Biochemical and functional characterization of rMe'exLec1, a recombinant tandem-repeat lectin from the ancient marine chelicerate Limulus polyphemus DOI Creative Commons

Francisco H Olvera-Lucio,

Héctor Riveros‐Rosas, Jaime Zaldívar-Rae

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142895 - 142895

Published: April 1, 2025

Mass extinctions have disrupted the evolutionary history of several species, and with it discovery novel proteins biomedical biotechnological value. However, Limulus polyphemus, a xiphosuran marine arthropod, is "living fossil" 480-million-year-old lineage. To explore this legacy, rMe'exLec1, 13.15 kDa tandem-repeat lectin from L. was studied. Named after ancient Maya term "Me'ex" ("spider fish"), Identified in genome, recombinantly expressed Escherichia coli, purified via nickel affinity chromatography, yielding 1 g/L culture. The protein remained stable across wide pH range different salts. Far-UV circular dichroism confirmed proper folding presence both α β secondary structures. rMe'exLec1 exhibited specificity for L-Fuc D-GalNAc, terminal sugars human A-antigen, demonstrating agglutinating activity on type A erythrocytes. It also bound divalent ions such as nickel, formed monodisperse oligomers. Additionally, inhibited growth Gram-negative (Vibrio parahaemolyticus, E. coli Rosetta(DE3) DH5α), Gram-positive (Lactiplantibacillus plantarum) bacteria, highlighting its potential applications. Structural sequence analyses homologous proteins, along their limited phyletic distribution unique relationships, support classification group family, named Me'exLec-type. Furthermore, tandemly repeated, non-identical binding sites are evolutionarily conserved phylogenetically distant groups.

Language: Английский

Biochemical and functional characterization of rMe'exLec1, a recombinant tandem-repeat lectin from the ancient marine chelicerate Limulus polyphemus DOI Creative Commons

Francisco H Olvera-Lucio,

Héctor Riveros‐Rosas, Jaime Zaldívar-Rae

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142895 - 142895

Published: April 1, 2025

Mass extinctions have disrupted the evolutionary history of several species, and with it discovery novel proteins biomedical biotechnological value. However, Limulus polyphemus, a xiphosuran marine arthropod, is "living fossil" 480-million-year-old lineage. To explore this legacy, rMe'exLec1, 13.15 kDa tandem-repeat lectin from L. was studied. Named after ancient Maya term "Me'ex" ("spider fish"), Identified in genome, recombinantly expressed Escherichia coli, purified via nickel affinity chromatography, yielding 1 g/L culture. The protein remained stable across wide pH range different salts. Far-UV circular dichroism confirmed proper folding presence both α β secondary structures. rMe'exLec1 exhibited specificity for L-Fuc D-GalNAc, terminal sugars human A-antigen, demonstrating agglutinating activity on type A erythrocytes. It also bound divalent ions such as nickel, formed monodisperse oligomers. Additionally, inhibited growth Gram-negative (Vibrio parahaemolyticus, E. coli Rosetta(DE3) DH5α), Gram-positive (Lactiplantibacillus plantarum) bacteria, highlighting its potential applications. Structural sequence analyses homologous proteins, along their limited phyletic distribution unique relationships, support classification group family, named Me'exLec-type. Furthermore, tandemly repeated, non-identical binding sites are evolutionarily conserved phylogenetically distant groups.

Language: Английский

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