Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages
Bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein, Hoc. The Hoc molecule (40 kDa) is present at the centre of each hexameric capsomer and provides a good platform for surface display of pathogen antigens. Biochemical and modelling studies show that Hoc consis...
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Veröffentlicht in: | Molecular microbiology 2010-07, Vol.77 (2), p.444-455 |
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description | Bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein, Hoc. The Hoc molecule (40 kDa) is present at the centre of each hexameric capsomer and provides a good platform for surface display of pathogen antigens. Biochemical and modelling studies show that Hoc consists of a string of four domains, three immunoglobulin (Ig)-like and one non-Ig domain at the C-terminus. Biochemical data suggest that the Hoc protein has two functional modules, a capsid binding module containing domains 1 and 4 and a solvent-exposed module containing domains 2 and 3. This model is consistent with the dumbbell-shaped cryo-EM density of Hoc observed in the reconstruction of the T4 capsid. Mutagenesis localized the capsid binding site to the C-terminal 25 amino acids, which are predicted to form two β-strands flanking a capsid binding loop. Mutations in the loop residues, ESRNG, abolished capsid binding, suggesting that these residues might interact with the major capsid protein, gp23*. With the conserved capsid binding module forming a foothold on the virus and the solvent-exposed module able to adapt to bind to a variety of surfaces, Hoc probably provides survival advantages to the phage, such as increasing the virus concentration near the host, efficient dispersion of the virus and exposing the tail for more efficient contact with the host cell surface prior to infection. |
doi_str_mv | 10.1111/j.1365-2958.2010.07219.x |
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The Hoc molecule (40 kDa) is present at the centre of each hexameric capsomer and provides a good platform for surface display of pathogen antigens. Biochemical and modelling studies show that Hoc consists of a string of four domains, three immunoglobulin (Ig)-like and one non-Ig domain at the C-terminus. Biochemical data suggest that the Hoc protein has two functional modules, a capsid binding module containing domains 1 and 4 and a solvent-exposed module containing domains 2 and 3. This model is consistent with the dumbbell-shaped cryo-EM density of Hoc observed in the reconstruction of the T4 capsid. Mutagenesis localized the capsid binding site to the C-terminal 25 amino acids, which are predicted to form two β-strands flanking a capsid binding loop. Mutations in the loop residues, ESRNG, abolished capsid binding, suggesting that these residues might interact with the major capsid protein, gp23*. With the conserved capsid binding module forming a foothold on the virus and the solvent-exposed module able to adapt to bind to a variety of surfaces, Hoc probably provides survival advantages to the phage, such as increasing the virus concentration near the host, efficient dispersion of the virus and exposing the tail for more efficient contact with the host cell surface prior to infection.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2010.07219.x</identifier><identifier>PMID: 20497329</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Antigens ; Bacteria ; Bacteriophage T4 - chemistry ; Bacteriophage T4 - immunology ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Capsid Proteins - chemistry ; Capsid Proteins - immunology ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Miscellaneous ; Models, Molecular ; Molecular Sequence Data ; Molecular structure ; Molecules ; Mutation ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Proteins ; Sequence Alignment ; Virology ; Viruses</subject><ispartof>Molecular microbiology, 2010-07, Vol.77 (2), p.444-455</ispartof><rights>2010 Blackwell Publishing Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Ltd. 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The Hoc molecule (40 kDa) is present at the centre of each hexameric capsomer and provides a good platform for surface display of pathogen antigens. Biochemical and modelling studies show that Hoc consists of a string of four domains, three immunoglobulin (Ig)-like and one non-Ig domain at the C-terminus. Biochemical data suggest that the Hoc protein has two functional modules, a capsid binding module containing domains 1 and 4 and a solvent-exposed module containing domains 2 and 3. This model is consistent with the dumbbell-shaped cryo-EM density of Hoc observed in the reconstruction of the T4 capsid. Mutagenesis localized the capsid binding site to the C-terminal 25 amino acids, which are predicted to form two β-strands flanking a capsid binding loop. Mutations in the loop residues, ESRNG, abolished capsid binding, suggesting that these residues might interact with the major capsid protein, gp23*. With the conserved capsid binding module forming a foothold on the virus and the solvent-exposed module able to adapt to bind to a variety of surfaces, Hoc probably provides survival advantages to the phage, such as increasing the virus concentration near the host, efficient dispersion of the virus and exposing the tail for more efficient contact with the host cell surface prior to infection.