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PubMed1992

Neutral glycolipid abnormalities in a t-complex mutant mouse embryo.

The content of neutral glycolipids was studied in normal and twl/twl mutant mouse embryos at embryonic day 11 (E-11). The twl mutation is part of the T/t complex on chromosome 17 and causes embryonic lethality from defects in the developing neural tube. Previous studies suggested that the mutation could involve a defect in ganglioside biosynthesis. Although the total neutral glycolipid content was similar in the normal and mutant whole embryos (approximately 80 nmol glucose/100 mg dry weight), marked differences were detected for the distribution of specific glycolipids. The content of lactosylceramide, globotriaosylceramide, and globotetraosylceramide was significantly higher in the mutant than in the normal embryos, whereas that of glucosylceramide was significantly reduced. The Forssman glycolipid was slightly elevated. The neutral glycolipid composition was similar in embryonic head and body regions of normal embryos, suggesting that the glycolipid abnormalities observed in the mutants are expressed in most embryonic cells and tissues. These and the previously reported ganglioside abnormalities in the twl/twl mutants could result from an inherited defect in glycolipid biosynthesis.

Animals↗
PubMed1987

Toxin A from Clostridium difficile binds to rabbit erythrocyte glycolipids with terminal Gal alpha 1-3Gal beta 1-4GlcNAc sequences.

The binding of Toxin A isolated from Clostridium difficile to rabbit erythrocyte glycolipids has been studied. Total lipid extracts from rabbit erythrocytes were subjected to thin-layer chromatography and toxin-binding glycolipids detected by using 125I-labeled Toxin A in a direct binding overlay technique. Two major and several minor toxin-binding glycolipids were detected in rabbit erythrocytes by this method. The results of structural analyses of the major toxin-binding glycolipids were consistent with a pentasaccharide-ceramide (Gal alpha 1-3Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4Glc-Cer) and a branched decasaccharide-ceramide (Gal alpha 1-3Gal beta 1-4GlcNAc beta 1-3[Gal alpha 1-3Gal beta 1-4GlcNAc beta 1-6]Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4Glc-Cer) previously identified as the two most abundant glycolipids in rabbit erythrocytes. 125I-Toxin A binding to these glycolipids could be inhibited by bovine thyroglobulin, monospecific antiserum to the toxin, or by treatment of the glycolipids with alpha-galactosidase. The absence of toxin interaction with isoglobotriaosylceramide (Gal alpha 1-3Gal beta 1-4Glc-Cer) isolated from canine intestine suggested that the GlcNAc residue present in the terminal Gal alpha 1-3Gal beta 1-4GLcNAc sequence common to all known toxin binding glycoconjugates is required for carbohydrate-specific recognition by Toxin A. These observations are consistent with the proposed carbohydrate binding specificity of Toxin A for the nonreducing terminal sequence, Gal alpha 1-3Gal beta 1-4GlcNAc.

Animals↗
PubMed1985

A Langmuir film balance study of the interactions of ionic and polar solutes with glycolipid monolayers.

Using a Langmuir film balance experiments have been conducted to discover if dissolved salts or carbohydrates interact with glycolipid monolayers. Two types of glycolipid were studied, simple glycosides made by ether linking monosaccharides to fatty alcohols and cerebrosides extracted from natural sources. It was found that salts or carbohydrates in the subphase expanded glycolipid monolayers. That is, a monolayer spread on a solution occupied a greater area at a given pressure than it would have spread on pure water. Of the carbohydrates galactose and glucose, galactose caused a markedly greater expansion of monolayers than glucose. However, the magnitude of the expansions measured for stearyl glucoside, mannoside and galactoside films on solutions of a particular sugar were not significantly different, demonstrating that this phenomenon is independent of the glycolipid sugar residue. As with carbohydrates, salts also have differing effects on glycolipid monolayers. Although the effect an individual ion has on a monolayer cannot be directly measured, comparisons between salts indicate that there is a correlation between the size of an ion and the extent of the monolayer expansion it causes. To explain these observations two different mechanisms are proposed. In the case of salts it is suggested that large ions which have a low charge density disrupt water structure in such a way that monolayers spread on the surface of their solutions are expanded. The ability of carbohydrates to expand monolayers is explained in terms of the carbohydrate replacing water molecules bound to the polar groups of the monolayer and in so doing increasing the effective area of the lipid molecules. It is suggested that the molecular mechanisms involved in the interactions of ions and carbohydrates with glycolipid monolayers may also operate in the interactions of glycolipids and glycoproteins with extracellular agents and surfaces.

