Structural Characterization at the Atomic Level of a Molecular Nano-Machine: The State of the Art of &lt;i&gt;Helicobacter Pylori&lt;/i&gt; Flagellum Organization

Pulić, Ivana; Loconte, Valentina; Zanotti, Giuseppe

doi:10.3844/ajbbsp.2014.143.161

Cited by 4 publications

(2 citation statements)

References 88 publications

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“…Flagellar filaments consist of the major (FlaA) and the minor (FlaB) flagellin proteins [53,75,76,78]. Additional related genes, fliD and flgK, are required for flagellar filaments assembly and flagella formation [76][77][78]. For flagellar assembly and motility, flagellin needs to be O-glycosylated with pseudaminic acid (Pse).…”

Section: Virulence (Adherence Motility and Pathogenicity)mentioning

confidence: 99%

Flavodoxins as Novel Therapeutic Targets against Helicobacter pylori and Other Gastric Pathogens

Salillas

Sancho

2020

IJMS

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Flavodoxins are small soluble electron transfer proteins widely present in bacteria and absent in vertebrates. Flavodoxins participate in different metabolic pathways and, in some bacteria, they have been shown to be essential proteins representing promising therapeutic targets to fight bacterial infections. Using purified flavodoxin and chemical libraries, leads can be identified that block flavodoxin function and act as bactericidal molecules, as it has been demonstrated for Helicobacter pylori (Hp), the most prevalent human gastric pathogen. Increasing antimicrobial resistance by this bacterium has led current therapies to lose effectiveness, so alternative treatments are urgently required. Here, we summarize, with a focus on flavodoxin, opportunities for pharmacological intervention offered by the potential protein targets described for this bacterium and provide information on other gastrointestinal pathogens and also on bacteria from the gut microbiota that contain flavodoxin. The process of discovery and development of novel antimicrobials specific for Hp flavodoxin that is being carried out in our group is explained, as it can be extrapolated to the discovery of inhibitors specific for other gastric pathogens. The high specificity for Hp of the antimicrobials developed may be of help to reduce damage to the gut microbiota and to slow down the development of resistant Hp mutants.

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Section: Virulence (Adherence Motility and Pathogenicity)mentioning

confidence: 99%

Flavodoxins as Novel Therapeutic Targets against Helicobacter pylori and Other Gastric Pathogens

Salillas

Sancho

2020

IJMS

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“…The BFM functions as a membrane-embedded rotary engine. The core component of its rotor, the rod, is surrounded by several rings 4 – 6 . In most flagellated bacteria, the force that rotates the rod is generated by the proton influx through several circumferentially positioned peptidoglycan (PG)-anchored MotA 4 MotB 2 stator complexes 7 .…”

Section: Introductionmentioning

confidence: 99%

Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper

Andrews

Nesmelov

Wilce

et al. 2017

Sci Rep

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Rotation of the bacterial flagellum is powered by a proton influx through the peptidoglycan (PG)-tethered stator ring MotA/B. MotA and MotB form an inner-membrane complex that does not conduct protons and does not bind to PG until it is inserted into the flagellar motor. The opening of the proton channel involves association of the plug helices in the periplasmic region of the MotB dimer into a parallel coiled coil. Here, we have characterised the structure of a soluble variant of full-length Helicobacter pylori MotB in which the plug helix was engineered to be locked in a parallel coiled coil state, mimicking the open state of the stator. Fluorescence resonance energy transfer measurements, combined with PG-binding assays and fitting of the crystal structures of MotB fragments to the small angle X-ray scattering (SAXS) data revealed that the protein’s C-terminal domain has a PG-binding-competent conformation. Molecular modelling against the SAXS data suggested that the linker in H. pylori MotB forms a subdomain between the plug and the C-terminal domain, that ‘clamps’ the coiled coil of the plug, thus stabilising the activated form of the protein. Based on these results, we present a pseudo-atomic model structure of full-length MotB in its activated form.

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Applications of IgY in Human Medicine

Vieira-Pires

Morgan

Choraria³

et al. 2021

IgY-Technology: Production and Application of Egg Yolk Antibodies

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Structural Characterization at the Atomic Level of a Molecular Nano-Machine: The State of the Art of <i>Helicobacter Pylori</i> Flagellum Organization

Cited by 4 publications

References 88 publications

Flavodoxins as Novel Therapeutic Targets against Helicobacter pylori and Other Gastric Pathogens

Flavodoxins as Novel Therapeutic Targets against Helicobacter pylori and Other Gastric Pathogens

Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper

Applications of IgY in Human Medicine

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