Studies on the specificity of the IgA-binding lectin, jacalin

The Glycosylation and Structure of Human Serum IgA1, Fab, and Fc Regions and the Role of N-Glycosylation on Fcα Receptor Interactions

“…Therefore, these data indicate that the amino acids at these positions were glycosylated. These data are consistent with jacalin precipitation studies of IgA1 fragments (60) , indicated by signal depression rather than absence, suggests that IgA1 exists as an array of glycoforms in which different potential O-glycan sites in the hinge region are occupied. In addition, each site may contain a range of oligosaccharides.…”

Serum IgA immune response to individual rotavirus polypeptides in young children with rotavirus infection

“…Because of difficulties to purify IgA from IgG it has not been possible to critically examine the role of IgA in virus induced mucosal infections. The previously described specificity ofjacalin for human IgA [3,14,24,26] together with the described IgA-RIPA now provides possibilities not only to dissect human IgA responses in greater detail, but also to examine protective and type-specific IgA immune responses.…”

“…In this report a novel lectin (jacalin) based IgA-RIPA was established and used to examine the IgA antibody response in human sera against individual rotavirus proteins. The described IgA-RIPA included a human IgA binding lectin jacalin [24,26] and high salt concentrations in the buffer instead of SDS [29], which favors detection of antibodies to conformationdependent epitopes.…”

“…Jacalin, a novel galactose-specific lectin prepared from the jack-fruit, Artrocarpus integrifolia, has been reported to specifically bind to h u m a n immunoglobulin A, and has been used to separate this immunoglobulin from IgG and IgM [24,26]. Of the two existing subclasses of IgA in serum [3,14] the specificity of jacalin is mainly directed to the most prevalent subclass, Ig A1.…”

NAI1 Gene Encodes a Basic-Helix-Loop-Helix–Type Putative Transcription Factor That Regulates the Formation of an Endoplasmic Reticulum–Derived Structure, the ER Body

“…Each of these regions is homologous to the a-chain of jacalin, a carbohydrate binding protein (lectin) isolated from jackfruit (Artocarpus integrifolia) (Yang and Czapla, 1993). The a-chain of jacalin has been shown to bind IgA 1 from human serum, specifically through the oligosaccharides of the IgA 1 hinge region (Skea et al, 1988;Biewenga et al, 1989;Sankaranarayanan et al, 1996). Myrosinase binding protein 70p (MBP70p) from Brassica napus has three jacalin-homologous regions (repeats 1 to 3 in Figure 9A) (Geshi and Brandt, 1998).…”