title: The proteome and interactome of Streptococcus pneumoniae phage Cp-1.
abstract: Mass spectrometry analysis of Streptococcus pneumoniae bacteriophage Cp-1 identified a total of 12 proteins, and proteome-wide yeast two-hybrid screens revealed 17 binary interactions mainly among these structural proteins. On the basis of the resulting linkage map, we suggest an improved structural model of the Cp-1 virion.
authors.affiliation: Institute of Toxicology and Genetics, Karlsruhe Institute for Technology, Karlsruhe, Germany.
authors.forename: Roman
authors.initials: R
authors.lastname: Häuser
authors.forename: Mourad
authors.initials: M
authors.lastname: Sabri
authors.forename: Sylvain
authors.initials: S
authors.lastname: Moineau
authors.forename: Peter
authors.initials: P
authors.lastname: Uetz
mesh_terms: D015967:Gene Expression Regulation, Viral / Q000502:physiology*; D016679:Genome, Viral; D011485:Protein Binding; D020543:Proteome; D040901:Proteomics / Q000379:methods; D017108:Streptococcus Phages / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D013296:Streptococcus pneumoniae / Q000821:virology*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D020543:Proteome; D014764:Viral Proteins