Loading…

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2012-08, Vol.109 (35), p.14001-14006
Main Authors: Aksyuk, Anastasia A, Bowman, Valorie D, Kaufmann, Bärbel, Fields, Christopher, Klose, Thomas, Holdaway, Heather A, Fischetti, Vincent A, Rossmann, Michael G
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033
cites cdi_FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033
container_end_page 14006
container_issue 35
container_start_page 14001
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 109
creator Aksyuk, Anastasia A
Bowman, Valorie D
Kaufmann, Bärbel
Fields, Christopher
Klose, Thomas
Holdaway, Heather A
Fischetti, Vincent A
Rossmann, Michael G
description The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.
doi_str_mv 10.1073/pnas.1207730109
format article
fullrecord <record><control><sourceid>jstor_pnas_</sourceid><recordid>TN_cdi_jstor_primary_41701632</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>41701632</jstor_id><sourcerecordid>41701632</sourcerecordid><originalsourceid>FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033</originalsourceid><addsrcrecordid>eNpdkc-P1CAcxYnRuOPo2ZNK4sWD3eULtJSLiZn4K9lEk3XPhFI6w6QtFegk-99Ld8ZZ9QKH93kPvt-H0Esgl0AEu5pGHS-BEiEYASIfoVU-oai4JI_RihAqippTfoGexbgnhMiyJk_RBaW1BCrLFZpuUphNmoPusRsPNia31cn5MWLfYY1_-NYfXHCttjimYKfkjTdmjnja6a3FG3iP3TD1zpxcnQ847SwerNnp0cVhyckJOd-OKdw9R0863Uf74nSv0e3nTz83X4vr71--bT5eF6YEmQroOG-rtpGdhIYAa5iQpO7AVFrLqjElBSHqBqADYF1DeQtl3ZRQt2VLKWFsjT4cc6e5GWxrlsd1r6bgBh3ulNdO_auMbqe2_qAYZzlG5oB3p4Dgf815MWpw0di-16P1c1RAmKCciXv07X_o3s9hzOPdU4zTqqozdXWkTPAxBtudPwNELW2qpU310GZ2vP57hjP_p74M4BOwOB_ipGKlAk7y4tbo1RHZx-TDmeEgCFSMZv3NUe-0V3obXFS3NzRr2UwlFzX7DTrhudg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1037342668</pqid></control><display><type>article</type><title>Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry</title><source>NCBI_PubMed Central(免费)</source><source>JSTOR Archival Journals and Primary Sources Collection</source><creator>Aksyuk, Anastasia A ; Bowman, Valorie D ; Kaufmann, Bärbel ; Fields, Christopher ; Klose, Thomas ; Holdaway, Heather A ; Fischetti, Vincent A ; Rossmann, Michael G</creator><creatorcontrib>Aksyuk, Anastasia A ; Bowman, Valorie D ; Kaufmann, Bärbel ; Fields, Christopher ; Klose, Thomas ; Holdaway, Heather A ; Fischetti, Vincent A ; Rossmann, Michael G</creatorcontrib><description>The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1207730109</identifier><identifier>PMID: 22891295</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Appendages ; Bacteria ; Bacteriophages ; Biological Sciences ; Capsid ; Capsid - chemistry ; Capsid - ultrastructure ; Capsid proteins ; Capsid Proteins - chemistry ; Cell walls ; Cells ; coat proteins ; cryo-electron microscopy ; Cryoelectron Microscopy ; Crystal structure ; Crystallography, X-Ray ; DNA ; genome ; Genomes ; Myoviridae ; Myoviridae - growth &amp; development ; Myoviridae - ultrastructure ; Podoviridae ; Podoviridae - growth &amp; development ; Podoviridae - ultrastructure ; Protein Structure, Tertiary ; Proteins ; sequence homology ; Siphoviridae ; Streptococcus ; Streptococcus - virology ; Streptococcus Phages - growth &amp; development ; Streptococcus Phages - ultrastructure ; structural proteins ; Viral Structural Proteins - chemistry ; Virus Replication - physiology ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-08, Vol.109 (35), p.14001-14006</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Aug 28, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033</citedby><cites>FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/35.