Related Experiment Video
Updated: Jun 26, 2025
11:16
Non-invasive Imaging of the Innate Immune Response in a Zebrafish Larval Model of Streptococcus iniae Infection
Published on: April 21, 2015
10.8K
Potential Involvement of the South American Lungfish Intelectin-2 in Innate-Associated Immune Modulation
Gabriela Patrícia Martins de Almeida Bernardes1, Gustavo Marques Serra2, Lucas da Silva E Silva1
1Laboratory of Genomics and Biotechnology, Biological Sciences Institute, Federal University of Pará (UFPA), Belém 66075-110, PA, Brazil.
International Journal of Molecular Sciences
|May 11, 2024
Summary
South American lungfish intelectin (LpITLN2-B) shows potential immune defense capabilities. Structural analysis reveals a homo-trimeric protein interacting with disaccharides, suggesting pathogen binding.
Area of Science:
- Biochemistry
- Immunology
- Zoology
Background:
- Intelectins are lectins crucial for immunity, involved in pathogen agglutination.
- Limited structural and carbohydrate-binding data exist for intelectins, hindering understanding of their function.
Purpose of the Study:
- To characterize the structure and carbohydrate-binding properties of LpITLN2-B from the South American lungfish (Lepidosiren paradoxa).
- To investigate the role of LpITLN2-B in the immune defense mechanisms of L. paradoxa.
Main Methods:
- RNA-sequencing data analysis to identify intelectin transcripts.
- In silico structural prediction of LpITLN2-B, including quaternary structure and domain analysis.
- Molecular docking simulations to assess carbohydrate interactions.
- Hemagglutination assays to evaluate lectin activity.
Main Results:
- LpITLN2-B was identified as a homo-trimeric globular protein (57 kDa) with a fibrinogen-like domain (FReD).
- Structural analysis revealed 11 β-sheets per domain and a trimeric quaternary structure (monomers A, B, C).
- Molecular docking indicated preferential binding to disaccharides over monosaccharides, suggesting interaction with pathogen molecules like LPS and Poly(I:C).
- Hemagglutination assays showed lectin activity inhibited by maltose and sucrose.
Conclusions:
- LpITLN2-B possesses structural and carbohydrate-binding characteristics consistent with an immune defense role in L. paradoxa.
- The preferential interaction with disaccharides suggests a mechanism for recognizing and binding to pathogen-associated molecular patterns.
- Further research into LpITLN2-B function can elucidate innate immune strategies in lungfish.
