Human monoclonal macroglobulins with specificity for Klebsiella K polysaccharides that contain 3,4-pyruvylated-D-galactose and 4,6-pyruvylated-D-galactose.

Abstract

Two human IgM myeloma proteins, IgMWEA and IgMMAY, were found to react with agar and Klebsiella polysaccharides that contain pyruvylated D-galactose (DGal). Quantitative precipitin data and precipitin inhibition studies with methyl alpha- and beta-glycosides of 4,6-pyruvylated-D-galactose showed their combining sites to be different, although each was directed against the pyruvylated-D-Gal, one reacting most specifically with Klebsiella polysaccharides with terminal nonreducing beta-linked 2,4 pyruvylated-D-Gal, whereas the other reacted equally well with Klebsiella polysaccharides that contain 3,4 beta-linked and 4,6 alpha-linked terminal nonreducing pyruvylated-DGal. Inhibition studies showed that both sites are directed toward one of the two space isomers of 3,4- or 4,6-pyruvylated DGal, the form in which the methyl group of the pyruvate is equatorial, or endo, and its carboxyl group axial, or exo, to the plane of the acetal ring. Coprecipitation studies showed the combining site of IgMWEA to be located on an (Fab')2 fragment and not on the (Fc)5mu fragment. The monoclonal peak in the serum of IgMMAY was specifically precipitated by Klebsiella polysaccharide. Myeloma proteins with specificities of this type may occur with reasonable frequency in humans and may be a consequence of clonal expansion from inapparent infection, carrier states, or disease produced by various Klebsiella organisms.

Distinct Immunomodulation of Bone Marrow-Derived Dendritic Cell Responses to Lactobacillus plantarum WCFS1 by Two Different Polysaccharides Isolated from Lactobacillus rhamnosus LOCK 0900

“…The presence of 4,6-0-(1-carboxyethylidene) ␣-galactose as a constituent of the backbone chain makes the structure of polysaccharide L900/2 uncommon. Previously, the pyruvic acid has been described in the exopolysaccharide of Lactobacillus rhamnosus strains RW-9595M and R (36), but mostly it has been reported to occur in extracellular acidic polysaccharides of pathogenic bacteria, including Streptococcus pneumoniae (37), Corynebacterium insidiosum (38), Escherichia coli (39), Klebsiella (40,41), Rhizobium (42), and Rhodococcus (32). The polymer L900/3, with a low average molecular mass of 1.8 kDa, contains five monosaccharide residues (two Glc, one Gal, one ManNAc, and one GalNAc) and one phosphate group in the repeating unit.…”

Homology of the NH2-terminal amino acid sequences of the heavy and light chains of human monoclonal lupus autoantibodies containing the dominant 16/6 idiotype.

“…Perhaps it is no coincidence that the WEA protein, which is structurally similar to four anti-DNA autoantibodies, binds to a capsular polysaccharide of Klebsiella pneumoniae (22). Analogous findings have recently been reported with monoclonal mouse antibodies.…”

Rapid Purification of Anti-I and Anti-i Cold Antibodies by Affinity Chromatography

“…There is no apparent similarity between the molecular structure of these beads, (D-galactose-3,6-anhydro-L-galactose)n [25], and the proposed sugar sequence which imparts i blood group specificity [1,2], Human monoclonal macroglobulins have been previously reported to react both with Sepharose [26] and agar components [26,27], This is the first report, however, to show that a specific monoclonal anti-i CA exhibits similar reactivity. It is interesting to note, too, that this serum could be inhibited by orosomucoid and purified i blood group sub stance at the same levels as all other anti-i serum tested.…”