Difference between revisions of "Part:BBa K3861001"
 
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<partinfo>BBa_K3861001 short</partinfo>
 
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N-terminal domain of the <i> Burkholderia cenocepacia </i> lectin, BC2L-C. As a part of our project, this lectin will be displayed at the surface of <i>Salmonella Typhimurium </i> derived minicells and mediate cancer cell recognition.  
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<i> Burkholderia cenocepacia </i>, a Gram-positive opportunistic bacterial species, possess several virulence factors. Among them are four soluble lectins which are used for host cell recognition and adhesion. One of these lectins is the lectin BC2L. This lectin has been shown to be a “super” lectin, containing two lectin domains, at the C- and N-terminus. These two lectin domains have been shown to have specificity for different substrates and have been proposed to mediate cell adhesion by conjugating with the bacterial membrane and the host's membrane.<sup>1</sup>
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The N-terminus builds a homotrimer that binds specifically to carbohydrates containing fucose at the interface between monomers.<sup>2</sup><br>
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In 2018 a study by Shimomura et al. (2018) determined that the N-terminus of the BC2L-C lectin could bind to a representative pancreatic cancer cell line (Capan-1) and be used as a delivery system by conjugating it with a drug<sup>3</sup>. It has additionally been shown that this lectin has the potential to recognize other cancer types, such as colorectal cancer<sup>4</sup>, breast cancer<sup>5</sup> and tumorigenic pluripotent stem cells<sup>6</sup>.<br>
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As a part of our project “TargetTaxi”, we aimed to utilize this lectin for cancer cell recognition and adhesion. The lectin would be exposed at the surface of Salmonella-derived minicells and mediate their binding. The surface display will be mediated by its fusion with a surface display system regulated by AIDA and FimH.  
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<partinfo>BBa_K3861001 parameters</partinfo>
 
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==='''References'''===
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1. Šulák, O. et al. Burkholderia cenocepacia bc2l-c is a super lectin with dual specificity and proinflammatory activity. PLoS Pathog. (2011) doi:10.1371/journal.ppat.1002238.<br>
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2. Šulák, O. et al. A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens. Structure (2010) doi:10.1016/j.str.2009.10.021.<br>
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3. Shimomura, O. et al. A novel therapeutic strategy for pancreatic cancer: Targeting cell surface glycan using rBC2LC-N lectin-drug conjugate (LDC). Mol. Cancer Ther. (2018) doi:10.1158/1535-7163.MCT-17-0232.<br>
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4. Kitaguchi, D. et al. Lectin drug conjugate therapy for colorectal cancer. Cancer Sci. (2020) doi:10.1111/cas.14687.<br>
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5. Mawaribuchi, S. et al. rBC2LCN lectin as a potential probe of early-stage HER2-positive breast carcinoma. FEBS Open Bio (2020) doi:10.1002/2211-5463.12852.<br>
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6. Haramoto, Y. et al. A technique for removing tumourigenic pluripotent stem cells using rBC2LCN lectin. Regen. Ther. (2020) doi:10.1016/j.reth.2020.03.017.<br>

Latest revision as of 20:19, 20 October 2021


rBC2LCN

Burkholderia cenocepacia , a Gram-positive opportunistic bacterial species, possess several virulence factors. Among them are four soluble lectins which are used for host cell recognition and adhesion. One of these lectins is the lectin BC2L. This lectin has been shown to be a “super” lectin, containing two lectin domains, at the C- and N-terminus. These two lectin domains have been shown to have specificity for different substrates and have been proposed to mediate cell adhesion by conjugating with the bacterial membrane and the host's membrane.1 The N-terminus builds a homotrimer that binds specifically to carbohydrates containing fucose at the interface between monomers.2
In 2018 a study by Shimomura et al. (2018) determined that the N-terminus of the BC2L-C lectin could bind to a representative pancreatic cancer cell line (Capan-1) and be used as a delivery system by conjugating it with a drug3. It has additionally been shown that this lectin has the potential to recognize other cancer types, such as colorectal cancer4, breast cancer5 and tumorigenic pluripotent stem cells6.
As a part of our project “TargetTaxi”, we aimed to utilize this lectin for cancer cell recognition and adhesion. The lectin would be exposed at the surface of Salmonella-derived minicells and mediate their binding. The surface display will be mediated by its fusion with a surface display system regulated by AIDA and FimH.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References

1. Šulák, O. et al. Burkholderia cenocepacia bc2l-c is a super lectin with dual specificity and proinflammatory activity. PLoS Pathog. (2011) doi:10.1371/journal.ppat.1002238.
2. Šulák, O. et al. A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens. Structure (2010) doi:10.1016/j.str.2009.10.021.
3. Shimomura, O. et al. A novel therapeutic strategy for pancreatic cancer: Targeting cell surface glycan using rBC2LC-N lectin-drug conjugate (LDC). Mol. Cancer Ther. (2018) doi:10.1158/1535-7163.MCT-17-0232.
4. Kitaguchi, D. et al. Lectin drug conjugate therapy for colorectal cancer. Cancer Sci. (2020) doi:10.1111/cas.14687.
5. Mawaribuchi, S. et al. rBC2LCN lectin as a potential probe of early-stage HER2-positive breast carcinoma. FEBS Open Bio (2020) doi:10.1002/2211-5463.12852.
6. Haramoto, Y. et al. A technique for removing tumourigenic pluripotent stem cells using rBC2LCN lectin. Regen. Ther. (2020) doi:10.1016/j.reth.2020.03.017.