Full-Length cDNA, Prokaryotic Expression, and Antimicrobial Activity of UuHb-F-I from Urechis unicinctus

Abstract EN

Hemoglobin, which widely exists in all vertebrates and in some invertebrates, is possibly a precursor of antimicrobial peptides (AMPs).

However, AMPs in the hemoglobin of invertebrates have been rarely investigated.

This study is the first to report the full-length cDNA, prokaryotic expression, and antimicrobial activity of UuHb-F-I from Urechis unicinctus.

The full-length cDNA sequence of UuHb-F-I was 780 bp with an open-reading frame of 429 bp encoding 142 amino acids.

MALDI-TOF-MS suggested that the recombinant protein of UuHb-F-I (rUuHb-F-I) yielded a molecular weight of 15,168.01 Da, and its N-terminal amino acid sequence was MGLTGAQIDAIK.

rUuHb-F-I exhibited different antimicrobial activities against microorganisms.

The lowest minimum inhibitory concentration against Micrococcus luteus was 2.78–4.63 μ M.

Our results may help elucidate the immune defense mechanism of U.

unicinctus and may provide insights into new AMPs in drug discovery.