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
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