Shell palaeoproteomics: First application of peptide mass fingerprinting for the rapid identification of mollusc shells in archaeology

Sakalauskaite, Jorune; Marin, Frédéric; Pergolizzi, Barbara; Demarchi, Beatrice

doi:10.1016/j.jprot.2020.103920

Cited by 25 publications

(18 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has previously been shown that exposure of shell biominerals to solutions of these chemicals for <3 hours causes no alteration to their composition or structure. 15,31,32 Even aer 240 hours (ten days) of oxidation with a less persistent oxidant, hydrogen peroxide, $50% of the original organic concentration persisted within the shell biomineral powders. 31 In the presence of biominerals with carbonate, hydrogen peroxide became less effective at oxidizing organic compounds; also hydrogen peroxide is thermodynamically unstable, decomposing into water and oxygen.…”

Section: Sample Preparationmentioning

confidence: 99%

Characterization of organophosphatic brachiopod shells: spectroscopic assessment of collagen matrix and biomineral components

et al. 2020

View full text Add to dashboard Cite

show abstract

Section: Sample Preparationmentioning

confidence: 99%

Characterization of organophosphatic brachiopod shells: spectroscopic assessment of collagen matrix and biomineral components

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Of these matrix components, proteins are the best studied; their preservation in the mineral can lead to inferences of function and provide indirect genetic information in the absence of preserved DNA (e.g., Schroeter et al, 2017). Recent analyses have shown that intact endogenous peptides remain in invertebrate skeletons for 1000s-100,000s of years (Sakalauskaite et al, 2019;Drake L. et al, 2020b;Sakalauskaite et al, 2020). Across various taxa, intact peptides may retain amino acids longer in fossil specimens than if those biomolecules exist individually as free amino acids (Bada et al, 1999), allowing for detection of ecological and ocean chemistry signatures including the occurrence of photosymbiosis in fossil scleractinian corals (Muscatine et al, 2005;Tornabene et al, 2017) and past local nitrogen cycling regimes (Wang et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Fossil Corals With Various Degrees of Preservation Can Retain Information About Biomineralization-Related Organic Material

2021

View full text Add to dashboard Cite

Scleractinian corals typically form a robust calcium carbonate skeleton beneath their living tissue. This skeleton, through its trace element composition and isotope ratios, may record environmental conditions of water surrounding the coral animal. While bulk unrecrystallized aragonite coral skeletons can be used to reconstruct past ocean conditions, corals that have undergone significant diagenesis have altered geochemical signatures and are typically assumed to retain insufficient meaningful information for bulk or macrostructural analysis. However, partially recrystallized skeletons may retain organic molecular components of the skeletal organic matrix (SOM), which is secreted by the animal and directs aspects of the biomineralization process. Some SOM proteins can be retained in fossil corals and can potentially provide past oceanographic, ecological, and indirect genetic information. Here, we describe a dataset of scleractinian coral skeletons, aged from modern to Cretaceous plus a Carboniferous rugosan, characterized for their crystallography, trace element composition, and amino acid compositions. We show that some specimens that are partially recrystallized to calcite yield potentially useful biochemical information whereas complete recrystalization or silicification leads to significant alteration or loss of the SOM fraction. Our analysis is informative to biochemical-paleoceanographers as it suggests that previously discounted partially recrystallized coral skeletons may indeed still be useful at the microstructural level.

show abstract

“…Our study shows the good potential for preservation of some SMPs across archaeological times. It consequently paves the road of an emerging discipline, ‘palaeoshellomics’ ( Wallace and Schiffbauer, 2016 ; Sakalauskaite et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

The ‘Shellome’ of the Crocus Clam Tridacna crocea Emphasizes Essential Components of Mollusk Shell Biomineralization

et al. 2021

Self Cite

View full text Add to dashboard Cite

Molluscan shells are among the most fascinating research objects because of their diverse morphologies and textures. The formation of these delicate biomineralized structures is a matrix-mediated process. A question that arises is what are the essential components required to build these exoskeletons. In order to understand the molecular mechanisms of molluscan shell formation, it is crucial to identify organic macromolecules in different shells from diverse taxa. In the case of bivalves, however, taxon sampling in previous shell proteomics studies are focused predominantly on representatives of the class Pteriomorphia such as pearl oysters, edible oysters and mussels. In this study, we have characterized the shell organic matrix from the crocus clam, Tridacna crocea, (Heterodonta) using various biochemical techniques, including SDS-PAGE, FT-IR, monosaccharide analysis, and enzyme-linked lectin assay (ELLA). Furthermore, we have identified a number of shell matrix proteins (SMPs) using a comprehensive proteomics approach combined to RNA-seq. The biochemical studies confirmed the presence of proteins, polysaccharides, and sulfates in the T. crocea shell organic matrix. Proteomics analysis revealed that the majority of the T. crocea SMPs are novel and dissimilar to known SMPs identified from the other bivalve species. Meanwhile, the SMP repertoire of the crocus clam also includes proteins with conserved functional domains such as chitin-binding domain, VWA domain, and protease inhibitor domain. We also identified BMSP (Blue Mussel Shell Protein, originally reported from Mytilus), which is widely distributed among molluscan shell matrix proteins. Tridacna SMPs also include low-complexity regions (LCRs) that are absent in the other molluscan genomes, indicating that these genes may have evolved in specific lineage. These results highlight the diversity of the organic molecules – in particular proteins – that are essential for molluscan shell formation.

show abstract

Shell palaeoproteomics: First application of peptide mass fingerprinting for the rapid identification of mollusc shells in archaeology

Cited by 25 publications

References 59 publications

Characterization of organophosphatic brachiopod shells: spectroscopic assessment of collagen matrix and biomineral components

Characterization of organophosphatic brachiopod shells: spectroscopic assessment of collagen matrix and biomineral components

Fossil Corals With Various Degrees of Preservation Can Retain Information About Biomineralization-Related Organic Material

The ‘Shellome’ of the Crocus Clam Tridacna crocea Emphasizes Essential Components of Mollusk Shell Biomineralization

Contact Info

Product

Resources

About