Marine Biology

, Volume 149, Issue 2, pp 307–312 | Cite as

Associations between metals and the blue mesogleal protein of Cassiopea xamachana

  • M. A. PhelanEmail author
  • J. L. Matta
  • Y. M. Reyes
  • R. Fernando
  • R. A. Boykins
  • R. S. Blanquet
Research Article


The blue mesogleal pigment of the symbiotic jellyfish, Cassiopea xamachana Bigelow, 1882, is composed of two subunits, a larger glycosylated (35 kDa) moiety and a non-glycosylated (30 kDa) variant in lower concentration. In solution, the subunits assemble in large complexes of at least 106 kDa. The pigment, known as Cassio Blue, appears to mitigate excessive solar radiation while allowing the passage of the wavelengths optimal for photosynthesis by the numerous algal symbionts in the mesoglea of the jellyfish. The pigment is an abundant protein comprising about 6% of all animal protein in the whole jellyfish and about 33% of all animal protein in the oral appendages. The protein also contains a diverse array of metals, notably Ag, Ca, Cu, Fe, Mg, and Zn, with traces of others. Metal stoichiometry varies among isolates averaging about 1 mol of all metals, taken together, for each mole of the pigment. Given the broad array of metals present, the pigment may also serve another purpose, for example, as a metal reservoir or trap. Few other proteins are associated with such a spectrum of metals. In addition, the amino acid sequences of the pigment tryptic peptides have no reasonable matches in any of the sequence databases. Our findings, taken as a whole, suggest that the Cassio pigment is indeed unusual and is likely a representative of a novel category of proteins, the original member of which is rpulFKz1, a chromoprotein endowed with Frizzled and Kringle domains.


Inductively Couple Plasma Mass Spectrometry Tryptic Peptide Inductively Couple Plasma Optical Emission Spectrometry Algal Symbiont Oxoglutarate Dehydrogenase 
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We thank our colleagues Dr. Ann McDermott for preparing the purified Cassio Blue and the whole homogenates of jellyfish tissues; Oliver Ashe for the densitometric evaluations of proteins resolved by SDS-PAGE; Dr. Jacqueline Muller for electron microscopy; Alicia Stanton for the alanine aminotransferase assays. We also note the RCMI Environmental Toxicology Program, Ponce School of Medicine for initial ICP analyses; the NIH-MBRS Program grant award (5 S06 GM08239-10) to J.L.M. for financial support. The sequencing work was supported partially by a grant provided by the W. M. Keck Foundation and the University of Virginia Pratt Committee. The authors declare that the experiments covered in this paper comply with current US laws governing the conduct of research.


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Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  • M. A. Phelan
    • 1
    Email author
  • J. L. Matta
    • 2
  • Y. M. Reyes
    • 3
  • R. Fernando
    • 4
  • R. A. Boykins
    • 5
  • R. S. Blanquet
    • 6
  1. 1.Division of Therapeutic Proteins, Office of Biotechnology ProductsFDABethesdaUSA
  2. 2.Department of Pharmacology and ToxicologyPonce School of MedicinePoncePuerto Rico
  3. 3.Cayey University CollegeUniversity of Puerto RicoCayeyPuerto Rico
  4. 4.Analytical and Chemical SciencesResearch Triangle InstituteResearch Triangle ParkUSA
  5. 5.Division of Bacterial, Parasitic and Allergenic Products, Office of Vaccine Research and ReviewFDABethesdaUSA
  6. 6.Department of BiologyGeorgetown UniversityWashingtonUSA

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