Isolation, Biochemical Characterization and Anti-adhesion Property of Mucin from the Blue Blubber Jellyfish (Catostylus mosaicus)  

Roger Pearson1 , Ross Tellam1 , Banglao Xu2 , Zhenjun Zhao2,3 , Mark Willcox2,3 , Kritaya Kongsuwan1
1. CSIRO Livestock Industries, Level 6 Queensland Bioscience Precinct, 306 Carmody Rd., St Lucia QLD 4067, Australia
2. Brien Holden Vision Institute, Level 4 North Wing, Rupert Myers Building, Gate 14 Barker Street, University of New South Wales, Kensington, NSW 2052, Australia
3. The School of Optometry and Vision Science, University of New South Wales, Kensington, NSW 2052, Australia
Author    Correspondence author
Bioscience Methods, 2011, Vol. 2, No. 4   doi: 10.5376/bm.2011.02.0004
Received: 18 May, 2011    Accepted: 23 May, 2011    Published: 03 Jun., 2011
© 2011 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Pearson et al., 2011, Isolation, biochemical characterization and anti-adhesion property of mucin from the blue blubber jellyfish (Catostylus mosaicus), Bioscience Methods, doi:10.5376/bm.2011.02.0004


Mucins are large glycoproteins that have been identified as the main component of various biological gels and lubricants. Their compositions contribute to the viscoelastic properties of mucus secretions. Gel-forming mucins have now been identified in a variety of organisms from marine molluscs to humans and are thought to cover and protect epithelial cells from attachment and entry of pathogens. We employed a new approach using a combination of tryptic digestion and the fractionation by hydrophobic interaction chromatography to enable the isolation and purification of mucins from the Blue Blubber jellyfish, Catostylus mosaicus. The purified proteins were stained with Alcian blue indicating extensive glycosylation. Amino acid composition analysis of the purified protein found that it was enriched for Ala, Glu, Thr, Pro and Val residues (together constituting ~93 mole % of the protein), which is typical for mucins. Consistent with this, monosaccharide composition analysis revealed extensive O-linked oligosaccharides with N-acetylgalactosamine (GalNAc), galactose (Gal) and N-acetylglucosamine (GlcNAc) as major monosaccharide constituents. The purified C. mosaicus mucins inhibited the attachment of an ocular Pseudomonas aeruginosa (PA) isolate (Paer6294) to human corneal epithelial (HCE) cells grown in vitro.

Mucin; Glycosylation; Protein purification; Bacterial anti-adhesion; Jellyfish
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