Carbohydrate Binding Module Family 47 - Revision history

Wenwen Tao: /* Ligand specificities */

2024-11-21T08:28:02Z

Ligand specificities

Wenwen Tao: /* Ligand specificities */

2024-11-21T08:26:24Z

Ligand specificities

Wenwen Tao: /* Ligand specificities */

2024-11-21T08:25:29Z

Ligand specificities

Wenwen Tao: /* Functionalities */

2024-11-21T08:21:35Z

Functionalities

Wenwen Tao: /* Functionalities */

2024-11-21T06:42:07Z

Functionalities

Wenwen Tao: /* Structural Features */

2024-11-21T06:35:29Z

Structural Features

Wenwen Tao: /* Structural Features */

2024-11-21T06:27:28Z

Structural Features

Wenwen Tao: /* Structural Features */

2024-11-21T06:26:23Z

Structural Features

Wenwen Tao: /* Ligand specificities */

2024-11-21T06:15:11Z

Ligand specificities

Wenwen Tao: /* Ligand specificities */

2024-11-21T06:13:38Z

Ligand specificities

@@ Line 18: / Line 18: @@
 == Ligand specificities ==
-The characterization of the C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin Sp[[GH98]], originating from the fucose utilization operon in ''Streptococcus pneumoniae'', was the founding member of the CBM47 family <cite>Boraston2006</cite>. However, the ''Anguilla anguilla'' agglutinin (AAA) derived from the European eel, which was characterized earlier and is also classified as an F-type lectin <cite>Bianchet2002</cite>, is also included in the CBM47 family. Several other members of the CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite>, and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to carbohydrates containing fucose, which could be oligosaccharides (often trisaccharides or smaller) or parts of polysaccharides, such as the AAA, and a portion of CBM47 members have demonstrated binding to glycans containing galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, another CBM47 domain (named WfCBM47) was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<Sup>T</Sup>, which is appended to the [[GH168]] family sequence. The CBM binds to the various sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.
+The characterization of the C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin Sp[[GH98]], originating from the fucose utilization operon in ''Streptococcus pneumoniae'', was the founding member of the CBM47 family <cite>Boraston2006</cite>. However, the ''Anguilla anguilla'' agglutinin (AAA) derived from the European eel, which was characterized earlier <cite>Bianchet2002</cite>, is also included in the CBM47 family. Several other members of the CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite>, and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to carbohydrates containing fucose, which could be oligosaccharides (often trisaccharides or smaller) or parts of polysaccharides, such as the AAA, and a portion of CBM47 members have demonstrated binding to glycans containing galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, another CBM47 domain (named WfCBM47) was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<Sup>T</Sup>, which is appended to the [[GH168]] family sequence. The CBM binds to the various sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.
 == Structural Features ==

@@ Line 18: / Line 18: @@
 == Ligand specificities ==
-The characterization of the C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin Sp[[GH98]], originating from the fucose utilization operon in ''Streptococcus pneumoniae'', was the founding member of the CBM47 family <cite>Boraston2006</cite>. However, the ''Anguilla anguilla'' agglutinin (AAA) derived from the European eel, which was characterized earlier which was characterized earlier and is also classified as an F-type lectin <cite>Bianchet2002</cite>, is also included in the CBM47 family. Several other members of the CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite>, and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to carbohydrates containing fucose, which could be oligosaccharides (often trisaccharides or smaller) or parts of polysaccharides, such as the AAA, and a portion of CBM47 members have demonstrated binding to glycans containing galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, another CBM47 domain (named WfCBM47) was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<Sup>T</Sup>, which is appended to the [[GH168]] family sequence. The CBM binds to the various sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.
+The characterization of the C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin Sp[[GH98]], originating from the fucose utilization operon in ''Streptococcus pneumoniae'', was the founding member of the CBM47 family <cite>Boraston2006</cite>. However, the ''Anguilla anguilla'' agglutinin (AAA) derived from the European eel, which was characterized earlier and is also classified as an F-type lectin <cite>Bianchet2002</cite>, is also included in the CBM47 family. Several other members of the CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite>, and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to carbohydrates containing fucose, which could be oligosaccharides (often trisaccharides or smaller) or parts of polysaccharides, such as the AAA, and a portion of CBM47 members have demonstrated binding to glycans containing galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, another CBM47 domain (named WfCBM47) was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<Sup>T</Sup>, which is appended to the [[GH168]] family sequence. The CBM binds to the various sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.
 == Structural Features ==

