A fibrinogen-related Lectin from Echinometra lucunter represents a new FReP family in Echinodermata phylum

Fibrinogen-related proteins (FREPs) have been identified in several animals. They are involved in the body's defense, acting as mediators of phagocytosis. Ficolins and intelectins are some of the most studied Fibrinogen-related Domain (FReD)-containing lectins. In this work, we have isolated a...

Full description

Saved in:
Bibliographic Details
Published in:Fish & shellfish immunology 2022-12, Vol.131, p.150-159
Main Authors: Duarte, Philippe Lima, Andrade, Francisco Regivânio Nascimento, Sousa, Andressa Rocha de Oliveira, Andrade, Alexandre Lopes, de Vasconcelos, Mayron Alves, Teixeira, Edson Holanda, Nagano, Celso Shiniti, Sampaio, Alexandre Holanda, Carneiro, Rômulo Farias
Format: Article
Language:English
Subjects:
Animals
Antibacterial activity
Echinodermata - metabolism
Escherichia coli
Fibrinogen - genetics
Fibrinogen-related protein
FReD
Intelectin
Lectin
Lectins - genetics
Lectins - metabolism
Lectins - pharmacology
Sea urchin
Sequence Alignment
Staphylococcus aureus - metabolism
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Fibrinogen-related proteins (FREPs) have been identified in several animals. They are involved in the body's defense, acting as mediators of phagocytosis. Ficolins and intelectins are some of the most studied Fibrinogen-related Domain (FReD)-containing lectins. In this work, we have isolated a singular FReD-containing lectin, which cannot be classified as ficolin or intelectin. ELL (Echinometra lucunter lectin) was isolated from coelomic plasma by affinity chromatography on xanthan gum. Primary structure was determined by tandem mass spectrometry. Moreover, antimicrobial activity of ELL was evaluated against planktonic cells and biofilm of Escherichia coli, Staphylococcus aureus and S. epidermidis. ELL showed hemagglutinating activity in Ca2+ presence, which was inhibited by glycoprotein mucin and thyroglobulin. Complete amino acid sequence consisted of 229 residues, including a FReD in the N-terminal. Searches for similarity found that ELL was very close to putative proteins from Strongylocentrotus purpuratus. ELL showed moderate similarity with uncharacterized sea stars proteins and protochordate intelectins. ELL was able to inhibit the planktonic growth of the Gram-positive bacteria and significantly reduce the biofilm formation of all bacteria tested. In conclusion, we identified a new type of FReP-containing lectin with some structural and functional conservation towards intelectins. •A Fibrinogen-related protein (FREP) was isolated from sea urchin Echinometra lcuunter.•ELL she is the first member of a new family of FREPs found in echinoderms.•ELL seems to be involved in the defense of the E. lucunter.•ELL was able to inhibit the planktonic growth of the Gram-positive bacteria.
ISSN:1050-4648
1095-9947
DOI:10.1016/j.fsi.2022.10.007