Membrane Penetration by Bacterial Viruses

Abstract

The bacteriophage ϕ29 infects Gram-positive Bacillus subtilis with a short noncontractile tail. Recent studies showed that the ϕ29 tail protein gp9 forms a hexameric tube with six long loops of membrane-active peptides blocking in the tube at the distal end of the tail. The long loops exit on genome release and form a membrane pore for passage of the genome. The membrane penetration mechanism of the ϕ29 tail might be common among tailed bacteriophages.

Keywords: bacteriophages; cryoEM; crystal structure; gp9; membrane penetration; membrane-active peptide; short noncontractile tail; tail knob; ϕ29.