Abstract
The M22.8 monoclonal antibody (mAb) developed against an antigen expressed at the mussel larval and postlarval stages of Mytilus galloprovincialis was studied on adult samples. Antigenic characterization by Western blot showed that the antigen MSP22.8 has a restricted distribution that includes mantle edge tissue, extrapallial fluid, extrapallial fluid hemocytes, and the shell organic matrix of adult samples. Other tissues such as central mantle, gonadal tissue, digestive gland, labial palps, foot, and byssal retractor muscle did not express the antigen. Immunohistochemistry assays identified MSP22.8 in cells located in the outer fold epithelium of the mantle edge up to the pallial line. Flow cytometry analysis showed that hemocytes from the extrapallial fluid also contain the antigen intracellularly. Furthermore, hemocytes from hemolymph have the ability to internalize the antigen when exposed to a cell-free extrapallial fluid solution. Our findings indicate that hemocytes could play an important role in the biomineralization process and, as a consequence, they have been included in a model of shell formation. This is the first report concerning a protein secreted by the mantle edge into the extrapallial space and how it becomes part of the shell matrix framework in M. galloprovincialis mussels.
Highlights
Molluscan shells are good examples of how living organisms elaborate a mineralized structure by a fully biologically controlled mineralization process called biomineralization [1,2,3]
We show here how hemocytes are able to internalize the antigen after exposure to a cell-free Extrapallial fluid (EPF) solution
In the present work it has been demostrated that M22.8 monoclonal antibody (mAb) recognizes an antigen (MSP22.8) in M. galloprovincialis larvae and in adult specimens, suggesting that it is expressed at all stages of mussel life
Summary
Molluscan shells are good examples of how living organisms elaborate a mineralized structure by a fully biologically controlled mineralization process called biomineralization [1,2,3]. The unique properties of shells as biomaterials (high fracture toughness) [4, 5] have attracted a great deal of interest and significant effort has been dedicated to the study of their structure and organic elements. Numerous opportunities are envisaged for the application of shell proteins in Nanotechnology, Bioscience and even in Biomedicine [6, 7]. Identification of a Protein Involved in Mussel Shell Formation
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