Hemocyanin of the caenogastropod Pomacea canaliculata exhibits evolutionary differences among gastropod clades
Autor: | Jian-Wen Qiu, Jin Sun, Santiago Ituarte, Ignacio Rafael Chiumiento, Horacio Heras, Marcos Sebastián Dreon |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0106 biological sciences
Models Molecular Proteomics Glycosylation Protein Conformation medicine.medical_treatment Gastropoda Glycobiology 01 natural sciences Biochemistry Mass Spectrometry purl.org/becyt/ford/1 [https] chemistry.chemical_compound Database and Informatics Methods Protein structure Lectins Protein Isoforms Post-Translational Modification Pomacea 0303 health sciences Multidisciplinary biology Eukaryota Hemocyanin Genomics Chemistry Physical Sciences Medicine Gene structure study Pomacea canaliculata Sequence Analysis Gastropod hemocyanins Research Article Chemical Elements Gene isoform animal structures Bioinformatics Science Protein domain Sequence alignment Genome Complexity Research and Analysis Methods 010603 evolutionary biology Evolution Molecular 03 medical and health sciences Microscopy Electron Transmission Protein Domains Amino Acid Sequence Analysis Sequence Motif Analysis Apple Snail medicine Genetics Animals Ciencias Naturales purl.org/becyt/ford/1.6 [https] Ciencias Exactas 030304 developmental biology Caenogastropoda Gene Expression Profiling Organisms Biology and Life Sciences Computational Biology Proteins Molluscs biology.organism_classification Invertebrates Introns Oxygen carbohydrates (lipids) chemistry Gastropods Hemocyanins Sequence Alignment |
Zdroj: | PLoS ONE, Vol 15, Iss 1, p e0228325 (2020) CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET SEDICI (UNLP) Universidad Nacional de La Plata instacron:UNLP PLoS ONE |
ISSN: | 1932-6203 |
Popis: | Structural knowledge of gastropod hemocyanins is scarce. To better understand their evolution and diversity we studied the hemocyanin of a caenogastropod, Pomacea canaliculata (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. Instituto de Investigaciones Bioquímicas de La Plata Facultad de Ciencias Naturales y Museo |
Databáze: | OpenAIRE |
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