Helical reconstruction of Salmonella and Shigella needle filaments attached to type 3 basal bodies
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Helical reconstruction of Salmonella and Shigella needle filaments attached to type 3 basal bodies. / Kotov, Vadim; Lunelli, Michele; Wald, Jiri; Kolbe, Michael; Marlovits, Thomas C.
In: BIOCHEM BIOPHYS REP, Vol. 27, 09.2021, p. 101039.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Helical reconstruction of Salmonella and Shigella needle filaments attached to type 3 basal bodies
AU - Kotov, Vadim
AU - Lunelli, Michele
AU - Wald, Jiri
AU - Kolbe, Michael
AU - Marlovits, Thomas C
N1 - © 2021 Published by Elsevier B.V.
PY - 2021/9
Y1 - 2021/9
N2 - Gram-negative pathogens evolved a syringe-like nanomachine, termed type 3 secretion system, to deliver protein effectors into the cytoplasm of host cells. An essential component of this system is a long helical needle filament that protrudes from the bacterial surface and connects the cytoplasms of the bacterium and the eukaryotic cell. Previous structural research was predominantly focused on reconstituted type 3 needle filaments, which lacked the biological context. In this work we introduce a facile procedure to obtain high-resolution cryo-EM structure of needle filaments attached to the basal body of type 3 secretion systems. We validate our approach by solving the structure of Salmonella PrgI filament and demonstrate its utility by obtaining the first high-resolution cryo-EM reconstruction of Shigella MxiH filament. Our work paves the way to systematic structural characterization of attached type 3 needle filaments in the context of mutagenesis studies, protein structural evolution and drug development.
AB - Gram-negative pathogens evolved a syringe-like nanomachine, termed type 3 secretion system, to deliver protein effectors into the cytoplasm of host cells. An essential component of this system is a long helical needle filament that protrudes from the bacterial surface and connects the cytoplasms of the bacterium and the eukaryotic cell. Previous structural research was predominantly focused on reconstituted type 3 needle filaments, which lacked the biological context. In this work we introduce a facile procedure to obtain high-resolution cryo-EM structure of needle filaments attached to the basal body of type 3 secretion systems. We validate our approach by solving the structure of Salmonella PrgI filament and demonstrate its utility by obtaining the first high-resolution cryo-EM reconstruction of Shigella MxiH filament. Our work paves the way to systematic structural characterization of attached type 3 needle filaments in the context of mutagenesis studies, protein structural evolution and drug development.
U2 - 10.1016/j.bbrep.2021.101039
DO - 10.1016/j.bbrep.2021.101039
M3 - SCORING: Journal article
C2 - 34258394
VL - 27
SP - 101039
JO - BIOCHEM BIOPHYS REP
JF - BIOCHEM BIOPHYS REP
SN - 2405-5808
ER -