The Experts below are selected from a list of 288657 Experts worldwide ranked by ideXlab platform
Lucy Shapiro - One of the best experts on this subject based on the ideXlab platform.
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topologically guided continuous Protein crystallization controls bacterial surface layer self assembly
Nature Communications, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Many bacteria and most archaea possess a crystalline Protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer Protein (SLP) from C. crescentus, we show that 2D Protein Self-Assembly is sufficient to build and maintain the S-layer in living cells by efficient Protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, Protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials. Bacteria assemble the surface layer (S-layer), a crystalline Protein coat surrounding the curved surface, using Protein Self-Assembly. Here authors image native and purified RsaA, the S-layer Protein from C. crescentus, and show that Protein crystallization alone is sufficient to assemble and maintain the S-layer in vivo.
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continuous topologically guided Protein crystallization controls bacterial surface layer self assembly
bioRxiv, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Abstract Bacteria assemble the cell envelope using localized enzymes to account for growth and division of a topologically complicated surface1–3. However, a regulatory pathway has not been identified for assembly and maintenance of the surface layer (S-layer), a 2D crystalline Protein coat surrounding the curved 3D surface of a variety of bacteria4,5. By specifically labeling, imaging, and tracking native and purified RsaA, the S-layer Protein (SLP) from C. crescentus, we show that Protein Self-Assembly alone is sufficient to assemble and maintain the S-layer in vivo. By monitoring the location of newly produced S-layer on the surface of living bacteria, we find that S-layer assembly occurs independently of the site of RsaA secretion and that localized production of new cell wall surface area alone is insufficient to explain S-layer assembly patterns. When the cell surface is devoid of a pre-existing S-layer, the location of S-layer assembly depends on the nucleation characteristics of SLP crystals, which grow by capturing RsaA molecules freely diffusing on the outer bacterial surface. Based on these observations, we propose a model of S-layer assembly whereby RsaA monomers are secreted randomly and diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated into growing 2D S-layer crystals. The complicated topology of the cell surface enables formation of defects, gaps, and grain boundaries within the S-layer lattice, thereby guiding the location of S-layer assembly without enzymatic assistance. This unsupervised mechanism poses unique challenges and advantages for designing treatments targeting cell surface structures or utilizing S-layers as self-assembling macromolecular nanomaterials. As an evolutionary driver, 2D Protein Self-Assembly rationalizes the exceptional S-layer subunit sequence and species diversity6.
Jonathan Herrmann - One of the best experts on this subject based on the ideXlab platform.
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topologically guided continuous Protein crystallization controls bacterial surface layer self assembly
Nature Communications, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Many bacteria and most archaea possess a crystalline Protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer Protein (SLP) from C. crescentus, we show that 2D Protein Self-Assembly is sufficient to build and maintain the S-layer in living cells by efficient Protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, Protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials. Bacteria assemble the surface layer (S-layer), a crystalline Protein coat surrounding the curved surface, using Protein Self-Assembly. Here authors image native and purified RsaA, the S-layer Protein from C. crescentus, and show that Protein crystallization alone is sufficient to assemble and maintain the S-layer in vivo.
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continuous topologically guided Protein crystallization controls bacterial surface layer self assembly
bioRxiv, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Abstract Bacteria assemble the cell envelope using localized enzymes to account for growth and division of a topologically complicated surface1–3. However, a regulatory pathway has not been identified for assembly and maintenance of the surface layer (S-layer), a 2D crystalline Protein coat surrounding the curved 3D surface of a variety of bacteria4,5. By specifically labeling, imaging, and tracking native and purified RsaA, the S-layer Protein (SLP) from C. crescentus, we show that Protein Self-Assembly alone is sufficient to assemble and maintain the S-layer in vivo. By monitoring the location of newly produced S-layer on the surface of living bacteria, we find that S-layer assembly occurs independently of the site of RsaA secretion and that localized production of new cell wall surface area alone is insufficient to explain S-layer assembly patterns. When the cell surface is devoid of a pre-existing S-layer, the location of S-layer assembly depends on the nucleation characteristics of SLP crystals, which grow by capturing RsaA molecules freely diffusing on the outer bacterial surface. Based on these observations, we propose a model of S-layer assembly whereby RsaA monomers are secreted randomly and diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated into growing 2D S-layer crystals. The complicated topology of the cell surface enables formation of defects, gaps, and grain boundaries within the S-layer lattice, thereby guiding the location of S-layer assembly without enzymatic assistance. This unsupervised mechanism poses unique challenges and advantages for designing treatments targeting cell surface structures or utilizing S-layers as self-assembling macromolecular nanomaterials. As an evolutionary driver, 2D Protein Self-Assembly rationalizes the exceptional S-layer subunit sequence and species diversity6.
