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1 Genome Center, Columbia University, New York, N.Y., USA; Genetics, Neurology and Neurological Sciences, Stanford University, Stanford, CA, USA; Anhui Medical University, Hefei, Anhui, China
2 The School of Public Health, Sun Yat-sen University, Guangzhou, Guangdong, China
* To whom correspondence should be addressed. E-mail: dw8{at}columbia.edu; dwang1@stanford.edu.
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 immunological 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 immunological evidences 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 immunological targets of other viral pathogens.
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