title: Membrane Penetration by Bacterial Viruses.
abstract: The bacteriophage ϕ29 infects Gram-positiveBacillus subtiliswith 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.
authors.affiliation: Beijing Advanced Innovation Center for Structural Biology, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Center for Global Health and Infectious Diseases, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
authors.forename: Jingwei
authors.initials: J
authors.lastname: Xu
authors.affiliation: Beijing Advanced Innovation Center for Structural Biology, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Center for Global Health and Infectious Diseases, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China yxiang@mail.tsinghua.edu.cn.
authors.forename: Ye
authors.initials: Y
authors.lastname: Xiang
mesh_terms: D017103:Bacillus Phages / Q000502:physiology*; D001412:Bacillus subtilis / Q000821:virology*; D001692:Biological Transport; D004279:DNA, Viral / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D004279:DNA, Viral; D008565:Membrane Proteins; D014764:Viral Proteins
keywords: bacteriophages; cryoEM; crystal structure; gp9; membrane penetration; membrane-active peptide; short noncontractile tail; tail knob; ϕ29