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Abstract
The notorious biofouling organism Dreissena polymorpha (the zebra mussel) attaches to a variety of surfaces using a byssus, a series of protein threads that connect the animal to adhesive plaques secreted onto hard substrata. Here, the use of matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) to characterize the composition of different regions of the byssus is reported. All parts of the byssus show mass peaks corresponding to small proteins in the range of 3.7–7 kDa, with distinctive differences between different regions. Indeed, spectra from thread and plaques are almost completely non-overlapping. In addition, several peaks were identified that are unique to the interfacial region of the plaque, and therefore likely represent specialized adhesive proteins. These results indicate a high level of control over the distribution of proteins, presumably with different functions, in the byssus of this freshwater species.
Acknowledgements
The authors gratefully acknowledge Feryal Sarraf cryo-sectioning, Dr Suzanne Ackloo of the Ontario Cancer Biomarker Network for MALDI analytical services and advice on sample preparation, and Shrirang Phatak for the SEM image of byssal plaques and threads. This work was supported by the National Sciences and Engineering Research Council (NSERC) of Canada, the Canadian Foundation for Innovation (CFI), and the Ontario Research Fund (ORF).