期刊
VIROLOGY
卷 421, 期 2, 页码 141-148出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2011.08.028
关键词
Bacteriophage; Myoviridae; DNA ejection; Contractile tail; Tail contraction; Bacillus anthracis; Cryo-electron tomography; Phage infection; Tail sheath; Base plate
类别
资金
- U.S. Department of the Army [W81XWH-10-2-0125]
- Welch Foundation [AU-1714]
- Structural Biology Center at the UT Houston Medical School
The structure of the Bacillus anthracis spore-binding phage 8a was determined by cryo-electron tomography. The phage capsid forms a T = 16 icosahedron attached to a contractile tail via a head-tail connector protein. The tail consists of a six-start helical sheath surrounding a central tail tube, and a structurally novel baseplate at the distal end of the tail that recognizes and attaches to host cells. The parameters of the icosahedral capsid lattice and the helical tail sheath suggest protein folds for the capsid and tail-sheath proteins, respectively, and indicate evolutionary relationships to other dsDNA viruses. Analysis of 2518 intact phage particles show four distinct conformations that likely correspond to four sequential states of the DNA ejection process during infection. Comparison of the four observed conformations suggests a mechanism for DNA ejection, including the molecular basis underlying coordination of tail sheath contraction and genome release from the capsid. (C) 2011 Elsevier Inc. All rights reserved.
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