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Structure type: homopolymer ; n is large
Trivial name: β-1,3-glucan, pachyman, curdlan, SSG
Compound class: EPS, glucan, cell wall glucn, cell wall glucan, cell wall glucoprotein
Contained glycoepitopes: IEDB_1397514,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_2278476,IEDB_2278477,IEDB_558869,IEDB_857743,IEDB_983931,SB_192

• Article ID: 1734
  Hrmova M, Fincher GB "Purification and properties of three (1-3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)" - Biochemical Journal 289 (1993) 453-461
  

  Three (1→3)-β-D-glucan glucanohydrolase (EC 3.2.1.39) isoenzymes GI, GII and GIII were purified from young leaves of barley (Hordeum vulgare) using (NH4)2SO4 fractional precipitation, ion-exchange chromatography, chromatofocusing and gel-filtration chromatography. The three (1→3)-β-D-glucanases are monomeric proteins of apparent M(r)32,000 with pI values in the range 8.8-10.3. N-terminal amino-acid-sequence analyses confirmed that the three isoenzymes represent the products of separate genes. Isoenzymes GI and GII are less stable at elevated temperatures and are active over a narrower pH range than is isoenzyme GIII, which is a glycoprotein containing 20-30 mol of hexose equivalents/mol of enzyme. The preferred substrate for the enzymes is laminarin from the brown alga Laminaria digitata, an essentially linear (1→3)-β-D-glucan with a low degree of glucosyl substitution at 0-6 and a degree of polymerization of approx. 25. The three enzymes are classified as endohydrolases, because they yield (1→3)-β-D-oligoglucosides with degrees of polymerization of 3-8 in the initial stages of hydrolysis of laminarin. Kinetic analyses indicate apparent Km values in the range 172-208 microM, kcat. constants of 36-155 s-1 and pH optima of 4.8. Substrate specificity studies show that the three isoenzymes hydrolyse substituted (1→3)-β-D-glucans with degrees of polymerization of 25-31 and various high-M(r), substituted and side-branched fungal (1→3;1→6)-β-D-glucans. However, the isoenzymes differ in their rates of hydrolysis of a (1→3;1→6)-β-D-glucan from baker's yeast and their specific activities against laminarin vary significantly. The enzymes do not hydrolyse (1→3;1→4)-β-D-glucans, (1→6)-β-D-glucan, CM-cellulose, insoluble (1→3)-β-D-glucans or aryl β-D-glycosides.

  NCBI PubMed ID: 8424790
  Publication DOI: 10.1042/bj2890453
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Institutions: Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia
  Methods: enzymatic digestion, ion-exchange chromatography, enzymatic assays, gel electrophoresis, amino acid sequence analysis, isoelectric focusing, chromatofocusing
  
   
  
  Alcaligenes faecalis, Poria cocos
  CSDB ID 106266 (all data & tools)
• Article ID: 4180
  Bertram PA, Buller CS, Stewart GC, Akagi JM "Isolation and characterization of a Bacillus strain capable of degrading the extracellular glucan from Cellulomonas flavigena strain KU" - Journal of Applied Bacteriology 74 (1993) 460-466
  

  Bacteria capable of utilizing the water-insoluble purified extracellular (1→3)-β-D-glucan (curdlan) from Cellulomonas flavigena strain KU by extracellular enzymes, were isolated and characterized. Enrichment cultures from a Winogradsky column were incubated anaerobically at 55 degrees C with curdlan as the sole source of carbon. Colonies surrounded by zones of clearing were selected from subcultures on solid curdlan media. One of the isolates was chosen for further study and identified by conventional methods, API-tests with calculation of similarity coefficients and ID-scores, estimation of mol% (G+C) and DNA-DNA liquid hybridization. The isolate is a facultatively anaerobic, facultatively thermophilic Bacillus sp. Identification at the species-level was not achieved. The isolate was characterized by some rare traits among bacilli, but it remains unresolved whether it defines a new taxon.

