A touch of glue to complete bacteriophage assembly: the tail‐to‐head joining protein (THJP) family

• DOI: 10.1111/mmi.12526
• Publication Date: 2014-01-21T12:12:16Z
• Authors: Isabelle Auzat; Isabelle Petitpas; Rudi Lurz; Frank Weise; Paulo Tavares
• Keywords: GLUE; Family member

Summary Bacteriophage SPP 1 is a nanomachine built to infect the bacterium B acillus subtilis . The phage particle composed of an icosahedric capsid, which contains viral DNA , and long non‐contractile tail. Capsids tails are produced in infected cells by two distinct morphogenetic pathways. Characterization suppressor‐sensitive mutant sus82 showed that it produces ‐filled capsids but unable assemble complete virions. Its purified have normal length lack narrow ring tapers tail end found at tail‐to‐head interface. defective production gp17. gp17 exposed free competent for assembly becomes shielded final virion structure. Recombinant active vitro assay stick together present extracts ‐infected cells, leading formation infectious particles. Gp17 thus plays fundamental role joining reaction, ultimate step virus assembly. This conserved function its structurally related proteins like lambda gpU family can also provide fidelity termination tube elongation reaction subset phages including coliphage lambda.