Structural characteristics of a novel antifreeze protein from the longhorn beetle Rhagium inquisitor

E Kristiansen, Hans Ramløv, Peter Højrup, S A Pedersen, L Hagen, K E Zachariassen

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Antifreeze proteins (AFPs) are characterized by their capacity to inhibit the growth of ice and are produced by a variety of polar fish, terrestrial arthropods and other organisms inhabiting cold environments. This capacity reflects their role as stabilizers of supercooled body fluids. The longhorn beetle Rhagium inquisitor is known to express AFPs in its body fluids. In this work we report on the primary structure and structural characteristics of a 12.8 kDa AFP from this beetle (RiAFP). It has a high capacity to evoke antifreeze activity as compared to other known insect AFPs and it is structurally unique in several aspects. In contrast to the high content of disulfide bond-formation observed in other coleopteran AFPs, RiAFP contains only a single such bond. Six internal repeat segments of a thirteen residue repeat pattern is irregularly spaced apart throughout its sequence. The central part of these repeat segments is preserved as TxTxTxT, which is effectively an expansion of the TxT ice-binding motif found in the AFPs of several known insect AFPs.
Original languageEnglish
JournalInsect Biochemistry and Molecular Biology
Volume41
Issue number2
Pages (from-to)109-117
ISSN0965-1748
DOIs
Publication statusPublished - 12. Nov 2011

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