  NCBI PubMed ID: 8486553
  Journal NLM ID: 7503050
  Institutions: University of Kansas, Department of Microbiology, Lawrence 66045
  
   
  
  Cellulomonas flavigena KU
  CSDB ID 131674 (all data & tools)
• Article ID: 4213
  Bertram PA, Chen P, Buller CS, Akagi JM "Endo-(1-3)-β-D-glucanase activity secreted by Bacillus sp. no. 215" - Letters in Applied Microbiology 19 (1994) 349-352
  

  The production of an extracellular endo-(1→3)-β-D‐glucanase by Bacillus sp. no. 215 was induced during growth with (1→3)-β-D-glucan (curdlan) from Cellulomonas flavigena strain KU as carbon and energy source. Maximum levels of activity (0.26 U ml-1 resp. 1.40 U mg-1) were detected in cell-free culture supernatant fluid after 25 h of aerobic growth at 55°C. The cells secreted an endo-(1→3)-β-D-glucanase with low electrophoretic mobility that used curdlan from C. flavigena strain KU and from Agrobacterium sp. (formerly Alcaligenes faecalis var. myxogenes) as substrates. The enzyme activity was highest at pH 7.0 and 55°C. It exhibited a remarkably low thermal stability with a half‐life of 14 min at 55°C in the presence of substrate. Divalent metal cations were required for enzyme activity.

  Publication DOI: 10.1111/j.1472-765X.1994.tb00472.x
  Journal NLM ID: 8510094
  Institutions: Department of Microbiology, University of Kansas, Lawrence, KS, USA
  
   
  
  Cellulomonas flavigena KU
  CSDB ID 142890 (all data & tools)
• Article ID: 6674
  Rouhier P, Bruneteau M, Michel G, Fiema J, Zurzycka A "Structural characterization of alkali-soluble glucans from the mycelium of Aspergillus giganteus mut. alba" - Carbohydrate Research 262 (1994) 155-159
  
  Journal NLM ID: 0043535
  Publisher: Elsevier
  
   
  
  Aspergillus giganteus mut. alba
  CSDB ID 118123 (all data & tools)
• Article ID: 6677
  Kreger DR "On the nature and formation of the fibrillar nets produced by protoplasts of Saccharomyces cerevisiae in liquid media: An electronmicroscopic, X-ray diffraction and chemical study" - Journal of General Microbiology 92 (1975) 207-220
  
  Journal NLM ID: 0375371
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 139820 (all data & tools)
• Article ID: 6679
  Gabriel M, Kopecka M "Studies on cell division in regenerating protoplasts of the yeast Schizosaccharomyces japonicus" - Journal of General Microbiology 134 (1988) 2029-2037
  
  Journal NLM ID: 0375371
  
   
  
  Schizosaccharomyces japonicus
  CSDB ID 139829 (all data & tools)
• Article ID: 6691
  Nollstadt KH, Powles MA, Fujioka H, Aikawa M, Schmatz DM "Use of b-1,3-glucan specific antibody to study the cyst wall of Pneumocystis carinii and effects of Pneumocandin B0 analog L-733,560" - Antimicrobial Agents and Chemotherapy 38 (1994) 2258-2265
  

  A new class of promising antipneumocystis agents, cyclic lipopeptide pneumocandin analogs, has been shown to effectively prevent Pneumocystis carinii cyst development in murine models. These compounds are believed to inhibit the biosynthesis of β-1,3-glucan, a major constituent of the cell walls of various pathogenic fungi. However, all evidence of the presence of this polymer in P. carinii cysts is based on indirect methods. To address this, highly specific rabbit polyclonal antiserum was raised against a laminariheptaose-human transferrin hapten conjugate. This antiserum was used to demonstrate the presence of β-1,3-glucan in alkaline extracts of P. carinii-infected rat lung tissue and to quantitate the degree of infection in this tissue as laminarin equivalents. The antiserum was also used to localize β-1,3-glucan in P. carinii-infected rat lung tissue at the transmission electron microscopic level by immunogold labeling. High concentrations of β-1,3-glucan were present in the electron-lucent layer of the P. carinii cyst wall, but β-1,3-glucan was absent from intracystic bodies and trophozoites. Ultrastructural evaluation of lung tissue from P. carinii-infected rats treated with the pneumocandin analog L-733,560 demonstrated that the few cysts which remained are deformed, lack the translucent layer of the cyst wall, and contain minimal amounts of β-1,3-glucan.

