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Mannosylerythritol lipid, a yeast extracellular glycolipid, shows high binding affinity towards human immunoglobulin G.

Im JH, Nakane T, Yanagishita H, Ikegami T, Kitamoto D - BMC Biotechnol. (2001)

Bottom Line: The bound amount of HIgG increased depending on the attached amount of MEL-A onto poly (2-hydroxyethyl methacrylate) (polyHEMA) beads, whereas the amount of human serum albumin slightly decreased.The composite of MEL-A and polyHEMA, exhibited a significant binding constant of 1.43 x 10(6) (M(-1)) for HIgG, which is approximately 4-fold greater than that of protein A reported.MEL-A shows high binding-affinity towards HIgG, and this is considered to be due to "multivalent effect" based on the binding molar ratio.

View Article: PubMed Central - HTML - PubMed

Affiliation: Research Institute of Green Technology, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 5, 1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan. jaehong-im@aist.go.jp

ABSTRACT

Background: There have been many attempts to develop new materials with stability and high affinity towards immunoglobulins. Some of glycolipids such as gangliosides exhibit a high affinity toward immunoglobulins. However, it is considerably difficult to develop these glycolipids into the practical separation ligand due to their limited amounts. We thus focused our attention on the feasible use of "mannosylerythritol lipid A", a yeast glycolipid biosurfactant, as an alternative ligand for immunoglobulins, and undertook the investigation on the binding between mannosylerythritol lipid A (MEL-A) and human immunoglobulin G (HIgG).

Results: In ELISA assay, MEL-A showed nearly the same binding affinity towards HIgG as that of bovine ganglioside GM1. Fab of human IgG was considered to play a more important role than Fc in the binding of HIgG by MEL-A. The bound amount of HIgG increased depending on the attached amount of MEL-A onto poly (2-hydroxyethyl methacrylate) (polyHEMA) beads, whereas the amount of human serum albumin slightly decreased. Binding-amount and -selectivity of HIgG towards MEL-A were influenced by salt species, salt concentration and pH in the buffer solution. The composite of MEL-A and polyHEMA, exhibited a significant binding constant of 1.43 x 10(6) (M(-1)) for HIgG, which is approximately 4-fold greater than that of protein A reported.

Conclusions: MEL-A shows high binding-affinity towards HIgG, and this is considered to be due to "multivalent effect" based on the binding molar ratio. This is the first report on the binding of a natural human antibody towards a yeast glycolipid.

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Structure of mannosylerythritol lipids produced by Candida antarctica.
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Figure 1: Structure of mannosylerythritol lipids produced by Candida antarctica.

Mentions: The mixture of MELs were produced from methyl tetradecanoate with a yeast strain of Candida antarctica T-34 [32], and purified by silica-gel column chromatography as reported previously [17,18]. The purified 4-O-[(4', 6'-di-O-acetyl-2', 3'-di-O-alkanoyl)-β-D-mannopyranosyl]meso-erythritol (MEL-A) (Fig. 1), which is the major component of the yeast product, was exclusively used in the following experiments. MEL-A (mean Mw: 676) is sparingly soluble in water [33].


Mannosylerythritol lipid, a yeast extracellular glycolipid, shows high binding affinity towards human immunoglobulin G.

Im JH, Nakane T, Yanagishita H, Ikegami T, Kitamoto D - BMC Biotechnol. (2001)

Structure of mannosylerythritol lipids produced by Candida antarctica.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC57981&req=5

Figure 1: Structure of mannosylerythritol lipids produced by Candida antarctica.
Mentions: The mixture of MELs were produced from methyl tetradecanoate with a yeast strain of Candida antarctica T-34 [32], and purified by silica-gel column chromatography as reported previously [17,18]. The purified 4-O-[(4', 6'-di-O-acetyl-2', 3'-di-O-alkanoyl)-β-D-mannopyranosyl]meso-erythritol (MEL-A) (Fig. 1), which is the major component of the yeast product, was exclusively used in the following experiments. MEL-A (mean Mw: 676) is sparingly soluble in water [33].

Bottom Line: The bound amount of HIgG increased depending on the attached amount of MEL-A onto poly (2-hydroxyethyl methacrylate) (polyHEMA) beads, whereas the amount of human serum albumin slightly decreased.The composite of MEL-A and polyHEMA, exhibited a significant binding constant of 1.43 x 10(6) (M(-1)) for HIgG, which is approximately 4-fold greater than that of protein A reported.MEL-A shows high binding-affinity towards HIgG, and this is considered to be due to "multivalent effect" based on the binding molar ratio.

View Article: PubMed Central - HTML - PubMed

Affiliation: Research Institute of Green Technology, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 5, 1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan. jaehong-im@aist.go.jp

ABSTRACT

Background: There have been many attempts to develop new materials with stability and high affinity towards immunoglobulins. Some of glycolipids such as gangliosides exhibit a high affinity toward immunoglobulins. However, it is considerably difficult to develop these glycolipids into the practical separation ligand due to their limited amounts. We thus focused our attention on the feasible use of "mannosylerythritol lipid A", a yeast glycolipid biosurfactant, as an alternative ligand for immunoglobulins, and undertook the investigation on the binding between mannosylerythritol lipid A (MEL-A) and human immunoglobulin G (HIgG).

Results: In ELISA assay, MEL-A showed nearly the same binding affinity towards HIgG as that of bovine ganglioside GM1. Fab of human IgG was considered to play a more important role than Fc in the binding of HIgG by MEL-A. The bound amount of HIgG increased depending on the attached amount of MEL-A onto poly (2-hydroxyethyl methacrylate) (polyHEMA) beads, whereas the amount of human serum albumin slightly decreased. Binding-amount and -selectivity of HIgG towards MEL-A were influenced by salt species, salt concentration and pH in the buffer solution. The composite of MEL-A and polyHEMA, exhibited a significant binding constant of 1.43 x 10(6) (M(-1)) for HIgG, which is approximately 4-fold greater than that of protein A reported.

Conclusions: MEL-A shows high binding-affinity towards HIgG, and this is considered to be due to "multivalent effect" based on the binding molar ratio. This is the first report on the binding of a natural human antibody towards a yeast glycolipid.

Show MeSH
Related in: MedlinePlus