@@ Line 18: / Line 18: @@
 == Ligand specificities ==
-The characterization of the C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin Sp[[GH98]], originating from the fucose utilization operon in ''Streptococcus pneumoniae'', first defined the CBM47 family <cite>Boraston2006</cite>. The CBM47 family was created after the discovery of SpX-1.2.3. ''Anguilla anguilla'' agglutinin (AAA), derived from the European eel, which was characterized earlier and is also classified as an F-type lectin <cite>Bianchet2002</cite>, is also included in the CBM47 family. Several other members of the CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite>, and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to carbohydrates containing fucose, which could be oligosaccharides (often trisaccharides or smaller) or parts of polysaccharides, such as the AAA, and a portion of CBM47 members have demonstrated binding to glycans containing galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, another CBM47 domain (named WfCBM47) was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<Sup>T</Sup>, which is appended to the [[GH168]] family sequence. The CBM binds to the various sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.
+The characterization of the C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin Sp[[GH98]], originating from the fucose utilization operon in ''Streptococcus pneumoniae'', was the founding member of the CBM47 family <cite>Boraston2006</cite>. However, the ''Anguilla anguilla'' agglutinin (AAA) derived from the European eel, which was characterized earlier which was characterized earlier and is also classified as an F-type lectin <cite>Bianchet2002</cite>, is also included in the CBM47 family. Several other members of the CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite>, and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to carbohydrates containing fucose, which could be oligosaccharides (often trisaccharides or smaller) or parts of polysaccharides, such as the AAA, and a portion of CBM47 members have demonstrated binding to glycans containing galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, another CBM47 domain (named WfCBM47) was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<Sup>T</Sup>, which is appended to the [[GH168]] family sequence. The CBM binds to the various sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.
 == Structural Features ==

@@ Line 29: / Line 29: @@
 Both LLY<sup>lec</sup> and SpX-1.2.3 are associated with bacterial toxins belonging to the [[GH98]] family. Under physiological conditions, these proteins form aggregates that bind to glycoproteins or glycolipids on the cell membrane. These aggregates, through protein-protein interactions with the toxin, steer the toxin to accumulate at fucose-rich sites on the cell surface, thereby enhancing the pore-forming activity of the toxins and accelerating cell lysis. Based on the binding specificity to fucoidan, the fluorescein isothiocyanate-labeled SpX-1.2.3 triplet was applied for in situ visualization of mouse lung tissue sections <cite>Boraston2006 Feil2012</cite>.
-Sulfated fucans, as one of the structural molecules in the sea cucumber body wall, play an important role in the formation of the structure and quality of sea cucumber. A fluorescent probe was constructed by fusing WfCBM47 with a green fluorescent protein, based on which the ''in situ'' visualization of sulfated fucan in the sea cucumber (''Apostichopus japonicus'') body wall was implemented for the first time by utilizing the probe <cite>Mei2022</cite>. It was observed that sulfated fucan existed as a ground substance in the extracellular matrix.
+Sulfated fucans, as one of the structural molecules in the sea cucumber body wall, play an important role in the formation of the structure and quality of sea cucumber. A fluorescent probe was constructed by fusing WfCBM47 with a green fluorescent protein, based on which the ''in situ'' visualization of sulfated fucan in the sea cucumber (''Apostichopus japonicus'') body wall was implemented for the first time <cite>Mei2022</cite>. It was observed that sulfated fucan existed as a ground substance in the extracellular matrix.
 == Family Firsts ==