  NCBI PubMed ID: 7840554
  Journal NLM ID: 0315061
  Institutions: Department of Parasite Biochemistry & Cell Biology, Merck Research Laboratories, Rahway, New Jersey 07065
  
   
  
  Pneumocystis carinii
  CSDB ID 103899 (all data & tools)
• Article ID: 6705
  Nakao A, Kato H, Kanbe T, Tanaka K, Tamura H, Tanaka S, Takagi H "Quantitative assay of (1-3)-β-D-glucan in culture media of Candida albicans using the G-test" - European Surgical Research 26 (1994) 194-200
  

  The diagnosis of invasive candidiasis is often difficult. The limulus test, which has been used for the assay of endotoxin in blood, was also found to react with (1-3)-β-D-glucan, a component of the fungal cell wall. The factor in the limulus test that is activated by glucan, but not by endotoxin, is called factor G. The G-test utilizes the activation pathway starting with factor G, and sensitivity reacts with trace amounts of glucan. In this study, we investigated in vitro proliferation of Candida albicans and changes in the glucan concentration of RPMI-1640 media in the presence and absence of neutrophils and antifungal agents, as a pilot evaluation to possible clinical applications of the G-test. The proliferation of C. albicans and the glucan level measured in the culture media showed parallel changes. The glucan level in the culture media also increased when C. albicans was phagocytosed and digested by neutrophils, but not with administration of amphotericin B. The G-test closely reflected quantitative changes of C. albicans in vitro, and should be considered for future clinical studies in the diagnosis and evaluation of therapeutics in invasive candidiasis.

  NCBI PubMed ID: 8005180
  Journal NLM ID: 0174752
  Publisher: Karger
  Institutions: Department of Surgery II, Nagoya University School of Medicine, Japan
  
   
  
  Candida albicans
  CSDB ID 125281 (all data & tools)
• Article ID: 6708
  Vallot N, Boudard F, Bastide M "Effect of a (1-3)-b-D-glucan, pichilan, extracted from Pichia fermentans on a murine macrophage cell line" - International Journal of Immunopathology and Pharmacology 7 (1994) 21-35
  
  Journal NLM ID: 8911335
  Publisher: Biomedical Research Press
  
   
  
  Pichia fermentans
  CSDB ID 130953 (all data & tools)
• Article ID: 6709
  Gallin EK, Green SW, Patchen ML "Comparative effects of particulate and soluble glucan on macrophages of C3H/HeN and C3H/HeJ mice" - International Journal of Immunopharmacology 14 (1992) 173-183
  

  In order to compare both the actions of soluble glucan (glucan-F) and particulate glucan (glucan-P) on macrophages and the responsiveness of macrophages from C3H/HeJ and C3H/HeN mice to these immunomodulators, interleukin-1 (IL-1) levels, phagocytosis and superoxide production were monitored after an in vitro exposure to glucan-F or glucan-P. A 2 or 20 h exposure to either glucan preparation decreased the ability of both C3H/HeJ and C3H/HeN macrophages to ingest zymosan. In contrast, glucan-P, but not glucan-F, decreased (after a 20 h exposure) the uptake of both IgG opsonized erythrocytes and latex beads. Furthermore, glucan-P, but not glucan-F was as effective as zymosan (after a 1 h exposure) in inducing superoxide release by macrophages isolated from both C3H/HeN and C3H/HeJ mice. While the effects of glucan-P on PMA-induced superoxide release and IL-1 levels were similar in macrophages from C3H/HeJ and C3H/HeN mice, glucan-F was ineffective at enhancing PMA-induced superoxide release or increasing IL-1 levels in C3H/HeJ mice. Thus (1) the effects of glucan-P on phagocytosis of opsonized erythrocytes and latex beads are not mimicked by glucan-F and (2) while macrophages from C3H/HeJ mice respond normally (as compared with C3H/HeN macrophages) to glucan-P, they are hyporesponders to glucan-F. These findings indicate that the activation of macrophages by glucan-P involves different (or additional) pathways from those activated by glucan-F.

