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Title: Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like Bacteriophage

Abstract

The head of bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein (Hoc). One Hoc molecule binds near the center of each hexameric capsomer. Hoc is dispensable for capsid assembly and has been used to display pathogenic antigens on the surface of T4. Here we report the crystal structure of a protein containing the first three of four domains of Hoc from bacteriophage RB49, a close relative of T4. The structure shows an approximately linear arrangement of the protein domains. Each of these domains has an immunoglobulin-like fold, frequently found in cell attachment molecules. In addition, we report biochemical data suggesting that Hoc can bind to Escherichia coli, supporting the hypothesis that Hoc could attach the phage capsids to bacterial surfaces and perhaps also to other organisms. The capacity for such reversible adhesion probably provides survival advantages to the bacteriophage.

Authors:
; ; ; ; ;  [1];  [2]
  1. (CUA)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NSFNIH
OSTI Identifier:
1021776
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Virol.; Journal Volume: 85; Journal Issue: (16) ; 08, 2011
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ADHESION; ANTIGENS; BACTERIOPHAGES; CAPACITY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; HYPOTHESIS; IMMUNOGLOBULINS; PROTEINS

Citation Formats

Fokine, Andrei, Islam, Mohammad Z., Zhang, Zhihong, Bowman, Valorie D., Rao, Venigalla B., Rossmann, Michael G., and Purdue). Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like Bacteriophage. United States: N. p., 2011. Web. doi:10.1128/JVI.00847-11.
Fokine, Andrei, Islam, Mohammad Z., Zhang, Zhihong, Bowman, Valorie D., Rao, Venigalla B., Rossmann, Michael G., & Purdue). Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like Bacteriophage. United States. doi:10.1128/JVI.00847-11.
Fokine, Andrei, Islam, Mohammad Z., Zhang, Zhihong, Bowman, Valorie D., Rao, Venigalla B., Rossmann, Michael G., and Purdue). Fri . "Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like Bacteriophage". United States. doi:10.1128/JVI.00847-11.
@article{osti_1021776,
title = {Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like Bacteriophage},
author = {Fokine, Andrei and Islam, Mohammad Z. and Zhang, Zhihong and Bowman, Valorie D. and Rao, Venigalla B. and Rossmann, Michael G. and Purdue)},
abstractNote = {The head of bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein (Hoc). One Hoc molecule binds near the center of each hexameric capsomer. Hoc is dispensable for capsid assembly and has been used to display pathogenic antigens on the surface of T4. Here we report the crystal structure of a protein containing the first three of four domains of Hoc from bacteriophage RB49, a close relative of T4. The structure shows an approximately linear arrangement of the protein domains. Each of these domains has an immunoglobulin-like fold, frequently found in cell attachment molecules. In addition, we report biochemical data suggesting that Hoc can bind to Escherichia coli, supporting the hypothesis that Hoc could attach the phage capsids to bacterial surfaces and perhaps also to other organisms. The capacity for such reversible adhesion probably provides survival advantages to the bacteriophage.},
doi = {10.1128/JVI.00847-11},
journal = {J. Virol.},
number = (16) ; 08, 2011,
volume = 85,
place = {United States},
year = {Fri Sep 16 00:00:00 EDT 2011},
month = {Fri Sep 16 00:00:00 EDT 2011}
}