title: Anatomy of a lactococcal phage tail.
abstract: Bacteriophages of the Siphoviridae family utilize a long noncontractile tail to recognize, adsorb to, and inject DNA into their bacterial host. The tail anatomy of the archetypal Siphoviridae lambda has been well studied, in contrast to phages infecting gram-positive bacteria. This report outlines a detailed anatomical description of a typical member of the Siphoviridae infecting a gram-positive bacterium. The tail superstructure of the lactococcal phage Tuc2009 was investigated using N-terminal protein sequencing, Western blotting, and immunogold transmission electron microscopy, allowing a tangible path to be followed from gene sequence through encoded protein to specific architectural structures on the Tuc2009 virion. This phage displays a striking parity with lambda with respect to tail structure, which reenforced a model proposed for Tuc2009 tail architecture. Furthermore, comparisons with lambda and other lactococcal phages allowed the specification of a number of genetic submodules likely to encode specific tail structures.
authors.affiliation: Department of Microbiology, National University of Ireland, Cork, Ireland. smcgrath@ucc.ie
authors.forename: Stephen
authors.initials: S
authors.lastname: Mc Grath
authors.forename: Horst
authors.initials: H
authors.lastname: Neve
authors.forename: Jos F M L
authors.initials: JF
authors.lastname: Seegers
authors.forename: Robyn
authors.initials: R
authors.lastname: Eijlander
authors.forename: Christina S
authors.initials: CS
authors.lastname: Vegge
authors.forename: Lone
authors.initials: L
authors.lastname: Brøndsted
authors.forename: Knut J
authors.initials: KJ
authors.lastname: Heller
authors.forename: Gerald F
authors.initials: GF
authors.lastname: Fitzgerald
authors.forename: Finn K
authors.initials: FK
authors.lastname: Vogensen
authors.forename: Douwe
authors.initials: D
authors.lastname: van Sinderen
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D005784:Gene Amplification; D005822:Genetic Vectors; D017045:Lactococcus / Q000821:virology*; D013294:Lactococcus lactis / Q000821:virology; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron; D016366:Open Reading Frames; D010957:Plasmids; D017906:Siphoviridae / Q000235:genetics* / Q000648:ultrastructure*; D014764:Viral Proteins / Q000302:isolation & purification
chemical_list: D014764:Viral Proteins