  NCBI PubMed ID: 1320591
  Journal NLM ID: 7904799
  Publisher: Elsevier
  Institutions: Department of Physiology, Armed Forces Radiobiology Research Institute, Bethesda, MD 20889
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 130960 (all data & tools)
• Article ID: 6710
  Sakurai T, Hashimoto K, Suzuki I, Ohno N, Oikawa S, Masuda A, Yadomae T "Enhancement of murine alveolar macrophage functions by orally administered b-glucan" - International Journal of Immunopharmacology 14 (1992) 821-830
  

  The effect of orally administered SSG, a β-1,3-glucan obtained from the culture filtrate of the fungus Sclerotinia sclerotiorum IFO 9395, on alveolar macrophage (AM) functions of CDF1 mice was examined. SSG administered orally (20, 40, 80 or 160 mg/kg) for 10 consecutive days enhanced the lysosomal enzyme activity of AM. The greatest enhancing effect was observed at 80 mg/kg of SSG. Multiple oral administrations of SSG (10 consecutive days) were needed to induce significant enhancing effects. Phagocytic activity and interleukin-1 (IL-1) production of AM were also augmented by oral administration of SSG, and the kinetics of the activated state differed depending on the kind of activity. However, H2O2 production of AM was not affected by SSG. Orally administered SSG also (40 or 80 mg/kg, 10 consecutive days) increased the number of AM and the greatest increment was observed 14 days after the first administration. On the other hand, the supernatant of Peyer's patch (PP) cells from mice administered SSG (80 mg/kg) orally stimulated the lysosomal enzyme activity of AM in vitro, and enhanced colony stimulating activity (CSA) was detected from this supernatant. These results demonstrate that SSG given by the oral route can activate murine AM both qualitatively and quantitatively, and it would mediated, at least in part, by the activation of PP cells in the intestine.

  NCBI PubMed ID: 1512075
  Journal NLM ID: 7904799
  Publisher: Elsevier
  Institutions: Laboratory of Immunopharmacology of Microbial Products, Tokyo College of Pharmacy, Japan
  
   
  
  Sclerotinia sclerotiorum IFO 9395
  CSDB ID 130963 (all data & tools)
• Article ID: 6751
  Ohno N, Saito K, Nemoto J, Kaneko S, Adachi Y, Nishijima M, Miyazaki T, Yadomae T "Immunopharmacological characterization of a highly branched fungal (1- 3)-b-D-Glucan, OL-2, isolated from Omphalia lapidescens" - Biological and Pharmaceutical Bulletin 16 (1993) 414-419
  

  The immunopharmacological activities of a fungal (1→3)-β-D-glucan, OL-2, isolated from "Leiwan" Omphalia lapidescens were examined. Intraperitoneal (i.p.) administration of OL-2 to ICR mice induced a significant number of peritoneal exudate cells (PEC) and white blood cells over the period of a few days. Spleen cell numbers were also increased by i.p. administration of OL-2 at about a week. These changes reverted to the normal level within a month. Responses of spleen cells and bone marrow cells (BM) to colony stimulating factors (CSF) were augmented by OL-2 administration assessed by cell proliferation assay. Sera from OL-2 administered mice contained an increased concentration of colony stimulating activity. Gene expressions of interleukin-1 β, interleukin-6, and tumor necrosis factor alpha in the spleen were also increased. These results suggested the activation of hematopoietic responses, and would well relate to the incremental increase in PEC, white blood cell and spleen cell numbers. OL-2 also increased the serum concentration of fibronectin and complement component C-3. However, OL-2 did not show adjuvant activity to SRBC and antitumor activity against the solid form of Sarcoma 180 by i.p. administration. Yet, OL-2 did not interfere with the antitumor activity of SSG against the same tumor system. These facts suggested that OL-2 could enhance nonspecific host defense mechanisms by enhancing hematopoietic responses, but would not enhance or inhibit the specific immunity mediated by lymphocytes.(ABSTRACT TRUNCATED AT 250 WORDS)

