Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus

Iimori, Minato; Oki, Hiroya; Akeda, Yukihiro; Ishii, Eiji; Kodama, Toshio; Ueda, Takumi; Nakamura, Shota; Matsuda, Shigeaki; Kawahara, Kazuki; Iida, Tetsuya

doi:https://doi.org/10.1016/j.bbrc.2025.152190

Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus

Iimori, Minato; Oki, Hiroya; Akeda, Yukihiro et al.

Biochemical and Biophysical Research Communications, 2025, 776, 152190

アクセス数:46件（2025-09-29 11:21 集計）

固定URL: https://hdl.handle.net/11094/102613

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タイトル	Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus
著者	著者名 Iimori, Minato
	NRID 1000030845285 1000030845285 researchmap permalink hiroya168 hiroya168 著者名 Oki, Hiroya
	NRID 1000060444527 1000060444527 researchmap permalink yakeda yakeda 著者名 Akeda, Yukihiro
	NRID 1000010835698 1000010835698 ORCID 0000-0001-7899-252X 0000-0001-7899-252X researchmap permalink eishii0322 eishii0322 Scopus Author ID 56890709800 56890709800 著者名 Ishii, Eiji
	NRID 1000020346133 1000020346133 著者名 Kodama, Toshio
	NRID 1000020451859 1000020451859 researchmap permalink TakumiUeda TakumiUeda 著者名 Ueda, Takumi
	NRID 1000090432434 1000090432434 ORCID 0000-0003-2058-5942 0000-0003-2058-5942 researchmap permalink nkmrshota nkmrshota Scopus Author ID 35315778200 35315778200 著者名 Nakamura, Shota
	NRID 1000030506499 1000030506499 ORCID 0000-0001-8430-9723 0000-0001-8430-9723 researchmap permalink shigeakimatsuda shigeakimatsuda Scopus Author ID 22135321100 22135321100 著者名 Matsuda, Shigeaki
	NRID 1000060585058 1000060585058 researchmap permalink 051619 051619 Scopus Author ID 9740512500 9740512500 著者名 Kawahara, Kazuki
	NRID 1000090221746 1000090221746 researchmap permalink iidatetsuya iidatetsuya Scopus Author ID 7402683497 7402683497 著者名 Iida, Tetsuya
キーワード等	Chaperone
	Effector
	Protein crystallography
	Type III secretion system
	Vibrio parahaemolyticus
内容	Iimori M., Oki H., Akeda Y., et al. Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus. Biochemical and Biophysical Research Communications 776, 152190 (2025); https://doi.org/10.1016/j.bbrc.2025.152190.
抄録	Many pathogenic gram-negative bacteria utilise the type III secretion system (T3SS), a specific protein injection apparatus, to translocate virulence effectors into host cells, modulating host cell functions and establishing infection. To facilitate the precise cytosolic transport of effectors to T3SS, a class of proteins called chaperones plays a crucial role. However, a limited number of available structural data on chaperone-effector complexes hampers understanding of the mechanisms underlying this process. In Vibrio parahaemolyticus, a major causative agent of seafood-associated acute gastroenteritis in humans, T3SS chaperone VecA transports its cognate membrane-disrupting effector, VepA. Here, we determined the crystal structure of VecA alone and in complex with VepA at resolutions of 2.20 Å and 2.49 Å, respectively. While the overall protein fold and the hydrophobic cleft that accommodates an N-terminal β-motif of effectors were conserved among T3SS chaperones, the structural analysis revealed that surface residues are remarkably different, reflecting their substrate specificity. Additionally, unlike other reported structures of the T3SS chaperone-effector complexes, in which the effectors are partially unfolded and wrapped around the chaperone, VepA adopts a highly folded conformation in the complex. This compact structure appears to protect the fragile glycine-rich transmembrane domain of VepA and suggests that upon secretion, VepA undergoes conformational changes, including α-helix formation, allowing the transmembrane domain to embed into and disrupt the membrane of organelles containing its binding target, V-ATPase. These findings elucidate the chaperone-mediated regulation of effector transport and function of the bacterial virulence-related T3SS.
出版者	Elsevier B.V.
収録物名	Biochemical and Biophysical Research Communications
巻(号)	776
ページ	152190
刊行年月	2025-06-14
言語	英語
ハンドルURL	https://hdl.handle.net/11094/102613
PISSN	0006291X
eISSN	10902104
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1016/j.bbrc.2025.152190
アクセス権	open access
権利情報	This article is licensed under a Creative Commons Attribution 4.0 International License.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Biochemical and Biophysical Research Communications. 2025, 776, p. 152190
DC.title	Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus
DC.creator	Iimori, Minato
	Oki, Hiroya
	Akeda, Yukihiro
	Ishii, Eiji
	Kodama, Toshio
	Ueda, Takumi
	Nakamura, Shota
	Matsuda, Shigeaki
	Kawahara, Kazuki
	Iida, Tetsuya
DC.publisher	Elsevier B.V.
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2025-06-14
DC.identifier	https://doi.org/10.1016/j.bbrc.2025.152190
DC.subject	Chaperone
	Effector
	Protein crystallography
	Type III secretion system
	Vibrio parahaemolyticus
DC.description	Iimori M., Oki H., Akeda Y., et al. Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus. Biochemical and Biophysical Research Communications 776, 152190 (2025); https://doi.org/10.1016/j.bbrc.2025.152190.
DCTERMS.abstract	Many pathogenic gram-negative bacteria utilise the type III secretion system (T3SS), a specific protein injection apparatus, to translocate virulence effectors into host cells, modulating host cell functions and establishing infection. To facilitate the precise cytosolic transport of effectors to T3SS, a class of proteins called chaperones plays a crucial role. However, a limited number of available structural data on chaperone-effector complexes hampers understanding of the mechanisms underlying this process. In Vibrio parahaemolyticus, a major causative agent of seafood-associated acute gastroenteritis in humans, T3SS chaperone VecA transports its cognate membrane-disrupting effector, VepA. Here, we determined the crystal structure of VecA alone and in complex with VepA at resolutions of 2.20 Å and 2.49 Å, respectively. While the overall protein fold and the hydrophobic cleft that accommodates an N-terminal β-motif of effectors were conserved among T3SS chaperones, the structural analysis revealed that surface residues are remarkably different, reflecting their substrate specificity. Additionally, unlike other reported structures of the T3SS chaperone-effector complexes, in which the effectors are partially unfolded and wrapped around the chaperone, VepA adopts a highly folded conformation in the complex. This compact structure appears to protect the fragile glycine-rich transmembrane domain of VepA and suggests that upon secretion, VepA undergoes conformational changes, including α-helix formation, allowing the transmembrane domain to embed into and disrupt the membrane of organelles containing its binding target, V-ATPase. These findings elucidate the chaperone-mediated regulation of effector transport and function of the bacterial virulence-related T3SS.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	102613
citation_title	Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus
citation_author	Iimori, Minato
	Oki, Hiroya
	Akeda, Yukihiro
	Ishii, Eiji
	Kodama, Toshio
	Ueda, Takumi
	Nakamura, Shota
	Matsuda, Shigeaki
	Kawahara, Kazuki
	Iida, Tetsuya
citation_publisher	Elsevier B.V.
citation_language	英語
citation_date	2025-06-14
citation_journal_title	Biochemical and Biophysical Research Communications
citation_volume	776
citation_firstpage	152190
citation_doi	https://doi.org/10.1016/j.bbrc.2025.152190
citation_public_url	https://hdl.handle.net/11094/102613

Structural basis of effector recognition by the T3SS chaperone VecA from Vibrio parahaemolyticus

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