From Sand Tube to Test Tube: The Adhesive Scretion From Sabellariid Tubeworms

Hennebert, Elise; Maldonado, Barbara; Weerdt, Cécile Van de; Demeuldre, Mélanie; Richter, Katharina; Rischka, Klaus; Flammang, Patrick

doi:10.1201/b18095-8

Cited by 4 publications

(4 citation statements)

References 36 publications

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“…Homogeneous granules contain the sulfated macromolecules and the proteins Pc-2 and Pc-5, whereas heterogeneous granules contain the proteins Pc-1, Pc-3 and Pc-4, paired with divalent cations. Co-secretion and limited mixing of the preassembled adhesive packets lead to formation of a complex composite cement in which the localization and role of the different adhesive proteins are still poorly understood [ 59 ].…”

Section: Animal Protein-based Adhesivesmentioning

confidence: 99%

“…Two barnacle recombinant adhesive proteins, rMrcp-19k [ 11 ] and rMrcp-20k [ 15 ], have been successfully produced. The protein Sa-1 from the tubeworm S. alveolata was also successfully expressed and the recombinant protein, rSa-1, was mainly produced in the insoluble fraction of the bacteria, probably as inclusion bodies [ 59 ]. In spiders, fragments of the attachment disc glue silk fibroin 2 (PySp2) from N. clavipes [ 17 ] and the aggregate gland protein AgSF1 from L. hesperus [ 18 ] were produced and used for artificial spinning.…”

Section: Molecular Tools To Characterize Protein-based Adhesivesmentioning

confidence: 99%

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Experimental strategies for the identification and characterization of adhesive proteins in animals: a review

et al. 2015

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Adhesive secretions occur in both aquatic and terrestrial animals, in which they perform diverse functions. Biological adhesives can therefore be remarkably complex and involve a large range of components with different functions and interactions. However, being mainly protein based, biological adhesives can be characterized by classical molecular methods. This review compiles experimental strategies that were successfully used to identify, characterize and obtain the full-length sequence of adhesive proteins from nine biological models: echinoderms, barnacles, tubeworms, mussels, sticklebacks, slugs, velvet worms, spiders and ticks. A brief description and practical examples are given for a variety of tools used to study adhesive molecules at different levels from genes to secreted proteins. In most studies, proteins, extracted from secreted materials or from adhesive organs, are analysed for the presence of post-translational modifications and submitted to peptide sequencing. The peptide sequences are then used directly for a BLAST search in genomic or transcriptomic databases, or to design degenerate primers to perform RT-PCR, both allowing the recovery of the sequence of the cDNA coding for the investigated protein. These sequences can then be used for functional validation and recombinant production. In recent years, the dual proteomic and transcriptomic approach has emerged as the best way leading to the identification of novel adhesive proteins and retrieval of their complete sequences.

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Section: Animal Protein-based Adhesivesmentioning

confidence: 99%

Section: Molecular Tools To Characterize Protein-based Adhesivesmentioning

confidence: 99%

Experimental strategies for the identification and characterization of adhesive proteins in animals: a review

et al. 2015

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“…Sabellariids are tube-dwelling marine polychaetes that live in the intertidal zone. To build their tube, they collect sand grains or mollusc shell fragments in their surroundings, dab them with spots of cement, and assemble them into a rigid composite tube ( Hennebert et al, 2015 ; Stewart et al, 2017 ). This cement is secreted by the so-called building organ, a complex secretory organ made up of bouquets of cement cells located deep within the thorax of the worms ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Involvement of sulfated biopolymers in adhesive secretions produced by marine invertebrates

2018

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Many marine invertebrates use adhesive secretions to attach to underwater surfaces and functional groups borne by their adhesive proteins and carbohydrates, such as catechols and phosphates, play a key role in adhesion. The occurrence of sulfates as recurrent moieties in marine bioadhesives suggests that they could also be involved. However, in most cases, their presence in the adhesive material remains speculative. We investigated the presence of sulfated biopolymers in five marine invertebrates representative of the four types of adhesion encountered in the sea: mussels and tubeworms for permanent adhesion, limpets for transitory adhesion, sea stars for temporary adhesion and sea cucumbers for instantaneous adhesion. The dry adhesive material of mussels, sea stars and sea cucumbers contained about 1% of sulfate. Using anti-sulfotyrosine antibodies and Alcian Blue staining, sulfated proteins and sulfated proteoglycans and/or polysaccharides were identified in the secretory cells and adhesive secretions of all species except the tubeworm. Sulfated proteoglycans appear to play a role only in the non-permanent adhesion of sea stars and limpets in which they could mediate cohesion within the adhesive material. In mussels and sea cucumbers, sulfated biopolymers would rather have an anti-adhesive function, precluding self-adhesion.

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“…This plays a key role in biofilm structure and adhesion to various surfaces. Various adhesive materials have been reported so far, but none of the products produced have been able to meet all the necessary requirements (Geurts et al 2010 ; Hennebert et al 2015 ). In the present study, the recombinant protein expressed in terms of the post-translational process was approved.…”

Section: Discussionmentioning

confidence: 99%

A novel recombinant chimeric bio-adhesive protein consisting of mussel foot protein 3, 5, gas vesicle protein A, and CsgA curli protein expressed in Pichia pastoris

et al. 2022

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Despite various efforts to produce potent recombinant bio-adhesive proteins for medical purposes, efficient production of a safe and feasible bio-glue is not yet a commercial reality due to the weak properties or low expression levels. Here, a feasible expression system has been developed to produce strong recombinant fusion bioinspired protein using mussel foot protein 3 and 5 (Mfps) along with gas vesicle protein A (GvpA) of Anabaena flos-aquae, and a curli protein CsgA from E. coli, expressed under the control of alcohol oxidase (AOX1) promoter for high-level production in yeast P. pastoris using pPICZα vector. Purified chimeric proteins were first evaluated using western blotting, and their remaining dihydroxyphenylalanine (DOPA) was measured in the modified proteins by NBT assay. We further elucidated the mechanistic properties of obtained adhesive protein assembly in various pH levels based on its different subunits using atomic force microscopy (AFM) when adsorbed onto the mica surface. We found that both combinational structural features of subunits and post-translational changes during expression in yeast host have led to potent adherence due to higher DOPA residues specially in acidic condition and tetrad complex which is higher than that of earlier reports in prokaryotic systems. We believe that our obtained chimeric protein resulted from the fusion of GvpA and CsgA proteins with DOPA-containing Mfp proteins, expressed in the methylotrophic yeast, P. pastoris, not only presents a candidate for future biomedical applications but also provides novel biological clues used for high-performance bioinspired biomaterial designation. Graphical Abstract

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From Sand Tube to Test Tube: The Adhesive Scretion From Sabellariid Tubeworms

Cited by 4 publications

References 36 publications

Experimental strategies for the identification and characterization of adhesive proteins in animals: a review

Experimental strategies for the identification and characterization of adhesive proteins in animals: a review

Involvement of sulfated biopolymers in adhesive secretions produced by marine invertebrates

A novel recombinant chimeric bio-adhesive protein consisting of mussel foot protein 3, 5, gas vesicle protein A, and CsgA curli protein expressed in Pichia pastoris

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