Acid-stable capsid structure of Helicobacter pylori bacteriophage KHP30 by single-particle cryoelectron microscopy

Ryosuke Kamiya, Jumpei Uchiyama, Shigenobu Matsuzaki, Kazuyoshi Murata, Kenji Iwasaki, Naoyuki Miyazaki

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)300-312.e3
JournalStructure
Volume30
Issue number2
DOIs
Publication statusPublished - Feb 3 2022
Externally publishedYes

Keywords

  • capsid structure
  • cryoelectron microscopy
  • Helicobacter pylori bacteriophage
  • near-atomic resolution
  • single-particle analysis

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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