Fatemeh Jabbarpour - One of the best experts on this subject based on the ideXlab platform.
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topologically guided continuous Protein crystallization controls bacterial surface layer self assembly
Nature Communications, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Many bacteria and most archaea possess a crystalline Protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer Protein (SLP) from C. crescentus, we show that 2D Protein Self-Assembly is sufficient to build and maintain the S-layer in living cells by efficient Protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, Protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials. Bacteria assemble the surface layer (S-layer), a crystalline Protein coat surrounding the curved surface, using Protein Self-Assembly. Here authors image native and purified RsaA, the S-layer Protein from C. crescentus, and show that Protein crystallization alone is sufficient to assemble and maintain the S-layer in vivo.
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continuous topologically guided Protein crystallization controls bacterial surface layer self assembly
bioRxiv, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Abstract Bacteria assemble the cell envelope using localized enzymes to account for growth and division of a topologically complicated surface1–3. However, a regulatory pathway has not been identified for assembly and maintenance of the surface layer (S-layer), a 2D crystalline Protein coat surrounding the curved 3D surface of a variety of bacteria4,5. By specifically labeling, imaging, and tracking native and purified RsaA, the S-layer Protein (SLP) from C. crescentus, we show that Protein Self-Assembly alone is sufficient to assemble and maintain the S-layer in vivo. By monitoring the location of newly produced S-layer on the surface of living bacteria, we find that S-layer assembly occurs independently of the site of RsaA secretion and that localized production of new cell wall surface area alone is insufficient to explain S-layer assembly patterns. When the cell surface is devoid of a pre-existing S-layer, the location of S-layer assembly depends on the nucleation characteristics of SLP crystals, which grow by capturing RsaA molecules freely diffusing on the outer bacterial surface. Based on these observations, we propose a model of S-layer assembly whereby RsaA monomers are secreted randomly and diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated into growing 2D S-layer crystals. The complicated topology of the cell surface enables formation of defects, gaps, and grain boundaries within the S-layer lattice, thereby guiding the location of S-layer assembly without enzymatic assistance. This unsupervised mechanism poses unique challenges and advantages for designing treatments targeting cell surface structures or utilizing S-layers as self-assembling macromolecular nanomaterials. As an evolutionary driver, 2D Protein Self-Assembly rationalizes the exceptional S-layer subunit sequence and species diversity6.
Colin J Comerci - One of the best experts on this subject based on the ideXlab platform.
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topologically guided continuous Protein crystallization controls bacterial surface layer self assembly
Nature Communications, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Many bacteria and most archaea possess a crystalline Protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer Protein (SLP) from C. crescentus, we show that 2D Protein Self-Assembly is sufficient to build and maintain the S-layer in living cells by efficient Protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, Protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials. Bacteria assemble the surface layer (S-layer), a crystalline Protein coat surrounding the curved surface, using Protein Self-Assembly. Here authors image native and purified RsaA, the S-layer Protein from C. crescentus, and show that Protein crystallization alone is sufficient to assemble and maintain the S-layer in vivo.