  NCBI PubMed ID: 8358393
  Journal NLM ID: 9311984
  Publisher: Pharmaceutical Society of Japan
  Institutions: Tokyo College of Pharmacy, Japan
  
   
  
  Sclerotinia sclerotiorum IFO 9395
  CSDB ID 110076 (all data & tools)
• Article ID: 6752
  Suda M, Ohno N, Adachi Y, Yadomae T "Relationship between the tissue distribution and antitumor activity of highly branched (1-3)-b-D-Glucan, SSG" - Biological and Pharmaceutical Bulletin 17 (1994) 131-135
  

  Distribution of 3H-labeled (1→3)-β-D-glucan([3H]SSG) obtained from the culture filtrate of Sclerotinia sclerotiorum IFO 9395, in various tissues in tumor-bearing mice was examined. [3H]SSG administered intra-peritoneally was mainly detected in liver, spleen, kidney and tumor masses. In contrast to i.p. administration, intra-lesionally administered [3H]SSG was not released from the tumor. Similarly, in a double grafted tumor system, [3H]SSG was located in the administered tumor and not distributed in the distant site tumor, in spite of the fact that significant antitumor effect was shown in both tumor sites in this system. Winn assay confirmed the activation of the systemic antitumor immunity. These results suggested that the distribution of glucans would be one important factor in determining their antitumor effects. However, this would not always be necessary if systemic immunity could be induced.

  NCBI PubMed ID: 8148801
  Journal NLM ID: 9311984
  Publisher: Pharmaceutical Society of Japan
  Institutions: Laboratory of Immunopharmacology of Microbial Products, Tokyo College of Pharmacy, Japan
  
   
  
  Sclerotinia sclerotiorum IFO 9395
  CSDB ID 110100 (all data & tools)
• Article ID: 6754
  Ohno N, Asada N, Adachi Y, Yadomae T "Enhancement of LPS triggered TNF-alpha (tumor necrosis factor-alpha) production by (1->3)-b-D-glucans in mice" - Biological and Pharmaceutical Bulletin 18 (1995) 126-133
  

  Effects of (1→3)-β-D-glucans on tumor necrosis factor alpha (TNF-α) production in mice in vivo were investigated with or without triggering stimulation of lipopolysaccharide (LPS). Administration of grifolan (GRN) (100-250 micrograms/mouse) obtained from Grifola frondosa, did not elevate the TNF-α concentration in serum, but significantly elevated LPS (10 micrograms/mouse)-elicited TNF-α production in serum. The priming effect was observed as early as 2 h after administration and remained high for 3 weeks. The priming effect was dependent on the strain of mice, i.e. ICR, BALB/c, and MRL/lpr (15 weeks old) showed high response. In addition, GRN administration increased membrane-bound TNF-α assessed by Western blotting and flow cytometry. Comparing the activity using structurally related glucans obtained from other microorganisms, highly branched glucans, SSG isolated from Sclerotinia sclerotiorum IFO 9395 and OL-2 from Omphalia lapidescence significantly increased TNF-α production. Small molecular weight GRN derivatives prepared by heat degradation method showed weaker priming effect. These facts suggested that the glucans showed priming effect of TNF-α production in vivo and that this effect was related to the degree of branching and molecular weight.

  NCBI PubMed ID: 7735226
  Journal NLM ID: 9311984
  Publisher: Pharmaceutical Society of Japan
  Institutions: Tokyo College of Pharmacy, Japan
  
   
  
  Sclerotinia sclerotiorum IFO 9395
  CSDB ID 110138 (all data & tools)
• Article ID: 6755
  da-Silva MM, Polizeli MLTM, Jorge JA, Terenzi HF "Cell wall deficiency in 'slime' strains of Neurospora crassa: osmotic inhibition of cell wall synthesis and b-D-glucan synthase activity" - Brazilian Journal of Medical and Biological Research = Revista brasileira de pesquisas médicas e biológicas 27 (1994) 2843-2857
  