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41701632$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41701632$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793,58238,58471</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22891295$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Aksyuk, Anastasia A</creatorcontrib><creatorcontrib>Bowman, Valorie D</creatorcontrib><creatorcontrib>Kaufmann, Bärbel</creatorcontrib><creatorcontrib>Fields, Christopher</creatorcontrib><creatorcontrib>Klose, Thomas</creatorcontrib><creatorcontrib>Holdaway, Heather A</creatorcontrib><creatorcontrib>Fischetti, Vincent A</creatorcontrib><creatorcontrib>Rossmann, Michael G</creatorcontrib><title>Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.</description><subject>Appendages</subject><subject>Bacteria</subject><subject>Bacteriophages</subject><subject>Biological Sciences</subject><subject>Capsid</subject><subject>Capsid - chemistry</subject><subject>Capsid - ultrastructure</subject><subject>Capsid proteins</subject><subject>Capsid Proteins - chemistry</subject><subject>Cell walls</subject><subject>Cells</subject><subject>coat proteins</subject><subject>cryo-electron microscopy</subject><subject>Cryoelectron Microscopy</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>genome</subject><subject>Genomes</subject><subject>Myoviridae</subject><subject>Myoviridae - growth &amp; development</subject><subject>Myoviridae - ultrastructure</subject><subject>Podoviridae</subject><subject>Podoviridae - growth &amp; development</subject><subject>Podoviridae - ultrastructure</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>sequence homology</subject><subject>Siphoviridae</subject><subject>Streptococcus</subject><subject>Streptococcus - virology</subject><subject>Streptococcus Phages - growth &amp; development</subject><subject>Streptococcus Phages - ultrastructure</subject><subject>structural proteins</subject><subject>Viral Structural Proteins - chemistry</subject><subject>Virus Replication - physiology</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNpdkc-P1CAcxYnRuOPo2ZNK4sWD3eULtJSLiZn4K9lEk3XPhFI6w6QtFegk-99Ld8ZZ9QKH93kPvt-H0Esgl0AEu5pGHS-BEiEYASIfoVU-oai4JI_RihAqippTfoGexbgnhMiyJk_RBaW1BCrLFZpuUphNmoPusRsPNia31cn5MWLfYY1_-NYfXHCttjimYKfkjTdmjnja6a3FG3iP3TD1zpxcnQ847SwerNnp0cVhyckJOd-OKdw9R0863Uf74nSv0e3nTz83X4vr71--bT5eF6YEmQroOG-rtpGdhIYAa5iQpO7AVFrLqjElBSHqBqADYF1DeQtl3ZRQt2VLKWFsjT4cc6e5GWxrlsd1r6bgBh3ulNdO_auMbqe2_qAYZzlG5oB3p4Dgf815MWpw0di-16P1c1RAmKCciXv07X_o3s9hzOPdU4zTqqozdXWkTPAxBtudPwNELW2qpU310GZ2vP57hjP_p74M4BOwOB_ipGKlAk7y4tbo1RHZx-TDmeEgCFSMZv3NUe-0V3obXFS3NzRr2UwlFzX7DTrhudg</recordid><startdate>20120828</startdate><enddate>20120828</enddate><creator>Aksyuk, Anastasia A</creator><creator>Bowman, Valorie D</creator><creator>Kaufmann, Bärbel</creator><creator>Fields, Christopher</creator><creator>Klose, Thomas</creator><creator>Holdaway, Heather A</creator><creator>Fischetti, Vincent A</creator><creator>Rossmann, Michael G</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120828</creationdate><title>Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry</title><author>Aksyuk, Anastasia A ; Bowman, Valorie D ; Kaufmann, Bärbel ; Fields, Christopher ; Klose, Thomas ; Holdaway, Heather A ; Fischetti, Vincent A ; Rossmann, Michael G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Appendages</topic><topic>Bacteria</topic><topic>Bacteriophages</topic><topic>Biological Sciences</topic><topic>Capsid</topic><topic>Capsid - chemistry</topic><topic>Capsid - ultrastructure</topic><topic>Capsid proteins</topic><topic>Capsid Proteins - chemistry</topic><topic>Cell walls</topic><topic>Cells</topic><topic>coat proteins</topic><topic>cryo-electron