Glycolipids↗
PubMed1982

Immunochemical determination of Forssman and blood group A-active glycolipids in human gastric mucosa by inhibition assay of liposome lysis.

A simple liposome immunoassay, liposome immune-lysis inhibition (LILI) assay, is described for quantitative determination of individual glycolipid antigens. Liposomes containing fluorogenic marker, 4-methylumbelliferyl phosphate, were prepared from sphingomyelin, cholesterol, dicetylphosphate and standard glycolipid. Release of trapped markers from these liposomes by antibody and complement (liposome lysis) was inhibited by preincubating the antibody with test glycolipid incorporated into inhibitor liposomes. Based on the competitive inhibition, it was possible to quantitate each glycolipid antigen in less than picomolar amounts. The sensitivity and specificity of the assay were examined with purified glycolipid standards. LILI assay has been applied for the determination of Forssman glycolipid and blood group A-active glycolipid in human gastric mucosa and cancer tissues.

ABO Blood-Group System↗
PubMed1996

Molecular species analysis and quantification of the glycosylphosphatidylinositol intermediate glycolipid C from Trypanosoma brucei.

The precursor of the glycosylphosphatidylinositol membrane anchor of the variant surface glycoprotein of Trypanosoma brucei is known as glycolipid A and it has the structure: EtN-PO4-6Man alpha 1-2Man alpha 1-6Man alpha 1-4GlcN alpha 1-6myo-inositol-PO4-(sn-1,2-dimyristoylglycerol). This precursor exists in equilibrium with its inositol-acylated form known as glycolipid C that contains a fatty acid attached to the inositol ring. In this study, we describe the purification to homogeneity of glycolipid C, its precise quantification and the analysis of the molecular species of glycolipid C by electrospray ionisation mass spectrometry. The results show that glycolipid C is present at 160000 copies per cell, that glycolipid C is acylated on the 2-position of the myo-inositol ring and that glycolipid C is heterogeneous with respect to the acyl chain attached to the inositol ring. The implications of these results with respect to the nature of the trypanosome inositol acyltransferase are discussed.

Acylation↗
PubMed1993

Glycolipids isolated from cultured rat hepatocytes: analysis of their role in insulin signal transduction.

The precise mechanism by which insulin elicits its effects remains to be fully determined. A glycophospholipid, isolated from H35 cells, has been proposed as a possible precursor for an insulin-generated second messenger that mediates the intracellular effects of insulin. This glycolipid contains a hexosamine moiety, inositol, galactose and palmitate. We have isolated a glycolipid from cultured rat hepatocytes that exhibits chromatographic and radiolabelling characteristics similar to this proposed precursor. The glycolipid can be radiolabelled with glucosamine, galactosamine, galactose and palmitate, but not myristate or myoinositol. Incorporation of radiolabel into this glycolipid was insensitive to the presence of either insulin (10(-7) M) or phosphatidylinositol-specific phospholipase C (PI-PLC) in the culture medium. The cultured hepatocytes used exhibited normal insulin responses with respect to glycogen turnover and gene expression. Treatment of partially purified glycolipid with either PI-PLC or nitrous acid did not result in the generation of an aqueous soluble phosphooligosaccharide indicating that the glycolipid was not cleaved by either agent. This is in contrast to the reported cleavage of the glycolipids found in H35 hepatoma and lymphocytes. These results question the role of the putative phosphooligosaccharide mediator in the intracellular transduction system activated by insulin.

Albumins↗
PubMed1999

Immunochemical characterisation of Schistosoma mansoni glycolipid antigens.

