scholarly journals Diverse supramolecular structures formed by self‐assembling proteins of the B acillus subtilis spore coat

2015 ◽  
Vol 97 (2) ◽  
pp. 347-359 ◽  
Author(s):  
Shuo Jiang ◽  
Qiang Wan ◽  
Daniela Krajcikova ◽  
Jilin Tang ◽  
Svetomir B. Tzokov ◽  
...  
Keyword(s):  
Supramolecular Structures ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Self Assembling

scholarly journals Laccase and Its Mutant Displayed on the Bacillus subtilis Spore Coat for Oxidation of Phenolic Compounds in Organic Solvents

Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 606
Author(s):  
Silu Sheng ◽  
Edgardo T. Farinas
Keyword(s):  
Bacillus Subtilis ◽  
Organic Solvents ◽  
Environmental Changes ◽  
Sinapic Acid ◽  
Product Yield ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore ◽  
Cota Laccase ◽  
Inert Surface

Enzymes displayed on the Bacillus subtilis spore coat have several features that are useful for biocatalysis. The enzyme is preimmobilized on an inert surface of the spore coat, which is due to the natural sporulation process. As a result, protein stability can be increased, and they are resistant to environmental changes. Next, they would not lyse under extreme conditions, such as in organic solvents. Furthermore, they can be easily removed from the reaction solution and reused. The laboratory evolved CotA laccase variant T480A-CotA was used to oxidize the following phenolic substrates: (+)-catechin, (−)-epicatechin, and sinapic acid. The kinetic parameters were determined and T480A-CotA had a greater Vmax/Km than wt-CotA for all substrates. The Vmax/Km for T480A-CotA was 4.1, 5.6, and 1.4-fold greater than wt-CotA for (+)-catechin, (−)-epicatechin, and sinapic acid, respectively. The activity of wt-CotA and T480A-CotA was measured at different concentrations from 0–70% in organic solvents (dimethyl sulfoxide, ethanol, methanol, and acetonitrile). The Vmax for T480A-CotA was observed to be greater than the wt-CotA in all organic solvents. Finally, the T480A-CotA was recycled 7 times over a 23-h period and up to 60% activity for (+)-catechin remained. The product yield was up to 3.1-fold greater than the wild-type.

Self-assembling of p-tert-butylcalix[4]arene into supramolecular structures using transition-metal derivatization

1996 ◽  
pp. 119 ◽  
Author(s):  
Antonio Zanotti-Gerosa ◽  
Euro Solari ◽  
Luca Giannini ◽  
Carlo Floriani ◽  
Angiola Chiesi-Villa ◽  
...  
Keyword(s):  
Transition Metal ◽  
Supramolecular Structures ◽  
Self Assembling

Display of Bombyx mori Nucleopolyhedrovirus GP64 on the Bacillus subtilis Spore Coat

2011 ◽  
Vol 62 (5) ◽  
pp. 1368-1373 ◽  
Author(s):  
Guohui Li ◽  
Qi Tang ◽  
Huiqing Chen ◽  
Qin Yao ◽  
Degang Ning ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Bombyx Mori ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Bombyx Mori Nucleopolyhedrovirus ◽  
Bacillus Subtilis Spore

scholarly journals Assembly of Multiple CotC Forms into the Bacillus subtilis Spore Coat

2004 ◽  
Vol 186 (4) ◽  
pp. 1129-1135 ◽  
Author(s):  
Rachele Isticato ◽  
Giovanni Esposito ◽  
Rita Zilhão ◽  
Sofia Nolasco ◽  
Giuseppina Cangiano ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Posttranslational Modifications ◽  
Mother Cell ◽  
Spore Coat ◽  
Spore Surface ◽  
Subtilis Spore ◽  
Cell Compartment ◽  
Bacillus Subtilis Spore ◽  
Molecular Masses

ABSTRACT We report evidence that the CotC polypeptide, a previously identified component of the Bacillus subtilis spore coat, is assembled into at least four distinct forms. Two of these, having molecular masses of 12 and 21 kDa, appeared 8 h after the onset of sporulation and were probably assembled on the forming spore immediately after their synthesis, since no accumulation of either of them was detected in the mother cell compartment, where their synthesis occurs. The other two components, 12.5 and 30 kDa, were generated 2 h later and were probably the products of posttranslational modifications of the two early forms occurring directly on the coat surface during spore maturation. None of the CotC forms was found either on the spore coat or in the mother cell compartment of a cotH mutant. This indicates that CotH serves a dual role of stabilizing the early forms of CotC and promoting the assembly of both early and late forms on the spore surface.