  1. The RCP-3 S/H mutant of Neurospora crassa was obtained by vegetative selection in medium of high osmolarity of a mycelial form of an fz, sg, os-1 ("slime"-like) segregant. The mutant exhibits spheroplast-hyphal dimorphism conditioned by the osmolarity of the culture medium (Pietro et al. (1990). Journal of General Microbiology, 136: 121-129). The carbohydrate composition of the cell wall of the mutant was different from that of the wild type in the absence of an alkali-soluble galactosaminoglycan polymer. Furthermore the mutant cell wall had a somewhat lower content of β-glucan relative to that of chitin. 2. Increasing concentrations of sorbitol in the culture medium of the mutant inhibited by 10-fold the formation of cell wall relative to total biomass. The cell wall of the mutant cultured in the presence of sorbitol lacked mannose- and galactose-containing polymers, and also showed progressively lower amounts of β-glucan relative to chitin. 3. The activity of membrane-bound (1-3)-β-D-glucan synthase from the mutant grown in the absence of sorbitol shared several properties with the wild type enzyme (i.e., Km app., Vmax, stability at 30 degrees C, activation by GTP gamma S, and dissociability by treatment with NaCl and Tergitol NP-40 into a membrane-bound catalytic center and a GTP-binding activating protein). On the other hand, the enzyme from the mutant but not that from the wild type was inactivated by about 15% by treatment with NaCl and detergent. 4. At high concentrations of sorbitol (1.0 M) the RCP-3 S/H mutant exclusively produced spheroplasts devoid of (1-3)-β-D-glucan synthase activity. The defect was at the level of the membrane-bound catalytic center. The activity of the GTP-binding activating factor was apparently normal in these cells. 5. These results suggest that the definitive loss of cell wall in the N. crassa "slime" RCP-3 S/H mutant was due to a defect in (1-3)-β-D-glucan synthase activity which was exaggerated in the presence of high osmolyte concentrations.

  NCBI PubMed ID: 7550004
  Journal NLM ID: 8112917
  Publisher: SP, Brasil: Associação Brasileira de Divulgação Científica
  Institutions: Departamento de Biologia, Faculdade de Filosofia, Universidade de São Paulo, Brasil
  
   
  
  Neurospora crassa RCP-3 S/H, Neurospora crassa
  CSDB ID 111873 (all data & tools)
• Article ID: 6757
  Mizuno T, Yeohlui P, Kinoshita T, Zhuang C, Ito H, Mayuzumi Y "Studies on the host-mediated antitumor polysaccharides. Part XXVI. Antitumor activity of chemically modified polysaccharides from Niohshimeji, Tricholma giganteum" - Shizuoka Daigaku Nōgakubu kenkyū hōkoku = Bulletin of the Faculty of Agriculture of Shizuoka University [Japanese] 44 (1994) 37-46
  
  Journal NLM ID: 101167071
  Publisher: Iwata-shi: Dō Gakubu
  
   
  
  Tricholoma giganteum
  CSDB ID 111972 (all data & tools)
• Article ID: 6758
  Mizuno T, Kinoshita T, Zhuang C, Itoh H, Ito H, Mayuzumi Y "Studies on the host-mediated antitumor polysaccharides. Part XXIII. Antitumor-active heteroglycans from Niohshimeji mushroom, Tricholoma giganteum" - Bulletin of Shizuoka University of Forest Resources and Environmental Studies 18 (1994) 97-106
  
   
  
  Tricholoma giganteum
  CSDB ID 111976 (all data & tools)
• Article ID: 6762
  Ram AJF, Brekelmans SSC, Oehlen LJWM, Klis FM "Identification of two cell cycle regulated genes affecting the b1,3- glucan content of cell walls of Saccharomyces cerevisiae" - FEBS Letters 358 (1995) 165-170
  

  The Calcofluor white-hypersensitive mutants cwh52 and cwh53 are severely reduced in β-1,3-glucan. CWH52 was equivalent to GAS1. CWH53 represented a new gene, located on the right arm of chromosome XII, and predicted to encode a 215 kDa protein with multiple transmembrane domains. The transcription of CWH53 was cell cycle-dependent and, similar to GAS1/CWH52, increased in late G1, indicating that the formation of β-glucan is cell cycle-regulated. Further, in some mutant alleles of both gas1/cwh52 and cwh53 lethal concentrations of Calcofluor induced growth arrest at a specific phase of the cell cycle.

