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
Hauptverfasser: Sathaliyawala, Taheri, Islam, Mohammad Z, Li, Qin, Fokine, Andrei, Rossmann, Michael G, Rao, Venigalla B
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container_issue 2
container_start_page 444
container_title Molecular microbiology
container_volume 77
creator Sathaliyawala, Taheri
Islam, Mohammad Z
Li, Qin
Fokine, Andrei
Rossmann, Michael G
Rao, Venigalla B
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.
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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.</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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