title: Deciphering the molecular mechanisms underlying sea urchin reversible adhesion: A quantitative proteomics approach.
abstract: Marine bioadhesives have unmatched performances in wet environments, being an inspiration for biomedical applications. In sea urchins specialized adhesive organs, tube feet, mediate reversible adhesion, being composed by a disc, producing adhesive and de-adhesive secretions, and a motile stem. After tube foot detachment, the secreted adhesive remains bound to the substratum as a footprint. Sea urchin adhesive is composed by proteins and sugars, but so far only one protein, Nectin, was shown to be over-expressed as a transcript in tube feet discs, suggesting its involvement in sea urchin adhesion. Here we use high-resolution quantitative mass-spectrometry to perform the first study combining the analysis of the differential proteome of an adhesive organ, with the proteome of its secreted adhesive. This strategy allowed us to identify 163 highly over-expressed disc proteins, specifically involved in sea urchin reversible adhesion; to find that 70% of the secreted adhesive components fall within five protein groups, involved in exocytosis and microbial protection; and to provide evidences that Nectin is not only highly expressed in tube feet discs but is an actual component of the adhesive. These results give an unprecedented insight into the molecular mechanisms underlying sea urchin adhesion, and opening new doors to develop wet-reliable, reversible, and ecological biomimetic adhesives.
  
  
  CONCLUSIONS
  Sea urchins attach strongly but in a reversible manner to substratum, being a valuable source of inspiration for industrial and biomedical applications. Yet, the molecular mechanisms governing reversible adhesion are still poorly studied delaying the engineering of biomimetic adhesives. We used the latest mass spectrometry techniques to analyze the differential proteome of an adhesive organ and the proteome of its secreted adhesive, allowing us to uncover the key players in sea urchin reversible adhesion. We demonstrate, that Nectin, a protein previously pointed out as potentially involved in sea urchin adhesion, is not only highly expressed in tube feet discs, but is a genuine component of the secreted adhesive.
authors.affiliation: Netherlands Proteomics Center, Padualaan 8, 3584, CH, Utrecht, Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584, CH, Utrecht, Netherlands.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Lebesgue
authors.affiliation: Centro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, Campo Grande, 1749-016, Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal; Laboratório de FTICR e espectrometria de massa estrutural, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal.
authors.forename: Gonçalo
authors.initials: G
authors.lastname: da Costa
authors.affiliation: Centro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, Campo Grande, 1749-016, Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal.
authors.forename: Raquel Mesquita
authors.initials: RM
authors.lastname: Ribeiro
authors.affiliation: Centro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, Campo Grande, 1749-016, Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal.
authors.forename: Cristina
authors.initials: C
authors.lastname: Ribeiro-Silva
authors.affiliation: Instituto Gulbenkian de Ciência, R. da Quinta Grande 6, 2780-156 Oeiras, Portugal; Centro de Ecologia, Evolução e Alterações Ambientais, Faculdade de Ciências da Universidade de Lisboa, Campo Grande 1749-016, Lisboa, Portugal.
authors.forename: Gabriel G
authors.initials: GG
authors.lastname: Martins
authors.affiliation: Consiglio Nazionale delle Ricerche, Istituto di Biomedicina e Immunologia Molecolare, 'Alberto Monroy', Via Ugo La Malfa 153, 90146 Palermo, Italy.
authors.forename: Valeria
authors.initials: V
authors.lastname: Matranga
authors.affiliation: Netherlands Proteomics Center, Padualaan 8, 3584, CH, Utrecht, Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584, CH, Utrecht, Netherlands.
authors.forename: Arjen
authors.initials: A
authors.lastname: Scholten
authors.affiliation: Centro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, Campo Grande, 1749-016, Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal; Laboratório de FTICR e espectrometria de massa estrutural, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal.
authors.forename: Carlos
authors.initials: C
authors.lastname: Cordeiro
authors.affiliation: Netherlands Proteomics Center, Padualaan 8, 3584, CH, Utrecht, Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584, CH, Utrecht, Netherlands.
authors.forename: Albert J R
authors.initials: AJ
authors.lastname: Heck
authors.affiliation: Centro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, Campo Grande, 1749-016, Lisboa, Portugal; MARE - Centro de Ciências do Mar e do Ambiente, Faculdade de Ciências da Universidade de Lisboa, Campo Grande 1749-016, Lisboa, Portugal. Electronic address: romana.santos@campus.ul.pt.
authors.forename: Romana
authors.initials: R
authors.lastname: Santos
mesh_terms: D000269:Adhesives / Q000378:metabolism*; D000818:Animals; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D000075983:Nectins; D047328:Paracentrotus / Q000378:metabolism*; D040901:Proteomics
chemical_list: D000269:Adhesives; D015815:Cell Adhesion Molecules; D000075983:Nectins
keywords: Paracentrotus lividus; Quantitative proteomics; Reversible adhesion; Sea urchin; Tube foot adhesive protein