Hemocyanin-derived phenoloxidase reaction products display anti-infective properties

Christopher J. Coates, James Talbot

Research output: Contribution to a Journal (Peer & Non Peer)Articlepeer-review

39 Citations (Scopus)

Abstract

Hemocyanin is a multi-functional protein located in the hemolymph (blood) of certain arthropods and molluscs. In addition to its well-defined role in oxygen transport, hemocyanin can be converted into a phenoloxidase-like enzyme. Herein, we tested the antimicrobial properties of horseshoe crab (Limulus polyphemus) hemocyanin-derived phenoloxidase reaction products using broad ranges of phenolic substrates (e.g. L-DOPA) and microbial targets (Gram-positive/negative bacteria, yeast). The enzyme-catalysed turnover of several substrates generated (by)products that reduced significantly the number of colony forming units. Microbicidal effects of hemocyanin-derived phenoloxidase were thwarted by the inhibitor phenylthiourea. Data presented here further support a role for hemocyanin in invertebrate innate immunity.

Original languageEnglish
Pages (from-to)47-51
Number of pages5
JournalDevelopmental and Comparative Immunology
Volume86
DOIs
Publication statusPublished - Sep 2018
Externally publishedYes

Keywords

  • Enzyme-substrate complexes
  • Horseshoe crabs
  • Innate immunity
  • Melanogenesis
  • Multifunctional protein

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