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Identification and characterization of a chitin-binding protein purified from coelomic fluid of the lugworm Arenicola marina defining a novel protein sequence family

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  • Nina Vitashenkova
  • Jesper Bonnet Moeller
  • Rikke Leth-Larsen
  • Anders Schlosser
  • Kit Peiter Lund
  • Ida Tornøe
  • Lars Vitved
  • Søren Hansen
  • Anthony Willis
  • Alexandra D Kharazova
  • Karsten Skjødt
  • Grith Lykke Sorensen
  • Uffe Laurits Holmskov
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We have isolated a novel type of lectin named Arenicola marina lectin-1 (AML-1) from the lugworm A. marina. The lectin was purified from the coelomic fluid by affinity chromatography on a GlcNAc-derivatized column and eluted with GlcNAc. On SDS-PAGE, AML-1 showed an apparent molecular mass of 27 and 31 kDa in the reduced state. The N-terminal amino acid sequences were identical in these two bands. In the unreduced state, a complex band pattern was observed with bands from 35 kDa to more than 200 kDa. Two different full-length clones encoding polypeptides of 241 and 243 amino acids, respectively, were isolated from a coelomocyte cDNA library. The two clones, designated AML-1a and AML-1b, were 92% identical at the protein level and represent a novel type of protein sequence family. Purified AML-1 induced agglutination of rabbit erythrocytes, which could be inhibited by N-acetylated saccharides. Recombinant AML-1b showed the same band pattern as the native protein, whereas recombinant AML-1a in the reduced state lacked a 27 kDa band. AML-1b bound GlcNAc-derivatized columns and chitin, whereas AML-1a did not bind to these matrices. Immunohistochemical analysis revealed that AML-1 is expressed by coelomocytes in the nephridium and in round cells in the epidermis and in eggs. Moreover, AML-1 expression was up-regulated in response to a parasitic infection. We conclude that AML-1 purified from coelomic fluid is encoded by AML-1b and represents a novel type of protein family that binds acetylated components.
OriginalsprogEngelsk
TidsskriftThe journal of biological chemistry
Vol/bind287
Udgave nummer51
Sider (fra-til)42846-55
Antal sider10
ISSN0021-9258
DOI
StatusUdgivet - 14 dec. 2012

ID: 42486488