Carbohydrate Binding Module Family 55 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:15:45Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Elizabeth Ficko-Blean: /* Ligand specificities */

2019-10-24T07:12:21Z

Ligand specificities

Elizabeth Ficko-Blean at 07:11, 24 October 2019

2019-10-24T07:11:26Z

Elizabeth Ficko-Blean at 14:42, 22 October 2019

2019-10-22T14:42:33Z

Elizabeth Ficko-Blean at 14:40, 22 October 2019

2019-10-22T14:40:08Z

Elizabeth Ficko-Blean at 09:44, 15 October 2019

2019-10-15T09:44:20Z

Elizabeth Ficko-Blean at 09:31, 15 October 2019

2019-10-15T09:31:41Z

Elizabeth Ficko-Blean at 09:23, 15 October 2019

2019-10-15T09:23:59Z

Elizabeth Ficko-Blean at 09:22, 15 October 2019

2019-10-15T09:22:49Z

Elizabeth Ficko-Blean at 09:09, 15 October 2019

2019-10-15T09:09:36Z

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]: ^^^John Samuelson^^^
+* [[Author]]: [[User:John Samuelson|John Samuelson]]
-* [[Responsible Curator]]:  ^^^Elizabeth Ficko-Blean^^^
+* [[Responsible Curator]]:  [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
 ----

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 == Ligand specificities ==
 [[File:CBM55.png|thumb|150px|right|'''Figure 1.''' ''Entamoeba'' proteins containing CBM55.]]
-A CBM55, which is ~60-aa long and contains eight cysteines in conserved positions, was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess (Figure 1) <cite>Van_Dellen2002,de_la_Vega1997</cite>. CBM55 members are also present at the N-termini of Jessie 3 lectins, which contain a self-aggregating (daub) domain, while CBM55 is the only domain in Jessie 1 and Jessie 2 lectins <cite>Chatterjee2009</cite>. CBM55 members are present in [[GH18]] chitinases and Jessie lectins of all five ''Entamoeba'' species that have been sequenced. CBM55 members are absent from other eukaryotes, eubacteria, and archaea, and so the CBM55 motif appears to have been “created from scratch” by the common ancestor to ''Entamoebae''.  CBM55 members of ''E. histolytica'' chitinase, Jessie 1, and Jessie 3 lectins, each produced by gene expression under a constitutive actin promoter in transformed trophozoites, demonstrated binding to chitin beads <cite>Van_Dellen2002</cite>.
+A CBM55, which is ~60-aa long and contains eight cysteines in conserved positions, was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess (Figure 1) <cite>Van_Dellen2002,de_la_Vega1997</cite>. CBM55 members are also present at the N-termini of Jessie 3 lectins, which contain a self-aggregating (daub) domain, while CBM55 is the only domain in Jessie 1 and Jessie 2 lectins <cite>Chatterjee2009</cite>. CBM55 members are present in [[GH18]] chitinases and Jessie lectins of all five ''Entamoeba'' species that have been sequenced <cite>Aurrecoechea2011</cite>. CBM55 members are absent from other eukaryotes, eubacteria, and archaea, and so the CBM55 motif appears to have been “created from scratch” by the common ancestor to ''Entamoebae''.  CBM55 members of ''E. histolytica'' chitinase, Jessie 1, and Jessie 3 lectins, each produced by gene expression under a constitutive actin promoter in transformed trophozoites, demonstrated binding to chitin beads <cite>Van_Dellen2002</cite>.
 == Structural Features ==

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: ^^^John Samuelson^^^
 * [[Responsible Curator]]:  ^^^Elizabeth Ficko-Blean^^^
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 #Samuelson2011 pmid=20934911
 #Ehrenkaufer2013 pmid=23889909
 </biblio>
 [[Category:Carbohydrate Binding Module Families|CBM055]]

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 == Ligand specificities ==
 [[File:CBM55.png|thumb|150px|right|'''Figure 1.''' ''Entamoeba'' proteins containing CBM55.]]
-A CBM55, which is ~60-aa long and contains eight cysteines in conserved positions, was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess (Figure 1) <cite>Van_Dellen2002,de_la_Vega1997</cite>. CBM55 members are also present at the N-termini of Jessie 3 lectins, which contain a self-aggregating (daub) domain, while CBM55 is the only domain in Jessie 1 and Jessie 2 lectins [3]. CBM55 members are present in [[GH18]] chitinases and Jessie lectins of all five ''Entamoeba'' species that have been sequenced. CBM55 members are absent from other eukaryotes, eubacteria, and archaea, and so the CBM55 motif appears to have been “created from scratch” by the common ancestor to ''Entamoebae''.  CBM55 members of ''E. histolytica'' chitinase, Jessie 1, and Jessie 3 lectins, each produced by gene expression under a constitutive actin promoter in transformed trophozoites, demonstrated binding to chitin beads <cite>Van_Dellen2002</cite>.
+A CBM55, which is ~60-aa long and contains eight cysteines in conserved positions, was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess (Figure 1) <cite>Van_Dellen2002,de_la_Vega1997</cite>. CBM55 members are also present at the N-termini of Jessie 3 lectins, which contain a self-aggregating (daub) domain, while CBM55 is the only domain in Jessie 1 and Jessie 2 lectins <cite>Chatterjee2009</cite>. CBM55 members are present in [[GH18]] chitinases and Jessie lectins of all five ''Entamoeba'' species that have been sequenced. CBM55 members are absent from other eukaryotes, eubacteria, and archaea, and so the CBM55 motif appears to have been “created from scratch” by the common ancestor to ''Entamoebae''.  CBM55 members of ''E. histolytica'' chitinase, Jessie 1, and Jessie 3 lectins, each produced by gene expression under a constitutive actin promoter in transformed trophozoites, demonstrated binding to chitin beads <cite>Van_Dellen2002</cite>.

