TY - JOUR
T1 - Acid-stable capsid structure of Helicobacter pylori bacteriophage KHP30 by single-particle cryoelectron microscopy
AU - Kamiya, Ryosuke
AU - Uchiyama, Jumpei
AU - Matsuzaki, Shigenobu
AU - Murata, Kazuyoshi
AU - Iwasaki, Kenji
AU - Miyazaki, Naoyuki
N1 - Funding Information:
This work was supported by JSPS KAKENHI grant nos. 15K18521 (to N.M.) and 18K06154 (to N.M.), the Collaborative Study Program of the National Institute for Physiological Sciences (to N.M. and J.U.), the Platform Project for Drug Discovery, Informatics, and Structural Life Science (PDIS) from the Ministry of Education, Culture, Sports, Science and Technology ( MEXT ) and the Japan Agency for Medical Research and Development ( AMED ), and for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research: BINDS) (to N.M. and K.I.).
Publisher Copyright:
© 2021 Elsevier Ltd
PY - 2022/2/3
Y1 - 2022/2/3
N2 - The acid-stable capsid structures of Helicobacter pylori phages KHP30 and KHP40 are solved at 2.7 and 3.0 Å resolutions by cryoelectron microscopy, respectively. The capsids have icosahedral T = 9 symmetry and consist of each 540 copies of 2 structural proteins, a major capsid protein, and a cement protein. The major capsid proteins form 12 pentagonal capsomeres occupying icosahedral vertexes and 80 hexagonal capsomeres located at icosahedral faces and edges. The major capsid protein has a unique protruding loop extending to the neighboring subunit that stabilizes hexagonal capsomeres. Furthermore, the capsid is decorated with trimeric cement proteins with a jelly roll motif. The cement protein trimer sits on the quasi-three-fold axis formed by three major capsid protein capsomeres, thereby enhancing the particle stability by connecting these capsomeres. Sequence and structure comparisons between the related Helicobacter pylori phages suggest a possible mechanism of phage adaptation to the human gastric environment.
AB - The acid-stable capsid structures of Helicobacter pylori phages KHP30 and KHP40 are solved at 2.7 and 3.0 Å resolutions by cryoelectron microscopy, respectively. The capsids have icosahedral T = 9 symmetry and consist of each 540 copies of 2 structural proteins, a major capsid protein, and a cement protein. The major capsid proteins form 12 pentagonal capsomeres occupying icosahedral vertexes and 80 hexagonal capsomeres located at icosahedral faces and edges. The major capsid protein has a unique protruding loop extending to the neighboring subunit that stabilizes hexagonal capsomeres. Furthermore, the capsid is decorated with trimeric cement proteins with a jelly roll motif. The cement protein trimer sits on the quasi-three-fold axis formed by three major capsid protein capsomeres, thereby enhancing the particle stability by connecting these capsomeres. Sequence and structure comparisons between the related Helicobacter pylori phages suggest a possible mechanism of phage adaptation to the human gastric environment.
KW - capsid structure
KW - cryoelectron microscopy
KW - Helicobacter pylori bacteriophage
KW - near-atomic resolution
KW - single-particle analysis
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U2 - 10.1016/j.str.2021.09.001
DO - 10.1016/j.str.2021.09.001
M3 - Article
C2 - 34597601
AN - SCOPUS:85123680583
SN - 0969-2126
VL - 30
SP - 300-312.e3
JO - Structure with Folding & design
JF - Structure with Folding & design
IS - 2
ER -