Yamaguchi T, Yamada A, Hong N, Ogawa T, Ishii T, Shibuya N Differences in the recognition of glucan elicitor signals between rice and soybean: β-glucan fragments from the rice blast disease fungus Pyricularia oryzae that elicit phytoalexin biosynthesis in suspension-cultured rice cells Plant Cell12 (2000)
817–826
The structure was elucidated in this paper Publication DOI:10.1105/tpc.12.5.817 Journal NLM ID:9208688 Publisher: Rockville, MD: American Society of Plant Physiologists Correspondence: shibuyaabr.affrc.go.jp Institutions: Department of Biotechnology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki 305-0826, Japan, Bio-Oriented Technology Research Advancement Institute, Tokyo 105-0001, Japan, Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan, Forestry and Forest Products Research Institute, Tsukuba, Ibaraki 305-8687, Japan
Partial acid/enzymatic hydrolysis of the β-(1→3, 1→6)-glucan from the cell walls of the rice blast disease fungus Pyricularia oryzae (Magnaporthe grisea) released elicitor-active fragments that induced phytoalexin biosynthesis in suspension-cultured rice cells. From the digestion of the glucan by an endo-β-(1→3)-glucanase, one highly elicitor-active glucopentaose was purified as a reduced compound, tetraglucosyl glucitol. The structure of this tetraglucosyl glucitol as well as two other related tetraglucosyl glucitols was elucidated as follows: (1) Glcβ(1→3)Glcβ(1→3)(Glcβ(1→6)) Glcβ(1→3)Glucitol (most active fragment); (2) Glcβ(1→3)(Glcβ(1→6))Glcβ(1→3)Glcβ(1→3)Glucitol; and (3) Glcβ(1→6) Glcβ(1→3)Glcβ(1→3)Glcβ(1→3)Glucitol. However, a synthetic hexa-β-glucoside, known as a minimal structural element for the phytoalexin elicitor for soybean cotyledon cells, did not induce phytoalexin biosynthesis in the rice cells. Conversely, the β-glucan fragment from P. oryzae did not induce phytoalexin biosynthesis in the soybean cotyledon cells, indicating differences in the recognition of glucooligosaccharide elicitor signals in these two plants. Because rice cells have been shown to recognize chitin fragments larger than pentamers as potent elicitors, these results also indicate that the rice cells can recognize at least two types of oligosaccharides from fungal cell walls as signal molecules to initiate defense response.
Yamaguchi T, Yamada A, Hong N, Ogawa T, Ishii T, Shibuya N Differences in the recognition of glucan elicitor signals between rice and soybean: β-glucan fragments from the rice blast disease fungus Pyricularia oryzae that elicit phytoalexin biosynthesis in suspension-cultured rice cells Plant Cell12 (2000)
817–826
The structure was elucidated in this paper Publication DOI:10.1105/tpc.12.5.817 Journal NLM ID:9208688 Publisher: Rockville, MD: American Society of Plant Physiologists Correspondence: shibuyaabr.affrc.go.jp Institutions: Department of Biotechnology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki 305-0826, Japan, Bio-Oriented Technology Research Advancement Institute, Tokyo 105-0001, Japan, Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan, Forestry and Forest Products Research Institute, Tsukuba, Ibaraki 305-8687, Japan
Partial acid/enzymatic hydrolysis of the β-(1→3, 1→6)-glucan from the cell walls of the rice blast disease fungus Pyricularia oryzae (Magnaporthe grisea) released elicitor-active fragments that induced phytoalexin biosynthesis in suspension-cultured rice cells. From the digestion of the glucan by an endo-β-(1→3)-glucanase, one highly elicitor-active glucopentaose was purified as a reduced compound, tetraglucosyl glucitol. The structure of this tetraglucosyl glucitol as well as two other related tetraglucosyl glucitols was elucidated as follows: (1) Glcβ(1→3)Glcβ(1→3)(Glcβ(1→6)) Glcβ(1→3)Glucitol (most active fragment); (2) Glcβ(1→3)(Glcβ(1→6))Glcβ(1→3)Glcβ(1→3)Glucitol; and (3) Glcβ(1→6) Glcβ(1→3)Glcβ(1→3)Glcβ(1→3)Glucitol. However, a synthetic hexa-β-glucoside, known as a minimal structural element for the phytoalexin elicitor for soybean cotyledon cells, did not induce phytoalexin biosynthesis in the rice cells. Conversely, the β-glucan fragment from P. oryzae did not induce phytoalexin biosynthesis in the soybean cotyledon cells, indicating differences in the recognition of glucooligosaccharide elicitor signals in these two plants. Because rice cells have been shown to recognize chitin fragments larger than pentamers as potent elicitors, these results also indicate that the rice cells can recognize at least two types of oligosaccharides from fungal cell walls as signal molecules to initiate defense response.
