Difference between revisions of "Carbohydrate Binding Module Family 70"

Latest revision as of 05:13, 30 October 2025

This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.

CAZy DB link
https://www.cazy.org/CBM70.html

Ligand specificities

The CBM70 family comprises members predominantly of bacterial origin [1]. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin [2].

Structural Features

CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the Streptococcus pneumoniae hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family. This groove, which is similar to the binding site observed in β-sandwich CBMs such as those in the CBM4 family, is the putative hyaluronan-binding site [3]. Structural studies and mutational analysis have identified key residues, including a conserved solvent-exposed tryptophan and several basic residues, that are essential for hyaluronan recognition, supporting its classification as a Type B CBM [1].

Figure 1. The fold of the hyaluronic acid binding molecule SpCBM70 from the Streptococcus pneumoniae hyaluronate lyase Hyl 4D0Q. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets [].

Functionalities

CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the Streptococcus genus, such as Hyl from the PL8 family [4, 5]. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix [6]. Infection by pathogens such as S. pneumoniae utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread [7]. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid [8]. Additionally, the CBM70 family member SrCBM70 has been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating its potential in diagnostic applications [2].

Family Firsts

First Identified: The first CBM70 module to be identified (SpCBM70) was from the S. pneumoniae hyaluronate lyase Hyl [1].
First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q [1].

References

Error fetching PMID 25100731:
Error fetching PMID 36395930:
Error fetching PMID 12079353:
Error fetching PMID 12833544:
Error fetching PMID 18838391:
Error fetching PMID 15214846:
Error fetching PMID 12130645:
Error fetching PMID 7719281:

Error fetching PMID 25100731: [Michael2014]
Error fetching PMID 36395930: [Xuanwei2022]
Error fetching PMID 12079353: [Alisdair2002]
Error fetching PMID 12833544: [Daniel2003]
Error fetching PMID 18838391: [Brandi2009]
Error fetching PMID 15214846: [Alisdair2004]
Error fetching PMID 12130645: [Luciane2002]
Error fetching PMID 7719281: [Kostyukova1995]

All Medline abstracts: PubMed

@@ Line 1: / Line 1: @@
 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: [[User:Menghui Sun|Menghui Sun]]
 * [[Responsible Curator]]:  [[User:Yaoguang Chang|Yaoguang Chang]]
@@ Line 18: / Line 17: @@
 == Ligand specificities ==
-Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.
+The CBM70 family comprises members predominantly of bacterial origin <cite>Michael2014</cite>. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Xuanwei2022</cite>.
-''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010 Armenta2017</cite>.
 == Structural Features ==
-''Content in this section should include, in paragraph form, a description of:''
+CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family. This groove, which is similar to the binding site observed in β-sandwich CBMs such as those in the CBM4 family, is the putative hyaluronan-binding site <cite>Alisdair2002</cite>. Structural studies and mutational analysis have identified key residues, including a conserved solvent-exposed tryptophan and several basic residues, that are essential for hyaluronan recognition, supporting its classification as a Type B CBM <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]
-* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)
-* '''Type:''' Include here Type A, B, or C and properties
-* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.
 == Functionalities ==
-''Content in this section should include, in paragraph form, a description of:''
+CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, the CBM70 family member SrCBM70 has been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating its potential in diagnostic applications <cite>Xuanwei2022</cite>.
-* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
-* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
-* '''Novel Applications:'''  Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.
 == Family Firsts ==
-;First Identified
+;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
-:Insert archetype here, possibly including ''very brief'' synopsis.
+;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.
-;First Structural Characterization
-:Insert archetype here, possibly including ''very brief'' synopsis.
 == References ==
 <biblio>
-#Cantarel2009 pmid=18838391
+#Michael2014 pmid=25100731
-#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].
-#Boraston2004 pmid=15214846
+#Xuanwei2022 pmid=36395930
-#Hashimoto2006 pmid=17131061
-#Shoseyov2006 pmid=16760304
+#Alisdair2002 pmid=12079353
-#Guillen2010 pmid=19908036
-#Armenta2017 pmid=28547780
+#Daniel2003 pmid=12833544
+#Brandi2009 pmid=18838391
+#Alisdair2004 pmid=15214846
+#Luciane2002 pmid=12130645
+#Kostyukova1995 pmid=7719281
 </biblio>
 <!-- Do not delete this Category tag -->
-[[Category:Carbohydrate Binding Module Families|CBM70]]
+[[Category:Carbohydrate Binding Module Families|CBM070]]
 <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. -->