AI Article Synopsis
- - The 3D structures of Helicobacter pylori phages KHP30 and KHP40 were determined using cryoelectron microscopy, revealing features like icosahedral symmetry and high resolution of 2.7 and 3.0 Å.
- - Each capsid contains 540 structural proteins, including major capsid proteins and cement proteins, with a unique arrangement forming pentagonal and hexagonal capsomeres that contribute to the stability of the virus.
- - Comparisons of sequences and structures among related phages indicate mechanisms through which these viruses may adapt to survive in the human gastric environment.
Article 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.
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| http://dx.doi.org/10.1016/j.str.2021.09.001 | DOI Listing |
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