scholarly journals Temporal and spatial regulation of protein cross-linking by the pre-assembled substrates of a Bacillus subtilis spore coat transglutaminase

PLoS Genetics ◽  
2019 ◽  
Vol 15 (4) ◽  
pp. e1007912 ◽  
Author(s):  
Catarina G. Fernandes ◽  
Diogo Martins ◽  
Guillem Hernandez ◽  
Ana L. Sousa ◽  
Carolina Freitas ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Cross Linking ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Spatial Regulation ◽  
Bacillus Subtilis Spore ◽  
Temporal And Spatial ◽  
Protein Cross Linking

scholarly journals Localization of Proteins to Different Layers and Regions of Bacillus subtilis Spore Coats

2009 ◽  
Vol 192 (2) ◽  
pp. 518-524 ◽  
Author(s):  
Daisuke Imamura ◽  
Ritsuko Kuwana ◽  
Hiromu Takamatsu ◽  
Kazuhito Watabe
Keyword(s):  
Bacillus Subtilis ◽  
Mother Cell ◽  
Fluorescent Proteins ◽  
Bacterial Spores ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Proximal Pole ◽  
Outer Coat ◽  
Outermost Layer ◽  
Bacillus Subtilis Spore

ABSTRACT Bacterial spores are encased in a multilayered proteinaceous shell known as the coat. In Bacillus subtilis, over 50 proteins are involved in spore coat assembly but the locations of these proteins in the spore coat are poorly understood. Here, we describe methods to estimate the positions of protein fusions to fluorescent proteins in the spore coat by using fluorescence microscopy. Our investigation suggested that CotD, CotF, CotT, GerQ, YaaH, YeeK, YmaG, YsnD, and YxeE are present in the inner coat and that CotA, CotB, CotC, and YtxO reside in the outer coat. In addition, CotZ and CgeA appeared in the outermost layer of the spore coat and were more abundant at the mother cell proximal pole of the forespore, whereas CotA and CotC were more abundant at the mother cell distal pole of the forespore. These polar localizations were observed both in sporangia prior to the release of the forespore from the mother cell and in mature spores after release. Moreover, CotB was observed at the middle of the spore as a ring- or spiral-like structure. Formation of this structure required cotG expression. Thus, we conclude not only that the spore coat is a multilayered assembly but also that it exhibits uneven spatial distribution of particular proteins.

scholarly journals Protein Supramolecular Structures: From Self-Assembly to Nanovaccine Design

Nanomaterials ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 1008 ◽  
Author(s):  
Ximena Zottig ◽  
Mélanie Côté-Cyr ◽  
Dominic Arpin ◽  
Denis Archambault ◽  
Steve Bourgault
Keyword(s):  
Immune Responses ◽  
Self Assembly ◽  
Molecular Level ◽  
Supramolecular Structures ◽  
Atomic Scale ◽  
Supramolecular Interactions ◽  
Protein Assemblies ◽  
Adaptive Immune ◽  
Self Assembling ◽  
Molecular Specificity

Life-inspired protein supramolecular assemblies have recently attracted considerable attention for the development of next-generation vaccines to fight against infectious diseases, as well as autoimmune diseases and cancer. Protein self-assembly enables atomic scale precision over the final architecture, with a remarkable diversity of structures and functionalities. Self-assembling protein nanovaccines are associated with numerous advantages, including biocompatibility, stability, molecular specificity and multivalency. Owing to their nanoscale size, proteinaceous nature, symmetrical organization and repetitive antigen display, protein assemblies closely mimic most invading pathogens, serving as danger signals for the immune system. Elucidating how the structural and physicochemical properties of the assemblies modulate the potency and the polarization of the immune responses is critical for bottom-up design of vaccines. In this context, this review briefly covers the fundamentals of supramolecular interactions involved in protein self-assembly and presents the strategies to design and functionalize these assemblies. Examples of advanced nanovaccines are presented, and properties of protein supramolecular structures enabling modulation of the immune responses are discussed. Combining the understanding of the self-assembly process at the molecular level with knowledge regarding the activation of the innate and adaptive immune responses will support the design of safe and effective nanovaccines.

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