</description><subject>Amino Acid Sequence</subject><subject>Antigens</subject><subject>Bacteria</subject><subject>Bacteriophage T4 - chemistry</subject><subject>Bacteriophage T4 - immunology</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Capsid Proteins - chemistry</subject><subject>Capsid Proteins - immunology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>Mutation</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Virology</subject><subject>Viruses</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkk1v1DAQhiMEokvhL4CFhLg0i7_i2AeQUEVppVY90ErcrInj7HrJxsFOSvfAf8fpbhfKBXwYWzPPvDPWTJYhgucknXerOWGiyKkq5Jzi5MUlJWp--yib7QOPsxlWBc6ZpF8PsmcxrjAmDAv2NDugmKuSUTXLfp6MnRmc76BFkMwmuoh8g4alRUu3WLab5B7cwnbOID8ONiADfXQ16oMfrOuO0Kk3RwjQjQtjRLU1PsAkeA-gJvg1uuJ5675ZVIFJGs73S1jY-Dx70kAb7YvdfZhdn3y6Oj7Nzy8_nx1_PM-NIFLlJeE1KE5sKStRKCAS49IIyUtpbFkLVlUNIQ21AHXNVaUEpxwkbzCxjaSYHWYftrr9WK1tbWw3BGh1H9wawkZ7cPphpHNLvfA3miqsWMGTwNudQPDfRxsHvXbR2LaFzvox6rLgBRMsmX-SvCixFJgl8vVf5MqPIc0gaoGVEozcFZZbyAQfY7DNvmmC9bQLeqWnketp5HraBX23C_o2pb7889P7xPvhJ-DNDoBooG0CdMbF3xxVkrOCJO79lvvhWrv57wb0xcXZ9Er5r7b5DXgNi5BqXH-h0zISKZgqGPsFlSXaTg</recordid><startdate>201007</startdate><enddate>201007</enddate><creator>Sathaliyawala, Taheri</creator><creator>Islam, Mohammad Z</creator><creator>Li, Qin</creator><creator>Fokine, Andrei</creator><creator>Rossmann, Michael G</creator><creator>Rao, Venigalla B</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>5PM</scope></search><sort><creationdate>201007</creationdate><title>Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages</title><author>Sathaliyawala, Taheri ; Islam, Mohammad Z ; Li, Qin ; Fokine, Andrei ; Rossmann, Michael G ; Rao, Venigalla B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6189-714da941e78b659a18007c68478ce7d63bbf11f2eaadd49b96424a84f01ef8203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Antigens</topic><topic>Bacteria</topic><topic>Bacteriophage T4 - chemistry</topic><topic>Bacteriophage T4 - immunology</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Capsid Proteins - chemistry</topic><topic>Capsid Proteins - immunology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular structure</topic><topic>Molecules</topic><topic>Mutation</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sathaliyawala, Taheri</creatorcontrib><creatorcontrib>Islam, Mohammad Z</creatorcontrib><creatorcontrib>Li, Qin</creatorcontrib><creatorcontrib>Fokine, Andrei</creatorcontrib><creatorcontrib>Rossmann, Michael G</creatorcontrib><creatorcontrib>Rao, Venigalla B</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>PubMed Central (Full Participant titles)</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sathaliyawala, Taheri</au><au>Islam, Mohammad Z</au><au>Li, Qin</au><au>Fokine, Andrei</au><au>Rossmann, Michael G</au><au>Rao, Venigalla B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2010-07</date><risdate>2010</risdate><volume>77</volume><issue>2</issue><spage>444</spage><epage>455</epage><pages>444-455</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein, Hoc. The Hoc molecule (40 kDa) is present at the centre of each hexameric capsomer and provides a good platform for surface display of pathogen antigens. Biochemical and modelling studies show that Hoc consists of a string of four domains, three immunoglobulin (Ig)-like and one non-Ig domain at the C-terminus. Biochemical data suggest that the Hoc protein has two functional modules, a capsid binding module containing domains 1 and 4 and a solvent-exposed module containing domains 2 and 3. This model is consistent with the dumbbell-shaped cryo-EM density of Hoc observed in the reconstruction of the T4 capsid. Mutagenesis localized the capsid binding site to the C-terminal 25 amino acids, which are predicted to form two β-strands flanking a capsid binding loop. Mutations in the loop residues, ESRNG, abolished capsid binding, suggesting that these residues might interact with the major capsid protein, gp23*. With the conserved capsid binding module forming a foothold on the virus and the solvent-exposed module able to adapt to bind to a variety of surfaces, Hoc probably provides survival advantages to the phage, such as increasing the virus concentration near the host, efficient dispersion of the virus and exposing the tail for more efficient contact with the host cell surface prior to infection.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>20497329</pmid><doi>10.1111/j.1365-2958.2010.07219.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Antigens Bacteria Bacteriophage T4 - chemistry Bacteriophage T4 - immunology Binding Sites Biochemistry Biological and medical sciences Capsid Proteins - chemistry Capsid Proteins - immunology Fundamental and applied biological sciences. Psychology Microbiology Miscellaneous Models, Molecular Molecular Sequence Data Molecular structure Molecules Mutation Protein Interaction Domains and Motifs Protein Structure, Tertiary Proteins Sequence Alignment Virology Viruses |
title | Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages |
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