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Although several lineage-specific gene losses and acquisitions are likely to have reshaped the organization of the proto-complement system during its evolution, leading to its complete loss in some major extant taxa (e.g., insects), the activation of this primary defense system often relies on the recognition of microbe-associated molecular patterns (MAMPs) by different types of soluble lectin-like molecules.
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Our observations point out that the evolutionary process behind the development of a large arsenal of C1qDC lectin-like molecules in marine bivalves is still ongoing and likely based on an unequal crossing over.Ī growing body of evidence supports the idea that a proto-complement system, composed of C3, factor B and complement receptors, has an ancient origin in the animal tree of life. The analysis of the chromosome-scale genome assembly of the Eastern oyster Crassostrea virginica revealed that the 476 oyster C1qDC genes, far from being uniformly distributed along the genome, are located in large clusters of tandemly duplicated paralogs, mostly found on chromosomes 7 and 8. While a large amount of functional data concerning the binding specificity of the globular head C1q domain and on the regulation of these molecules in response to infection are quickly accumulating, the genetic mechanisms that have led to the extraordinary lineage-specific expansion of the C1qDC gene family in bivalves are still largely unknown. Growing experimental evidence suggests that these highly abundant secretory proteins are involved in the recognition of microbe-associated molecular patterns, serving as lectin-like molecules in the bivalve proto-complement system. C1q-domain-containing (C1qDC) proteins are rapidly emerging as key players in the innate immune response of bivalve mollusks.