Immunodetection of Mytilus galloprovincialis larvae using monoclonal antibodies to monitor larval abundance on the Galician coast: Optimization of the method and comparison with identification by morphological traits

Pérez, Daniel; Lorenzo-Abalde, Silvia; González-Fernández, África; Fuentes, José

doi:10.1016/j.aquaculture.2009.05.020

Cited by 7 publications

(3 citation statements)

References 20 publications

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“…edulis species. This implies that the antigen recognized by M22.8 is shared by at least two species of the genus Mytilus, and this mAb has proven to be useful in the identification of mussel larvae and postlarvae [ 34 ]. Immunofluorescence and immunohistochemistry assays showed a peripheral pattern of recognition in M .…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Monoclonal Antibody Directed against Mytilus spp Larvae Reveals an Antigen Involved in Shell Biomineralization

et al. 2016

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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.

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Section: Introductionmentioning

confidence: 99%

Characterization of a Monoclonal Antibody Directed against Mytilus spp Larvae Reveals an Antigen Involved in Shell Biomineralization

et al. 2016

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“…Sampling was done using double oblique tows equipped with a 40-μm mesh at a depth of 10 m. The samples (400-500 L) were filtered again through 40-μm mesh upon return to the laboratory and any retained material was suspended in 20 ml of sterile seawater. Bivalve larvae were isolated using sugar gradient centrifugation (Pérez et al 2009), suspended in seawater and stored at −20…”

Section: Samples Collectionmentioning

confidence: 99%

“…Some authors have successfully applied polyclonal antibodies for larval identification in plankton samples (Paugam et al 2000;Paugam et al 2003) but cross-reactions with non-target species. The use of monoclonal antibodies is an alternative method which has been successfully applied in the identification of mussel species (Lorenzo-Abalde et al 2005;Pérez et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Identification and quantification of two species of oyster larvae using real-time PCR

Sánchez

Quinteiro

Rey-Méndez

et al. 2014

Aquat. Living Resour.

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-A real-time polymerase chain reaction (PCR) assay was developed for the identification and quantification of two oyster species: Ostrea edulis and Crassostrea gigas. Two sets of primers and TaqMan-MGB probes were designed, based on partial sequences of the 16S rRNA gene. An amplification positive control system was also located in the 18S rRNA gene sequences. Closely related species of oysters and other bivalves, known to co-occur with the target species in European waters, were used to test the assay for cross-reactivity. The assay designed was specific for the target species and no signal or no significant signal was detected for all non-target species tested. The high sensitivity of this method was demonstrated since it is possible to detect just one larva (150-200 μm size) of each species even when it is present with others. Furthermore, this assay provided an acceptable quantification of the number of spiked larvae (1, 10 and 100 larvae) in plankton samples employing a standard curve for larvae.

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MSP22.8 is a protease inhibitor‐like protein involved in shell mineralization in the edible mussel Mytilus galloprovincialis

Calvo-Iglesias

Pérez-Estévez²,

González-Fernández

2017

FEBS Open Bio

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The mussel shell protein 22.8 (MSP22.8) is recognized by a monoclonal antibody (M22.8) directed against larvae of the mussel Mytilus galloprovincialis. After being secreted by cells of the mantle‐edge epithelium into the extrapallial (EP) space (the gap between the mantle and the shell), the protein is detected in the extrapallial fluid (EPF) and EP hemocytes and finally becomes part of the shell matrix framework in adult specimens of M. galloprovincialis. In the work described here, we show how MSP22.8 is detected in EPF samples from different species of mussels (M. galloprovincialis, Mytilus edulis, and Xenostrobus securis), and also as a shell matrix protein in M. galloprovincialis, Mytilus chilensis, and Perna canaliculus. A multistep purification strategy was employed to isolate the protein from the EPF, which was then analyzed by mass spectrometry in order to identify it. The results indicate that MSP22.8 is a serpin‐like protein that has great similarity with the protease inhibitor‐like protein‐B1, reported previously for Mytilus coruscus. We suggest that MSP22.8 is part of a system offering protection from proteolysis during biomineralization and is also part of the innate immune system in mussels.

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Immunodetection of Mytilus galloprovincialis larvae using monoclonal antibodies to monitor larval abundance on the Galician coast: Optimization of the method and comparison with identification by morphological traits

Cited by 7 publications

References 20 publications

Characterization of a Monoclonal Antibody Directed against Mytilus spp Larvae Reveals an Antigen Involved in Shell Biomineralization

Characterization of a Monoclonal Antibody Directed against Mytilus spp Larvae Reveals an Antigen Involved in Shell Biomineralization

Identification and quantification of two species of oyster larvae using real-time PCR

MSP22.8 is a protease inhibitor‐like protein involved in shell mineralization in the edible mussel Mytilus galloprovincialis

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