  NCBI PubMed ID: 7828729
  Journal NLM ID: 0155157
  Publisher: Elsevier
  Institutions: Institute for Molecular Cell Biology, University of Amsterdam, The Netherlands
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 125854 (all data & tools)
• Article ID: 6763
  Kapteyn JC, Dijkgraaf GJP, Montijn RC, Klis FM "Glucosylation of cell wall proteins in regenerating spheroplasts of Candida albicans" - FEMS Microbiology Letters 128 (1995) 271-277
  

  The cell wall of Candida albicans contains mannoproteins that are covalently associated with β-1,6-glucan. When spheroplasts were allowed to regenerate a new cell wall, initially non-glucosylated cell wall proteins accumulated in the medium. While the spheroplasts became osmotically stable, β-1,6-glucosylated proteins could be identified in their cell wall by SDS-extraction or β-1,3-glucanase digestion. At later stages of regeneration, β-1,3-glucosylated proteins were also found. Hence, incorporation of proteins into the cell wall is accompanied by extracellular coupling to β-1,6-/β-1,3-glucan. The SDS-extractable glucosylated proteins probably represent degradation products of wall proteins rather than their precursors. Tunicamycin delayed, but did not prevent the formation of β-1,6-glucosylated proteins, demonstrating that β-1,6-glucan is not attached to N-glycosidic side-chains of wall proteins.

  NCBI PubMed ID: 7781974
  Journal NLM ID: 7705721
  Publisher: Blackwell Publishing
  Institutions: Institute of Molecular Cell Biology, University of Amsterdam, The Netherlands
  
   
  
  Candida albicans
  CSDB ID 126051 (all data & tools)
• Article ID: 6776
  Sone Y, Shibata S, Kishida E, Misaki A "Alteration of b-D-glucan from edible mushroom after injection into mouse peritoneal cavity" - Journal of Nutritional Science and Vitaminology 40 (1994) 335-341
  

  Tritium-labeled antitumor β-D-glucan derivative (T-labeled glucan) was prepared from the branched β-1,3-D-glucan of an edible mushroom, Volvariella volvacea, by its periodate oxidation followed by reduction with NaBT4. Twenty-three hours after T-labeled glucan had been injected into the mouse peritoneal cavity, about 3% of the total radioactivity injected was found in the mouse serum. In spite of the fact that T-labeled glucan had no affinity to the anion-exchange column before injection, about 50% of the labeled β-D-glucan in the serum thus obtained was adsorbed onto the column. The labeled β-D-glucan fraction eluted from the column by salt gradient showed antitumor activity in vivo.

  NCBI PubMed ID: 7844640
  Journal NLM ID: 0402640
  Publisher: University of Tokyo Press
  Institutions: Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University, Japan
  
   
  
  Volvariella volvacea
  CSDB ID 141508 (all data & tools)
• Article ID: 6799
  Matsumoto T, Haraoka M, Kubo S, Takahashi K, Tanaka M, Ogata N, Kumazawa J "β-D-glucan concentrations detected by toxicolor and endospecy testsin the urine of patients with urinary fungal infections" - Urological Research 21 (1993) 117-120
  

  β-D-glucan is an essential component of the cell wall of fungi. We measured its concentration in the urine of patients with funguria using the chromogenic endotoxin assay kits, Toxicolor and Endospecy. These assay systems use the same Limulus coagulation enzymes. Since the Endospecy test detects endotoxin but not factor G, which is activated by β-D-glucan, the β-D-glucan concentration can be calculated by subtracting the Endospecy value from the Toxicolor value. Concentrations of β-D-glucan were found to be significantly higher in urine samples from patients with funguria (> or = 10(3) colony-forming units/ml) than in non-infected samples.

  NCBI PubMed ID: 8503147
  Journal NLM ID: 0364311
  Institutions: Department of Urology, Faculty of Medicine, Kyushu University, Fukuoka, Japan
  
   
  
  Candida, Trichosporon
  CSDB ID 149482 (all data & tools)