Yamaguchi T, Yamada A, Hong N, Ogawa T, Ishii T, Shibuya N Differences in the recognition of glucan elicitor signals between rice and soybean: β-glucan fragments from the rice blast disease fungus Pyricularia oryzae that elicit phytoalexin biosynthesis in suspension-cultured rice cells Plant Cell12 (2000)
817–826
The structure was elucidated in this paper Publication DOI:10.1105/tpc.12.5.817 Journal NLM ID:9208688 Publisher: Rockville, MD: American Society of Plant Physiologists Correspondence: shibuyaabr.affrc.go.jp Institutions: Department of Biotechnology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki 305-0826, Japan, Bio-Oriented Technology Research Advancement Institute, Tokyo 105-0001, Japan, Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan, Forestry and Forest Products Research Institute, Tsukuba, Ibaraki 305-8687, Japan
Partial acid/enzymatic hydrolysis of the β-(1→3, 1→6)-glucan from the cell walls of the rice blast disease fungus Pyricularia oryzae (Magnaporthe grisea) released elicitor-active fragments that induced phytoalexin biosynthesis in suspension-cultured rice cells. From the digestion of the glucan by an endo-β-(1→3)-glucanase, one highly elicitor-active glucopentaose was purified as a reduced compound, tetraglucosyl glucitol. The structure of this tetraglucosyl glucitol as well as two other related tetraglucosyl glucitols was elucidated as follows: (1) Glcβ(1→3)Glcβ(1→3)(Glcβ(1→6)) Glcβ(1→3)Glucitol (most active fragment); (2) Glcβ(1→3)(Glcβ(1→6))Glcβ(1→3)Glcβ(1→3)Glucitol; and (3) Glcβ(1→6) Glcβ(1→3)Glcβ(1→3)Glcβ(1→3)Glucitol. However, a synthetic hexa-β-glucoside, known as a minimal structural element for the phytoalexin elicitor for soybean cotyledon cells, did not induce phytoalexin biosynthesis in the rice cells. Conversely, the β-glucan fragment from P. oryzae did not induce phytoalexin biosynthesis in the soybean cotyledon cells, indicating differences in the recognition of glucooligosaccharide elicitor signals in these two plants. Because rice cells have been shown to recognize chitin fragments larger than pentamers as potent elicitors, these results also indicate that the rice cells can recognize at least two types of oligosaccharides from fungal cell walls as signal molecules to initiate defense response.
Komae K, Komae A, Misaki A A 4,5-unsaturated low molecular oligogalacturonide as a potent phytoalexin-elicitor isolated from polygalacturonide of Ficus awkeotsang Agricultural and Biological Chemistry54 (1990)
1477-1484
Journal NLM ID:0370452 WWW link:http://ci.nii.ac.jp/naid/110006324975 Publisher: Tokyo: Agricultural Chemical Society Of Japan Institutions: Department of Food and Nutrition, Faculty of Science of Living, Osaka City University, Osaka, Japan
A highly methyl esterified linear α-(1→4)-linked polygalacturonide, isolated from a water extract of seeds of Ficus awkeotsang Makino, was used for the study of elicitor-active oligo-saccharides on host-parasite interactions in higher plants. Oligogalacturonides (OLGAs), obtained from awkeotsang polygalacturonide or low methyl esterified apple pectin by treatment with the purified endo-pectate lyase (EC 4.2.2.2) of Erwinia carotovora, were found to induce glyceollin accumulation in soybean cotyledons. The de-esterified awkeotsang-OLGAs was precisely fractionated by anion-exchange chromatography using a QAE-Sephadex A-25 column, and was assayed for the elicitor activity. Among the purified Oligogalacturonides with DP 3 to 12, it was found that 4,5-unsaturated hexa-α-1,4-galacturonide of the low molecular elicitor-active Oligogalacturonides (DP 5 to 7) also was a potent elicitor as well as the 4,5-unsaturated deca-α-1,4-galacturonide of the high molecular elicitor-active Oligogalacturonides (DP 9 to 11) previously reported by Davis et al.
Found 
report error
(later renamed to: Magnaporthe oryzae Ken-60-19)
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