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 == Ligand specificities ==
-[[File:CBM55.png|thumb|200px|right|'''Figure 1.''' ''Entamoeba'' proteins containing CBM55.]]
+[[File:CBM55.png|thumb|150px|right|'''Figure 1.''' ''Entamoeba'' proteins containing CBM55.]]
 A CBM55, which is ~60-aa long and contains eight cysteines in conserved positions, was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'', the protist that causes dysentery and liver abscess (Figure 1) <cite>Van_Dellen2002,de_la_Vega1997</cite>. CBM55 members are also present at the N-termini of Jessie 3 lectins, which contain a self-aggregating (daub) domain, while CBM55 is the only domain in Jessie 1 and Jessie 2 lectins [3]. CBM55 members are present in [[GH18]] chitinases and Jessie lectins of all five ''Entamoeba'' species that have been sequenced. CBM55 members are absent from other eukaryotes, eubacteria, and archaea, and so the CBM55 motif appears to have been “created from scratch” by the common ancestor to ''Entamoebae''.  CBM55 members of ''E. histolytica'' chitinase, Jessie 1, and Jessie 3 lectins, each produced by gene expression under a constitutive actin promoter in transformed trophozoites, demonstrated binding to chitin beads <cite>Van_Dellen2002</cite>.

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 :A CBM55 was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'' <cite>Van_Dellen2002, de_la_Vega1997</cite>.
 ;First Structural Characterization
-:There is no structure available at this time.
+:There is no structure available.
 == References ==

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 == Family Firsts ==
 ;First Identified
-:A CBM55 was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica''<cite>Van_Dellen2002, de_la_Vega1997</cite>.
+:A CBM55 was first identified at the N-terminus of the [[GH18]] chitinase of ''Entamoeba histolytica'' <cite>Van_Dellen2002, de_la_Vega1997</cite>.
 ;First Structural Characterization
-:Insert archetype here, possibly including ''very brief'' synopsis.
+:There is no structure available at this time.
 == References ==

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 In the human intestine, motile ''E. histolytica'' trophozoites phagocytose bacteria and/or attach to and take bites out of (trogocytose) host epithelial cells <cite>Ralston2014</cite>.  Alternatively, trophozoites form cysts, which have chitin and deacetylated chitin (chitosan) in their wall <cite>Van_Dellen2006a,Das2006</cite>. ''E. histolytica'' is transmitted when cysts are shed in the feces and contaminate food, soil, or water. When cysts are ingested, trophozoites escape their wall and are released into the intestine, completing the life cycle.
 The most abundant proteins identified by mass spectrometry of cyst walls of ''E. invadens'', a model for the human pathogen, are chitinases, Jessie 3 lectins, and Jacob lectins, which contain two or three chitin-binding domains each with six conserved cysteines <cite>Frisardi2000,Van_Dellen2006b</cite>. Mass spectrometry and specific antibodies have confirmed the presence of chitinase, Jessie lectins, and Jacob lectins in cyst walls of ''E. histolytica'', the human pathogen <cite>Ghosh2010,Ali2012</cite>.
-Cyst wall proteins, which are absent from trophozoites but abundant in cysts, coat chitin fibrils and protect them from bacterial chitinases, which are ubiquitous in the environment <cite>Samuelson2011,Ehrenkaufer2013</cite>. One function of CBM55 is to retain chitinase and Jessie 3 lectins in the cyst wall. The chitinase is likely involved in remodeling the cyst wall during encystation and breaking down the cyst wall when the trophozoite escapes during excystation. The daub domain of Jessie 3, which forms a biofilm when expressed as a maltose-binding protein in the periplasm of bacteria, makes the cyst wall impenetrable to molecules as small as one kilodalton [3].
+Cyst wall proteins, which are absent from trophozoites but abundant in cysts, coat chitin fibrils and protect them from bacterial chitinases, which are ubiquitous in the environment <cite>Samuelson2011,Ehrenkaufer2013</cite>. One function of CBM55 is to retain chitinase and Jessie 3 lectins in the cyst wall. The chitinase is likely involved in remodeling the cyst wall during encystation and breaking down the cyst wall when the trophozoite escapes during excystation. The daub domain of Jessie 3, which forms a biofilm when produced recombinantly as a fusion with maltose-binding protein in the periplasm of bacteria, makes the cyst wall impenetrable to molecules as small as one kilodalton <cite>Chatterjee2009</cite>.
 == Family Firsts ==