@@ Line 25: / Line 25: @@
 == Functionalities ==
-The AAA, discovered in the serum of European eel, and MsaFBP32, isolated from the plasma of the striped bass ''Morone saxatilis'', participate in the recognition of bacterial lipopolysaccharides by the animal innate immune system <cite>Bianchet2002 Bianchet2010</cite>.
+The AAA, discovered in the serum of European eel, and MsaFBP32, isolated from the plasma of the striped bass ''Morone saxatilis'', participate in the recognition of bacterial lipopolysaccharides by the animal innate immune system. For instance, they are capable of recognizing and binding to specific carbohydrate structures on the surfaces of pathogens, such as L-fucose and D-galactose methylether derivatives, serving as vital immune recognition molecules. Furthermore, they can also recognize H and Le<sup>a</sup> antigens, which are used in determining ABO and Lewis blood group types <cite>Bianchet2002 Bianchet2010</cite>.
-Both LLY<sup>lec</sup> and SpX-1.2.3 are associated with bacterial toxins belonging to [[GH98]] family. Under physiological conditions, these proteins form aggregates that bind to glycoproteins or glycolipids on the cell membrane and insert into the membrane, thereby enhancing the pore-forming activity of the toxins and accelerating cell lysis. Based on the binding specificity to fucoidan, the fluorescein isothiocyanate-labeled SpX-1.2.3 triplet was applied for in situ visualization of mouse lung tissue sections <cite>Boraston2006 Feil2012</cite>.
+Both LLY<sup>lec</sup> and SpX-1.2.3 are associated with bacterial toxins belonging to the [[GH98]] family. Under physiological conditions, these proteins form aggregates that bind to glycoproteins or glycolipids on the cell membrane. These aggregates, through protein-protein interactions with the toxin, steer the toxin to accumulate at fucose-rich sites on the cell surface, thereby enhancing the pore-forming activity of the toxins and accelerating cell lysis. Based on the binding specificity to fucoidan, the fluorescein isothiocyanate-labeled SpX-1.2.3 triplet was applied for in situ visualization of mouse lung tissue sections <cite>Boraston2006 Feil2012</cite>.
-Sulfated fucans, constituting a pivotal structural component within the body wall of sea cucumbers, are important to the overall architecture and quality of these marine invertebrates. To evaluate the feasibility of WfCBM47 as a tool in the ''in situ'' investigation of sulfated fucan, a fluorescent probe was constructed by fusing WfCBM47 with a green fluorescent protein. The ''in situ'' visualization of sulfated fucan in the sea cucumber (''Apostichopus japonicus'') body wall was implemented for the first time by utilizing the probe <cite>Mei2022</cite>.
+Sulfated fucans, as one of the structural molecules in the sea cucumber body wall, play an important role in the formation of the structure and quality of sea cucumber. A fluorescent probe was constructed by fusing WfCBM47 with a green fluorescent protein, based on which the ''in situ'' visualization of sulfated fucan in the sea cucumber (''Apostichopus japonicus'') body wall was implemented for the first time by utilizing the probe <cite>Mei2022</cite>. It was observed that sulfated fucan existed as a ground substance in the extracellular matrix.
 == Family Firsts ==

@@ Line 21: / Line 21: @@
 == Structural Features ==
-[[File:CBM47_Fig.1.png|thumb|350px|right|'''Figure 1. Crystal structure of (A) AAA ([{{PDBlink}}1k12 PDB 1k12]) and (B) SpX-1.''' The strand, helix, loop, Ca<sup>2+</sup> and Cl<sup>-</sup> are colored in cyan, yellow, white ,green and orange respectively.]]
+[[File:CBM47_Fig.1.png|thumb|350px|right|'''Figure 1. Crystal structure of (A) AAA ([{{PDBlink}}1k12 PDB 1k12]) and (B) SpX-1 ([{{PDBlink}}2j1r PDB 2j1r]).''' The strand, helix, loop, Ca<sup>2+</sup> and Cl<sup>-</sup> are colored in cyan, yellow, white ,green and orange respectively.]]
 All the fucose-binding proteins, SpX-1 ([{{PDBlink}}2j1r PDB 2j1r]), SpX-3 ([{{PDBlink}}2j22 PDB 2j22]) and AAA ([{{PDBlink}}1k12 PDB 1k12]), have had their tertiary structures determined through X-ray crystallography <cite>Boraston2006 Bianchet2002</cite>. The core structures of the CBM47 family exhibit remarkable similarity, adopting an eight-stranded β-sandwich fold, which is comprised of a five-stranded anti-parallel β-sheet on one side and a three-stranded anti-parallel β-sheet on the other <cite>Boraston2006 Bianchet2002 Bianchet2010 Feil2012 Lawrence2012</cite>. Additionally, CBM47 typically exists as a dimer or trimer under physiological conditions, with Ca<sup>2+</sup> playing a pivotal role in maintaining its conformational stability <cite>Boraston2006 Feil2012 Bianchet2002</cite>. The CBM47 family recognizes and binds glycans through shallow grooves located within their complementarity-determining regions (CDRs); these variable loops have been shown to exhibit a high degree of sequence and conformational variability among different CBM47s, enabling them to recognize diverse ligands <cite>Feil2012</cite>. For instance, LLY<sup>lec</sup> and SpX-1 reveal smaller differences among their loops, permitting them to bind to a wide array of Lewis blood group oligosaccharides <cite>Boraston2006 Feil2012</cite>. While AAA features a particularly longer and rigid loop, which may account for its preference to form complexes with type 1 antigens while lacking affinity for type 2 antigens <cite>Bianchet2002</cite>. Additionally, the loop regions of MsaFBP32 are shorter than those of AAA, resulting in fewer steric hindrances, which facilitates easier contact with oligosaccharide molecules and the formation of stable binding, but concurrently may reduce binding specificity <cite>Bianchet2010</cite>.