Keyhole Limpet Hemocyanin (KLH) N-Glycans Share Similar Structural Features With Saccharides of Schistosoma, Trypanosoma, Leishmania, Cryptococcus, Aspergillis, Candida, E. coli, Salmonella, Clostridium and Hepatitis C virus (HCV)

Ref ID: 18731

Author:

J. S. Sundsmo, PhD – Vice President, R&D, H. Chow, PhD – Vice President, Product Development, M. Sagermann, PhD – Senior Scientist;

Author address:

Stellar Biotechnologies, Inc., Port Hueneme, CA.

Full conference title:

52nd Annual ICAAC

Date: 9 September 2014

Abstract:

Background: KLH is a highly immunogenic homo-didecameric (20-mer) protein complex obtained from the hemolymph of the marine mollusk Megathura crenulata. Widely used as a vaccine carrier in oncology with possible binding to mannose and fucose C-lectin receptors on antigen presenting cells (APCs), studies by Wirguin, 1995, Kurokawa 2002, Kantelhardt 2002 and Wuhrer 2004, summarized in Geyer 2005, established antigenic cross-reactions between KLH glycans and oligosaccharides of Schistosoma mansoni. Methods: As first step to identifying other possible microbial cross-reactions, KLH was subject to N-glycan profiling by hydrophilic interaction HPLC chromatography with fluorescence linker detection and electrospray ionization tandem mass spectrometry. Since KLH preparative methods could theoretically alter glycan structure, eight different commercial and research preparations were examined in an attempt to derive a consensus global glycan profile. Results: Fifty eight KLH N-glycan structures were identified. Of those 27 were reported previously, 13 were not reported before and 18 reported previously were not identified in any of the present preparations. To identify possible KLH N-glycans non-immunogenic in humans by virtue of their similarity with mammalian glycan structures, each of the 58 structures was compared with structures in the Consortium for Functional Glycomics database (www.functionalglycomics.org). Forty seven potentially non-immunogenic glycan structures were removed from consideration. The resultant 11 candidate immunogenic KLH N-glycans were used to query microbial glycomics structures in the scientific literature and in the Bacterial Carbohydrate Structure Database (csdb.glycoscience.ru/bacterial). Conclusions: Our results suggest structural similarities to Cryptococcus oligosaccharides, i.e., possibly related to serologic cross-reactions reported previously (May 2003). Other possible structural cross-reactive similarities were noted with Leishmania, Aspergillis, Candida, E. coli, Salmonella, Clostridium and Hepatitis C virus higher mannan and complex saccharide structures.

Abstract Number: B-053

Conference Poster: y

Conference Year: 2012

Link to conference website: NULL

New link: NULL

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