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Physiol. Genomics 18: 245-248, 2004. First published May 25, 2004; doi:10.1152/physiolgenomics.00102.2004
1094-8341/04 $5.00
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Received 28 April 2004; accepted in final form 13 May 2004.
Physiological Genomics 18:245-248 (2004)
1094-8341/04 $5.00 © 2004 American Physiological Society

Report

Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV

Denong Wang1,2,* and Jiahai Lu3,*

1 Columbia Genome Center, College of Physicians and Surgeons, Columbia University, New York, New York 10032
2 Departments of Genetics, Neurology and Neurological Sciences, Stanford University School of Medicine, Stanford, California 94305-5318
3 School of Public Health of Sun Yat-sen University, Guangzhou 510089, China

ABSTRACT

Using carbohydrate microarrays, we characterized the carbohydrate binding activity of SARS-CoV neutralizing antibodies elicited by an inactivated SARS-CoV vaccine. In these antibodies, we detected undesired autoantibody reactivity specific for the carbohydrate moieties of an abundant human serum glycoprotein asialo-orosomucoid (ASOR). This observation provides important clues for the selection of specific immunologic probes to examine whether SARS-CoV expresses antigenic structures that mimic the host glycan. We found that lectin PHA-L (Phaseolus vulgaris L.), which is specific for a defined complex carbohydrate of ASOR, stained the SARS-CoV-infected cells specifically and intensively. Taken together, we present immunologic evidence that a carbohydrate structure of SARS-CoV shares antigenic similarity with host glycan complex carbohydrates. The experimental approaches we applied in this study are likely applicable for the identification of immunologic targets of other viral pathogens.

microarray; carbohydrate; autoantigen; antibody and lectin; asialo-orosomucoid




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