Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins

Daichi Yamashita, Takaki Sugawara, Miyu Takeshita, Jun Kaneko, Yoshiyuki Kamio, Isao Tanaka, Yoshikazu Tanaka () and Min Yao
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Daichi Yamashita: Graduate School of Life Sciences, Hokkaido University
Takaki Sugawara: Graduate School of Life Sciences, Hokkaido University
Miyu Takeshita: Graduate School of Agricultural Science, Tohoku University
Jun Kaneko: Graduate School of Agricultural Science, Tohoku University
Yoshiyuki Kamio: Graduate School of Comprehensive Human Sciences, Shokei Gakuin University
Isao Tanaka: Graduate School of Life Sciences, Hokkaido University
Yoshikazu Tanaka: Graduate School of Life Sciences, Hokkaido University
Min Yao: Graduate School of Life Sciences, Hokkaido University

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the β-barrel formation process. Here, we report crystal structures of staphylococcal γ-haemolysin and leucocidin prepores. The structures reveal a disordered bottom half of the β-barrel corresponding to the transmembrane region, and a rigid upper extramembrane half. Spectroscopic analysis of fluorescently labelled mutants confirmed that the prepore is distinct from the pore within the transmembrane region. Mutational analysis also indicates a pivotal role for the glycine residue located at the lipid–solvent interface as a ‘joint’ between the two halves of the β-barrel. These observations suggest a two-step transmembrane β-barrel pore formation mechanism in which the upper extramembrane and bottom transmembrane regions are formed independently.

Date: 2014
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DOI: 10.1038/ncomms5897

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