Extraordinarily Stable Amyloid Fibrils Engineered from Structurally Defined β-Solenoid Proteins

Peng, Zeyu; Peralta, Maria D R; Toney, Michael D.

doi:10.1021/acs.biochem.7b00364

Cited by 14 publications

(11 citation statements)

References 52 publications

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“…The HET-s fibril is a left-handed β-solenoid with each protein molecule forming two helical turns [10] by which multilayer formation of two layers was reported for HET-s(218–289). In addition synthetically engineered β-solenoid proteins were shown to be extraordinarily stable toward organic solvents, urea, and pH extremes and temperature [59]. However despite sharing some structural and biochemical properties with amyloid proteins, the HP1542 bactofilin was neither resistant to proteinase K digestion nor stainable with thioflavin T which is often used for identifying amyloid fibrils both in vivo and in vitro [60].…”

Section: Discussionmentioning

confidence: 99%

Biochemical characterization of the Helicobacter pylori bactofilin-homolog HP1542

et al. 2019

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The human pathogen Helicobacter pylori is known for its colonization of the upper digestive system, where it escapes the harsh acidic environment by hiding in the mucus layer. One factor promoting this colonization is the helical cell shape of H . pylori . Among shape determining proteins are cytoskeletal elements like the recently discovered bactofilins. Bactofilins constitute a widespread family of polymer-forming bacterial proteins whose biology is still poorly investigated. Here we describe the first biochemical analysis of the bactofilin HP1542 of H . pylori reference strain 26695. Purified HP1542 forms sheet-like 2D crystalline assemblies, which clearly depend on a natively structured C-terminus. Polymerization properties and protein stability were investigated. Additionally, we also could demarcate HP1542 from amyloid proteins that share similarities with the bactofilin DUF domain. By using zonal centrifugation of total H . pylori cell lysates and immunfluorescence analysis we revealed peripheral membrane association of HP1542 mostly pronounced near mid-cell. Interestingly our results indicate that H . pylori bactofilin does not contribute to cell wall stability. This study might act as a starting point for biophysical studies of the H . pylori bactofilin biology as well as for the investigation of bactofilin cell physiology in this organism. Importantly, this study is the first biochemical analysis of a bactofilin in a human pathogen.

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Section: Discussionmentioning

confidence: 99%

Biochemical characterization of the Helicobacter pylori bactofilin-homolog HP1542

et al. 2019

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“…This discontinuity is one of the features of the DUF3494 fold that would be difficult to duplicate in an independent evolution of the fold. It is also a reason why beta‐solenoids are typically ‘capped’ to prevent end‐to‐end associations that can lead to amyloid formation .…”

Section: Structural Features Of Ibps Belonging To Duf3494mentioning

confidence: 99%

Ice‐binding proteins and the ‘domain of unknown function’ 3494 family

et al. 2019

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Ice‐binding proteins (IBPs) control the growth and shape of ice crystals to cope with subzero temperatures in psychrophilic and freeze‐tolerant organisms. Recently, numerous proteins containing the domain of unknown function (DUF) 3494 were found to bind ice crystals and, hence, are classified as IBPs. DUF3494 IBPs constitute today the most widespread of the known IBP families. They can be found in different organisms including bacteria, yeasts and microalgae, supporting the hypothesis of horizontal transfer of its gene. Although the 3D structure is always a discontinuous β‐solenoid with a triangular cross‐section and an adjacent alpha‐helix, DUF3494 IBPs present very diverse activities in terms of the magnitude of their thermal hysteresis and inhibition of ice recrystallization. The proteins are secreted into the environments around the host cells or are anchored on their cell membranes. This review covers several aspects of this new class of IBPs, which promise to leave their mark on several research fields including structural biology, protein biochemistry and cryobiology.

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“…The self‐assembled amyloid aggregates have closely packed cross‐β‐sheet secondary structure, in which β‐strands are held together securely by repetitive hydrogen bonding and side‐chain interactions . Owing to their structural robustness, the amyloid assemblies exhibit high resistance to degradation by chemical or biological means …”

Section: Introductionmentioning

confidence: 99%

Photoactive Bismuth Vanadate Structure for Light‐Triggered Dissociation of Alzheimer's β‐Amyloid Aggregates

Kim

Lee

Choi

et al. 2018

Adv Funct Materials

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Bismuth vanadate (BiVO 4 ) is an attractive, low-cost n-type semiconductor that exhibits excellent photoelectrocatalytic properties, chemical stability, and biocompatibility. This study reports a newly discovered function of BiVO 4 dissociating highly stable, self-assembled amyloid aggregates associated with Alzheimer's disease. A visible light-active, nanoporous BiVO 4 platform is developed to break β-amyloid (Aβ) assemblies and alleviate Aβ aggregateinduced toxicity. Multiple photochemical and microscopic analyses reveal that β-sheet-rich, long Aβ fibrils are effectively destabilized and broken into small-sized, soluble species by BiVO 4 photoelectrode under illumination of a white light-emitting diode and an anodic bias. The photoactivated BiVO 4 under anodic bias generates oxidative stress, such as superoxide ions and hole-derived hydrogen peroxide, which causes photooxidation of Aβ residues and irreversible disassembly of Aβ aggregates. The efficacy of photoelectrocatalytic dissociation of Aβ aggregates is enhanced by Mo-doped BiVO 4 , which facilitates the separation of electron-hole pairs by improving electrontransport properties of BiVO 4 . Furthermore, it is verified that both pristine and Mo-doped BiVO 4 photoelectrodes are nontoxic and effective in reducing Aβ-associated cytotoxicity. The work shows the potential of BiVO 4 -based photoelectrode platforms for the dissociation of neurotoxic, highly stable Aβ assemblies using light energy.

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Extraordinarily Stable Amyloid Fibrils Engineered from Structurally Defined β-Solenoid Proteins

Cited by 14 publications

References 52 publications

Biochemical characterization of the Helicobacter pylori bactofilin-homolog HP1542

Biochemical characterization of the Helicobacter pylori bactofilin-homolog HP1542

Ice‐binding proteins and the ‘domain of unknown function’ 3494 family

Photoactive Bismuth Vanadate Structure for Light‐Triggered Dissociation of Alzheimer's β‐Amyloid Aggregates

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