microscopy</topic><topic>Cryoelectron Microscopy</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>DNA</topic><topic>genome</topic><topic>Genomes</topic><topic>Myoviridae</topic><topic>Myoviridae - growth &amp; development</topic><topic>Myoviridae - ultrastructure</topic><topic>Podoviridae</topic><topic>Podoviridae - growth &amp; development</topic><topic>Podoviridae - ultrastructure</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>sequence homology</topic><topic>Siphoviridae</topic><topic>Streptococcus</topic><topic>Streptococcus - virology</topic><topic>Streptococcus Phages - growth &amp; development</topic><topic>Streptococcus Phages - ultrastructure</topic><topic>structural proteins</topic><topic>Viral Structural Proteins - chemistry</topic><topic>Virus Replication - physiology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aksyuk, Anastasia A</creatorcontrib><creatorcontrib>Bowman, Valorie D</creatorcontrib><creatorcontrib>Kaufmann, Bärbel</creatorcontrib><creatorcontrib>Fields, Christopher</creatorcontrib><creatorcontrib>Klose, Thomas</creatorcontrib><creatorcontrib>Holdaway, Heather A</creatorcontrib><creatorcontrib>Fischetti, Vincent A</creatorcontrib><creatorcontrib>Rossmann, Michael G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aksyuk, Anastasia A</au><au>Bowman, Valorie D</au><au>Kaufmann, Bärbel</au><au>Fields, Christopher</au><au>Klose, Thomas</au><au>Holdaway, Heather A</au><au>Fischetti, Vincent A</au><au>Rossmann, Michael G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-08-28</date><risdate>2012</risdate><volume>109</volume><issue>35</issue><spage>14001</spage><epage>14006</epage><pages>14001-14006</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a φ 29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22891295</pmid><doi>10.1073/pnas.1207730109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 2012-08, Vol.109 (35), p.14001-14006
issn 0027-8424
1091-6490
language eng
recordid cdi_jstor_primary_41701632
source NCBI_PubMed Central(免费); JSTOR Archival Journals and Primary Sources Collection
subjects Appendages
Bacteria
Bacteriophages
Biological Sciences
Capsid
Capsid - chemistry
Capsid - ultrastructure
Capsid proteins
Capsid Proteins - chemistry
Cell walls
Cells
coat proteins
cryo-electron microscopy
Cryoelectron Microscopy
Crystal structure
Crystallography, X-Ray
DNA
genome
Genomes
Myoviridae
Myoviridae - growth & development
Myoviridae - ultrastructure
Podoviridae
Podoviridae - growth & development
Podoviridae - ultrastructure
Protein Structure, Tertiary
Proteins
sequence homology
Siphoviridae
Streptococcus
Streptococcus - virology
Streptococcus Phages - growth & development
Streptococcus Phages - ultrastructure
structural proteins
Viral Structural Proteins - chemistry
Virus Replication - physiology
Viruses
title Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T12%3A47%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pnas_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20investigations%20of%20a%20Podoviridae%20streptococcus%20phage%20C1,%20implications%20for%20the%20mechanism%20of%20viral%20entry&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Aksyuk,%20Anastasia%20A&rft.date=2012-08-28&rft.volume=109&rft.issue=35&rft.spage=14001&rft.epage=14006&rft.pages=14001-14006&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.1207730109&rft_dat=%3Cjstor_pnas_%3E41701632%3C/jstor_pnas_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c519t-1f44d6db9f91b013b37908f1c6aa96bc521778b11f113fb24d158b518d5d22033%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1037342668&rft_id=info:pmid/22891295&rft_jstor_id=41701632&rfr_iscdi=true