2012
DOI: 10.1074/jbc.m112.420976
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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

Abstract: Background:The immune system of the lugworm depends solely on innate pattern recognition molecules. Results: AML-1 was isolated from the coelomic fluid, cloned and characterized as a pattern recognition receptor that binds chitin. Conclusion: AML-1 is the first polychaete lectin cloned and characterized. Significance: AML-1 represents a novel protein sequence family that may give rise to a new protein structure.

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Cited by 2 publications
(5 citation statements)
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“…We identified a new variant of AML‐1, AML‐1C, in the transcriptome of A. marina coelomocytes. Its amino‐acid sequence is identical to that previously described in AML‐1A and AML‐1B (Vitashenkova et al, 2012) by 95% and 91%, respectively. In addition, we described three novel genes encoding AML‐1‐like proteins with the C‐terminal u‐domain.…”
Section: Resultssupporting
confidence: 73%
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“…We identified a new variant of AML‐1, AML‐1C, in the transcriptome of A. marina coelomocytes. Its amino‐acid sequence is identical to that previously described in AML‐1A and AML‐1B (Vitashenkova et al, 2012) by 95% and 91%, respectively. In addition, we described three novel genes encoding AML‐1‐like proteins with the C‐terminal u‐domain.…”
Section: Resultssupporting
confidence: 73%
“…Another chitin‐binding lectin, the only one experimentally characterized in A. marina coelomocytes and coelomic fluid, is AML‐1 (Vitashenkova et al, 2012). It represents a family of calcium‐independent secreted oligomeric lectins bearing a novel C‐terminal unnamed domain (u‐domain).…”
Section: Resultsmentioning
confidence: 99%
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