in addition to the RIO-1 and T7 groups. Molecular phylogeny indicated that these groups all arose about the same ancient time as the φRIO-1/T7 split. Hence, the T7-like infection mechanism involving the IVPs was an ancestral property of most podoviruses. The IVPs were found to variably host both tail lysozyme domains and domains destined for the cytoplasm, including the N4 virion RNA polymerase embedded within an IVP-D homolog.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2015.12.005</identifier><identifier>PMID: 26748333</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacteriophage ; Bacteriophages - classification ; Bacteriophages - genetics ; Bacteriophages - growth & development ; Bacteriophages - isolation & purification ; Evolution, Molecular ; Genome, Viral ; Infectious Disease ; Molecular Sequence Data ; Phylogeny ; Podoviridae ; Podoviridae - classification ; Podoviridae - genetics ; Podoviridae - growth & development ; Podoviridae - isolation & purification ; Podoviruses ; Pseudoalteromonas ; Pseudoalteromonas - virology ; Virion structure</subject><ispartof>Virology (New York, N.Y.), 2016-02, Vol.489, p.116-127</ispartof><rights>The Authors</rights><rights>2015 The Authors</rights><rights>Copyright © 2015 The Authors. 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Bioinformatic methods customized to deal with extreme divergence defined a φRIO-1 tail structure homology group of phages, which was further related to T7 tail and internal virion proteins (IVPs). Similarly, homologs of tubular tail components and internal virion proteins were identified in essentially all completely sequenced podoviruses other than those in the subfamily Picovirinae. The podoviruses were subdivided into several tail structure homology groups, in addition to the RIO-1 and T7 groups. Molecular phylogeny indicated that these groups all arose about the same ancient time as the φRIO-1/T7 split. Hence, the T7-like infection mechanism involving the IVPs was an ancestral property of most podoviruses. The IVPs were found to variably host both tail lysozyme domains and domains destined for the cytoplasm, including the N4 virion RNA polymerase embedded within an IVP-D homolog.</description><subject>Bacteriophage</subject><subject>Bacteriophages - classification</subject><subject>Bacteriophages - genetics</subject><subject>Bacteriophages - growth & development</subject><subject>Bacteriophages - isolation & purification</subject><subject>Evolution, Molecular</subject><subject>Genome, Viral</subject><subject>Infectious Disease</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Podoviridae</subject><subject>Podoviridae - classification</subject><subject>Podoviridae - genetics</subject><subject>Podoviridae - growth & development</subject><subject>Podoviridae - isolation & purification</subject><subject>Podoviruses</subject><subject>Pseudoalteromonas</subject><subject>Pseudoalteromonas - virology</subject><subject>Virion structure</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUs1u1DAYjBCIbgtPgIR85JLlc5zEyYFKqCplpUpF_Jwtr_1l4yWxF9tZ1BfgCXgvXglnt1TABU6fLM-MZzxflj2jsKRA65fb5d54NywLoNWSFkuA6kG2oNDWObCSPswWAGWR101RnGSnIWwhnTmHx9lJUfOyYYwtsu8rjTaazigZjbPEdSREP6k4eTkQaTUZnd_1boMWgwnkMGfUu4CTdnKI6N3orAxk18sNkh_f3q9ucnqg7gapcEz65KuJvbEk9khw74Zpfkv6W9KbEF2as6DTLgUyWuKT7FEnh4BP7-ZZ9unN5ceLt_n1zdXq4vV1rqqSx7wBBqqtS6mYqjtWsaYtypZVWjWoWr6mDaiSASiQreRadrKANa805bpmrQJ2lp0fdXfTekStktOUWuy8GZM54aQRf95Y04uN24uyoW3LqyTw4k7Auy8ThihGExQOg7TopiAob1MdZQnsP6A1B55y1QnKjlDlXQgeu3tHFMRcvdiKQ_Virl7QQqTqE-v572HuOb-6ToBXRwCmL90b9CIog1ahNh5VFNqZfzxw_hdfDcamxRk-4y2GrZu8TW0JKkIiiA_z9s3LR6vETi7YT4KK2mY</recordid><startdate>20160201</startdate><enddate>20160201</enddate><creator>Hardies, Stephen C</creator><creator>Thomas, Julie A</creator><creator>Black, Lindsay</creator><creator>Weintraub, Susan T</creator><creator>Hwang, Chung Y</creator><creator>Cho, Byung C</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QL</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20160201</creationdate><title>Identification of structural and morphogenesis genes of Pseudoalteromonas phage φRIO-1 and placement within the evolutionary history of Podoviridae</title><author>Hardies, Stephen C ; 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Bioinformatic methods customized to deal with extreme divergence defined a φRIO-1 tail structure homology group of phages, which was further related to T7 tail and internal virion proteins (IVPs). Similarly, homologs of tubular tail components and internal virion proteins were identified in essentially all completely sequenced podoviruses other than those in the subfamily Picovirinae. The podoviruses were subdivided into several tail structure homology groups, in addition to the RIO-1 and T7 groups. Molecular phylogeny indicated that these groups all arose about the same ancient time as the φRIO-1/T7 split. Hence, the T7-like infection mechanism involving the IVPs was an ancestral property of most podoviruses. 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subjects | Bacteriophage Bacteriophages - classification Bacteriophages - genetics Bacteriophages - growth & development Bacteriophages - isolation & purification Evolution, Molecular Genome, Viral Infectious Disease Molecular Sequence Data Phylogeny Podoviridae Podoviridae - classification Podoviridae - genetics Podoviridae - growth & development Podoviridae - isolation & purification Podoviruses Pseudoalteromonas Pseudoalteromonas - virology Virion structure |
title | Identification of structural and morphogenesis genes of Pseudoalteromonas phage φRIO-1 and placement within the evolutionary history of Podoviridae |
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