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Degalactosylated and/or Denatured IgA, but Not Native IgA in Any Form, Bind to Mannose-Binding Lectin¹

Itaru Terai^2,*, Kunihiko Kobayashi, Jean-Pierre Vaerman and Naoki Mafune

^* Department of Pediatrics, Institute of Medical Science, Health Sciences University of Hokkaido, Sapporo, Japan; Department of Pediatrics, Hokkaido University Graduate School of Medicine and Sapporo Hokuyu Hospital, Sapporo, Japan; Unit of Experimental Medicine, Catholic University of Louvain, C. de Duve Institute of Cellular Pathology, Brussels, Belgium; and Laboratory of Medical Dietetics, Department of Food Science, Faculty of Dairy Science, Rakuno Gakuen University, Ebetsu, Japan

Mannose-binding lectin (MBL) is reported to bind to agalactosyl IgG, but not to normally galactosylated (native) IgG. It was recently reported that serum polymeric IgA in its native form reacts with MBL, whereas a more recent report has claimed that native IgD and IgE, and possibly IgM, do not. This led us to investigate whether IgA is truly reactive with MBL. To accomplish this, we collected purified human Igs, of various classes, subclasses, and allotypes, and tested their ability to bind to MBL using an ELISA method. Among these preparations, only one (monoclonal IgA2m(2):Kur) exhibited significant MBL binding. In particular, polymeric or monomeric forms of our normal serum IgA preparation lacked any ability to bind to MBL whatsoever. However, all the Ig preparations which had not bound to MBL became able to do so when they were degalactosylated with a galactosidase treatment, and the binding was further enhanced by acidic denaturation of the Igs. Among the degalactosylated and/or acid-denatured IgA, the IgA2 subclass exhibited a higher level of MBL binding than did IgA1. Our results suggest that MBL does not bind to native Igs (viewed in principle as "self" components), and that only Igs with abnormal glycosylation (degalactosylated forms) and/or denaturation would be MBL reactive.

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