Hemocyanin of the caenogastropod <i>Pomacea canaliculata</i> exhibits evolutionary differences among gastropod clades

Structural knowledge of gastropod hemocyanins is scarce. To better understand their evolution and diversity we studied the hemocyanin of a caenogastropod, <i>Pomacea canaliculata</i> (PcH). Through a proteomic and genomic approach, we identified 4 PcH subunit isoforms, in contrast with o...

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Autores principales: Chiumiento, Ignacio Rafael, Ituarte, Santiago, Sun, Jin, Qiu, Jian Wen, Heras, Horacio, Dreon, Marcos Sebastián
Formato: Articulo
Lenguaje:Inglés
Publicado: 2020
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/107884
http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC6992001&blobtype=pdf
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Sumario:Structural knowledge of gastropod hemocyanins is scarce. To better understand their evolution and diversity we studied the hemocyanin of a caenogastropod, <i>Pomacea canaliculata</i> (PcH). Through a proteomic and genomic approach, we identified 4 PcH subunit isoforms, in contrast with other gastropods that usually have 2 or 3. Each isoform has the typical Keyhole limpet-type hemocyanin architecture, comprising a string of eight globular functional units (FUs). Correspondingly, genes are organized in eight FUs coding regions. All FUs in the 4 genes are encoded by more than one exon, a feature not found in non- caenogastropods. Transmission electron microscopy images of PcH showed a cylindrical structure organized in di, tri and tetra-decamers with an internal collar structure, being the di and tridecameric cylinders the most abundant ones. PcH is N-glycosylated with high mannose and hybrid-type structures, and complex-type N-linked glycans, with absence of sialic acid. Terminal β-N-GlcNAc residues and nonreducing terminal α-GalNAc are also present. The molecule lacks O-linked glycosylation but presents the T-antigen (Gal-β1,3-GalNAc). Using an anti-PcH polyclonal antibody, no cross-immunoreactivity was observed against other gastropod hemocyanins, highlighting the presence of clade-specific structural differences among gastropod hemocyanins. This is, to the best of our knowledge, the first gene structure study of a Caenogastropoda hemocyanin.