Structural highlights
Publication Abstract from PubMed
The head of bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein or 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 T4 surface. Here we report the crystal structure of a protein containing the first three of four domains of Hoc from the 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 E. coli supporting the hypothesis that Hoc could attach the phage capsids to bacterial surfaces and maybe also to other organisms. The ability of such reversible adhesion probably provides survival advantages to the bacteriophage.
Structure of the Three N-terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-like Bacteriophage.,Fokine A, Islam MZ, Zhang Z, Bowman VD, Rao VB, Rossmann MG J Virol. 2011 Jun 1. PMID:21632759[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fokine A, Islam MZ, Zhang Z, Bowman VD, Rao VB, Rossmann MG. Structure of the Three N-terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-like Bacteriophage. J Virol. 2011 Jun 1. PMID:21632759 doi:10.1128/JVI.00847-11
