Authors
Hajime Yamauchi, Kei Sakamoto, Yasuyuki Matsuda, Yuko Tanishita, Akito Ariyoshi, Daisuke Sasaki, Yu Shimoyama, Akihiro Hasegawa, Takayoshi Yamauchi, Yoichiro Iwakura, Haruki Okamura, Shun'ichiro Taniguchi, Masafumi Takahashi, Akihiko Yoshimura, Katsunori Yanagihara, Gabriel Nuñez, Hideki Hara
Published in
EMBO reports. Sep 07, 2026. Epub Sep 07, 2026.
Abstract
Excessive inflammasome activation is increasingly recognized as a critical driver of pathology during bacterial infections, yet the pathogen-derived mechanisms that trigger dysregulated inflammasome responses remain poorly defined. Here, we identify a previously unrecognized role for the serine/threonine kinase Aurora A in promoting inflammasome activation during Staphylococcus aureus infection. We demonstrate that S. aureus activates JNK-dependent signaling in macrophages, leading to the phosphorylation of Aurora A. Activated Aurora A directly phosphorylates ASC, the inflammasome adaptor, on serine residues, enhancing ASC oligomerization and facilitating robust caspase-1 activation through both NLRP3 and AIM2 inflammasomes. This phosphorylation event stabilizes ASC speck formation and amplifies downstream IL-1β production, thereby intensifying inflammatory responses. Importantly, pharmacological inhibition or genetic disruption of Aurora A markedly suppresses inflammasome activation in vitro and in vivo, significantly reduces bacterial burdens and improves survival in mice infected with antibiotic-resistant S. aureus. These findings reveal Aurora A as a key host regulator exploited by S. aureus to potentiate inflammasome-driven inflammation and highlight inflammasome inhibition as a potential therapeutic strategy that augments host defense independently of antibiotic resistance.
PMID:
42706431
Bibliographic data and abstract were imported from PubMed on 08 Sep 2026.
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