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continuous topologically guided Protein crystallization controls bacterial surface layer self assembly
bioRxiv, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Abstract Bacteria assemble the cell envelope using localized enzymes to account for growth and division of a topologically complicated surface1–3. However, a regulatory pathway has not been identified for assembly and maintenance of the surface layer (S-layer), a 2D crystalline Protein coat surrounding the curved 3D surface of a variety of bacteria4,5. By specifically labeling, imaging, and tracking native and purified RsaA, the S-layer Protein (SLP) from C. crescentus, we show that Protein Self-Assembly alone is sufficient to assemble and maintain the S-layer in vivo. By monitoring the location of newly produced S-layer on the surface of living bacteria, we find that S-layer assembly occurs independently of the site of RsaA secretion and that localized production of new cell wall surface area alone is insufficient to explain S-layer assembly patterns. When the cell surface is devoid of a pre-existing S-layer, the location of S-layer assembly depends on the nucleation characteristics of SLP crystals, which grow by capturing RsaA molecules freely diffusing on the outer bacterial surface. Based on these observations, we propose a model of S-layer assembly whereby RsaA monomers are secreted randomly and diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated into growing 2D S-layer crystals. The complicated topology of the cell surface enables formation of defects, gaps, and grain boundaries within the S-layer lattice, thereby guiding the location of S-layer assembly without enzymatic assistance. This unsupervised mechanism poses unique challenges and advantages for designing treatments targeting cell surface structures or utilizing S-layers as self-assembling macromolecular nanomaterials. As an evolutionary driver, 2D Protein Self-Assembly rationalizes the exceptional S-layer subunit sequence and species diversity6.
Joshua Yoon - One of the best experts on this subject based on the ideXlab platform.
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topologically guided continuous Protein crystallization controls bacterial surface layer self assembly
Nature Communications, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Many bacteria and most archaea possess a crystalline Protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer Protein (SLP) from C. crescentus, we show that 2D Protein Self-Assembly is sufficient to build and maintain the S-layer in living cells by efficient Protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, Protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials. Bacteria assemble the surface layer (S-layer), a crystalline Protein coat surrounding the curved surface, using Protein Self-Assembly. Here authors image native and purified RsaA, the S-layer Protein from C. crescentus, and show that Protein crystallization alone is sufficient to assemble and maintain the S-layer in vivo.
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continuous topologically guided Protein crystallization controls bacterial surface layer self assembly
bioRxiv, 2019Co-Authors: Colin J Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F Nomellini, John Smit, Lucy ShapiroAbstract:Abstract Bacteria assemble the cell envelope using localized enzymes to account for growth and division of a topologically complicated surface1–3. However, a regulatory pathway has not been identified for assembly and maintenance of the surface layer (S-layer), a 2D crystalline Protein coat surrounding the curved 3D surface of a variety of bacteria4,5. By specifically labeling, imaging, and tracking native and purified RsaA, the S-layer Protein (SLP) from C. crescentus, we show that Protein Self-Assembly alone is sufficient to assemble and maintain the S-layer in vivo. By monitoring the location of newly produced S-layer on the surface of living bacteria, we find that S-layer assembly occurs independently of the site of RsaA secretion and that localized production of new cell wall surface area alone is insufficient to explain S-layer assembly patterns. When the cell surface is devoid of a pre-existing S-layer, the location of S-layer assembly depends on the nucleation characteristics of SLP crystals, which grow by capturing RsaA molecules freely diffusing on the outer bacterial surface. Based on these observations, we propose a model of S-layer assembly whereby RsaA monomers are secreted randomly and diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated into growing 2D S-layer crystals. The complicated topology of the cell surface enables formation of defects, gaps, and grain boundaries within the S-layer lattice, thereby guiding the location of S-layer assembly without enzymatic assistance. This unsupervised mechanism poses unique challenges and advantages for designing treatments targeting cell surface structures or utilizing S-layers as self-assembling macromolecular nanomaterials. As an evolutionary driver, 2D Protein Self-Assembly rationalizes the exceptional S-layer subunit sequence and species diversity6.
