scholarly journals Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase From Shigella flexneri

2018 ◽  
Vol 9 ◽  
Author(s):  
Xiaopan Gao ◽  
Zhixia Mu ◽  
Xia Yu ◽  
Bo Qin ◽  
Justyna Wojdyla ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Type Iii Secretion ◽  
Shigella Flexneri ◽  
Atp Binding ◽  
Type Iii ◽  
Structural Insight ◽  
Insight Into

scholarly journals Conformational Changes in IpaD fromShigella flexneriupon Binding Bile Salts Provide Insight into the Second Step of Type III Secretion

Biochemistry ◽  
2011 ◽  
Vol 50 (2) ◽  
pp. 172-180 ◽  
Author(s):  
Nicholas E. Dickenson ◽  
Lingling Zhang ◽  
Chelsea R. Epler ◽  
Philip R. Adam ◽  
Wendy L. Picking ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Type Iii Secretion ◽  
Bile Salts ◽  
Second Step ◽  
Type Iii ◽  
Insight Into

scholarly journals Transcriptional slippage controls production of type III secretion apparatus components in Shigella flexneri

2006 ◽  
Vol 62 (5) ◽  
pp. 1460-1468 ◽  
Author(s):  
Christophe Penno ◽  
Abderrahman Hachani ◽  
Latefa Biskri ◽  
Philippe Sansonetti ◽  
Abdelmounaïm Allaoui ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Shigella Flexneri ◽  
Type Iii ◽  
Transcriptional Slippage

scholarly journals Small-Molecule Type III Secretion System Inhibitors Block Assembly of the Shigella Type III Secreton

2008 ◽  
Vol 191 (2) ◽  
pp. 563-570 ◽  
Author(s):  
Andreas K. J. Veenendaal ◽  
Charlotta Sundin ◽  
Ariel J. Blocker
Keyword(s):  
Type Iii Secretion ◽  
Bacterial Infections ◽  
Shigella Flexneri ◽  
Effector Proteins ◽  
Host Cells ◽  
Incomplete Penetrance ◽  
Secretion Systems ◽  
Bacterial Surface ◽  
Type Iii ◽  
Type Iii Secretion Systems

ABSTRACT Type III secretion systems (T3SSs) are essential virulence devices for many gram-negative bacteria that are pathogenic for plants, animals, and humans. They serve to translocate virulence effector proteins directly into eukaryotic host cells. T3SSs are composed of a large cytoplasmic bulb and a transmembrane region into which a needle is embedded, protruding above the bacterial surface. The emerging antibiotic resistance of bacterial pathogens urges the development of novel strategies to fight bacterial infections. Therapeutics that rather than kill bacteria only attenuate their virulence may reduce the frequency or progress of resistance emergence. Recently, a group of salicylidene acylhydrazides were identified as inhibitors of T3SSs in Yersinia, Chlamydia, and Salmonella species. Here we show that these are also effective on the T3SS of Shigella flexneri, where they block all related forms of protein secretion so far known, as well as the epithelial cell invasion and induction of macrophage apoptosis usually demonstrated by this bacterium. Furthermore, we show the first evidence for the detrimental effect of these compounds on T3SS needle assembly, as demonstrated by increased numbers of T3S apparatuses without needles or with shorter needles. Therefore, the compounds generate a phenocopy of T3SS export apparatus mutants but with incomplete penetrance. We discuss why this would be sufficient to almost completely block the later secretion of effector proteins and how this begins to narrow the search for the molecular target of these compounds.

scholarly journals Ribosome protection by antibiotic resistance ATP-binding cassette protein

2018 ◽  
Vol 115 (20) ◽  
pp. 5157-5162 ◽  
Author(s):  
Weixin Su ◽  
Veerendra Kumar ◽  
Yichen Ding ◽  
Rya Ero ◽  
Aida Serra ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
Conformational Changes ◽  
Atp Binding ◽  
Peptidyl Transferase ◽  
Exit Site ◽  
Peptidyl Transferase Center ◽  
Biochemical Assays ◽  
Exit Tunnel ◽  
Insight Into ◽  
Atp Binding Cassette

The ribosome is one of the richest targets for antibiotics. Unfortunately, antibiotic resistance is an urgent issue in clinical practice. Several ATP-binding cassette family proteins confer resistance to ribosome-targeting antibiotics through a yet unknown mechanism. Among them, MsrE has been implicated in macrolide resistance. Here, we report the cryo-EM structure of ATP form MsrE bound to the ribosome. Unlike previously characterized ribosomal protection proteins, MsrE is shown to bind to ribosomal exit site. Our structure reveals that the domain linker forms a unique needle-like arrangement with two crossed helices connected by an extended loop projecting into the peptidyl-transferase center and the nascent peptide exit tunnel, where numerous antibiotics bind. In combination with biochemical assays, our structure provides insight into how MsrE binding leads to conformational changes, which results in the release of the drug. This mechanism appears to be universal for the ABC-F type ribosome protection proteins.

scholarly journals Studying Conformational Changes of the Yersinia Type-III-Secretion Effector YopO in Solution by Integrative Structural Biology

Structure ◽  
2019 ◽  
Vol 27 (9) ◽  
pp. 1416-1426.e3 ◽  
Author(s):  
Martin F. Peter ◽  
Anne T. Tuukkanen ◽  
Caspar A. Heubach ◽  
Alexander Selsam ◽  
Fraser G. Duthie ◽  
...  
Keyword(s):  
Structural Biology ◽  
Conformational Changes ◽  
Type Iii Secretion ◽  
Type Iii ◽  
Integrative Structural Biology ◽  
Type Iii Secretion Effector
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