Jacalin: A new laboratory tool in immunochemistry and cellular immunology

Abstract

In recent years, a new lectin--jacalin--has raised the interest of immunologists because of its original properties with respect to human immunoglobulins and lymphocytes. Its structure and carbohydrate binding specificity are now well documented, and it can be purified easily from jackfruit seeds by ion exchange or affinity chromatography. The binding and precipitating specificities of jacalin with heavy chains of human immunoglobulins allow its use as a diagnostic (IgA subclass typing) and preparative tool (purification of IgA and IgD, removal of IgA from biologic samples and preparations). Other possible applications of jacalin's binding properties also can be envisaged. In addition, the lectin displays a mitogenic activity specific for human CD4 T-lymphocytes; consequently, the proliferative response induced by jacalin appears to represent a new and interesting assay for a functional study of CD4 cells, with obvious applications in primary and acquired, especially AIDS, immune deficiency states.

The lectin jacalin induces phosphorylation of ERK and JNK in CD4+ T cells

“…Lectins such as phytohemagglutinin (PHA) and concanavalin A are mitogenic to all T cells, whereas jacalin, a purified lectin from jackfruit, is mitogenic only for CD4 ϩ T cells [29,30]. Jacalin is a plant lectin that induces mitogenic responses selectively in CD4 ϩ T lymphocytes and has been shown to block infection by HIV-1 in a T lymphoid cell line [31].…”

AtJAC1 Regulates Nuclear Accumulation of GRP7, Influencing RNA Processing of FLC Antisense Transcripts and Flowering Time in Arabidopsis

“…As a subgroup of lectins, Jacalin-lectin proteins have one or more jacalin-like lectin domains with binding specificity to Man or Gal (Kabir, 1998;Peumans et al, 2001). They are involved in multiple biological processes (Aucouturier et al, 1989;Yong et al, 2003;Jiang et al, 2006). Arabidopsis (Arabidopsis thaliana) JASMONATE ACID RESPONSE1 and wheat (Triticum aestivum) JACALIN-RELATED LECTIN LIKE1 are involved in jasmonic acid-mediated defense responses (León et al, 1998;Xiang et al, 2011).…”

Inhibition of human immunodeficiency virus infection by the lectin jacalin and by a derived peptide showing a sequence similarity with gp120

“…The glycosylated and unglycosylated a-subunits were isolated by preparative SDS-PAGE according to Aucouturier et al [22]. Separated chains were then electroeluted; SDS was removed by chromatography on Extracti gel D column (Pierce) equilibrated with 0.05 M Tris buffer (pH 9).…”

“…Jacalin, the Gal Pl-3 Gal-Nac binding lectin from jackfruit (Artocarpus heterophyllus) is commonly used in immunochemistry because of its human IgAl and IgD binding specificity (reviewed in [22]). This 50-kDa molecule is made up of non-covalently linked 133 amino acid a subunits, one 15-kDa glycosylated and one 12-kDa unglycosylated subunit, and of a minor component, a small peptide of 20 residues, the p subunit [23, 241. Jacalin was recently shown to be selectively mitogenic for human CD4+ T lymphocytes, although it binds every blood cell through several membrane molecules [25].…”