The aim of this study was to investigate the occurrence, distribution and immunochemical properties of antibody-defined carbohydrate epitopes in neutral glycolipid fractions of Schistosoma mansoni eggs, cercariae and adults. The amount of extractable, antigenic, neutral glycolipids was lowest in adult worms, increasing consecutively in cercariae and eggs. The immunoreactivity of the glycolipids resided in the carbohydrate moiety in that it was periodate-sensitive. Serological reactivity, and monosaccharide component analysis, anomeric configuration and methylation-linkage analyses indicated that there were two dominant epitopes, which could be partially defined immunologically. The first epitope was detected on egg, cercarial and adult glycolipids. It was strongly recognised by mouse chronic infection sera and rabbit hyperimmune sera raised against specific egg antigens, and was defined by the monoclonal antibody M2D3H (Bickle QD, Andrews BJ. Characterisation of Schistosoma mansoni monoclonal antibodies which block in-vitro killing: failure to demonstrate blockage of immunity in vivo. Parasite Immunol 1988;10:151-168). M2D3H appeared to have the same epitope specificity as monoclonal antibody 128C3/3 (Weiss J, Magnani JL, Strand M. Identification of Schistosoma mansoni glycolipids that share immunogenic carbohydrate epitopes with glycoproteins. J Immunol. 1986;136:4275-82). The internal epitope was defined structurally by the presence of fucose 3-linked to 3,4-disubstituted N-acetylglucosamine, which was itself partially substituted by a second fucose residue, to yield the determinant -4[Fucalpha1,2Fucalpha3]GlcNAcbeta1-. The second epitope was defined by the anti-LewisX monoclonal antibody 4D1 and was found primarily on cercarial glycolipids. It was chemically characterised as the LewisX epitope of Galbeta1,4[Fucalpha1,3]GlcNAcbeta1- in a terminal position. The removal of fucose greatly diminished the binding of the anti-LewisX and M2D3H monoclonal antibodies, as well as the polyclonal chronic infection sera, to glycolipids of all three life-cycle stages and thus revealed the epitopic importance of fucose.

Animals↗
PubMed1997

Distribution of surface-exposed antigenic glycolipids in recent clinical isolates of Mycobacterium tuberculosis.

The distribution of surface-exposed antigenic glycolipids in seven recent clinical isolates of Mycobacterium tuberculosis was established. Thin-layer and liquid chromatographies revealed a uniformity in the glycolipid pattern. Chemical analysis of the individual glycolipids of a selected strain enabled the identification of glycolipids of serological interest in all the other clinical isolates. Phenolic glycolipid-Tb1 (PGL-Tb1) was lacking in all strains, but appreciable amounts of a partially deglycosylated version (PGL-Tb1D) were present in the seven isolates. Diacyltrehaloses (DATs) were detected in all strains, showing themselves to be major glycolipids. Lipooligosaccharides (LOS-II) were present in the seven strains studied though only in trace amounts. These results shed new light on the open debate on the distribution of these interesting glycolipids in typical clinical isolates of M. tuberculosis. In the search for a serological test for tuberculosis, and in accordance with our observations, we believe that PGL-Tb1 and LOS-II should not be the target molecules for serology and that it is worthwhile to continue investigating the value of DATs as antigens. We also believe that it would be of interest to undertake research to assess the usefulness of PGL-Tb1D as an antigen.

Antigens, Bacterial↗
PubMed2005

Mapping fucosylated epitopes on glycoproteins and glycolipids of Schistosoma mansoni cercariae, adult worms and eggs.

The developmental expression of the antigenic fucosylated glycan motifs Fucalpha1-3GalNAcbeta1-4GlcNAc (F-LDN), Fucalpha1-3GalNAcbeta1-4(Fucalpha1-3)GlcNAc (F-LDN-F), GalNAcbeta1-4(Fucalpha1-3)GlcNAc (LDN-F), Galbeta1-4(Fucalpha1-3)GlcNAc (Lewis X), and GalNAcbeta1-4(Fucalpha1-2Fucalpha1-3)GlcNAc (LDN-DF) in Schistosoma mansoni cercariae, adult worms and eggs, was surveyed using previously defined anti-carbohydrate monoclonal antibodies (mAbs). Lewis X was found both on glycolipids and glycoproteins, yet with completely different expression patterns during the life-cycle: on glycolipids, Lewis X was mainly found in the cercarial stage, while protein-conjugated Lewis X was mainly present in the egg stage. Also protein-conjugated LDN-F and LDN-DF were most highly expressed in the egg-stage. On glycolipids LDN-DF was found in all three examined stages, whereas LDN-F containing glycolipids were restricted to adult worms and eggs. The motifs F-LDN and F-LDN-F were found both on glycoproteins and glycolipids of the cercarial and egg stage, while in the adult stage, they appeared to occur predominantly on glycolipids. Immunofluorescence assays (IFA) showed that these F-LDN and F-LDN-F containing glycolipids were localized in a yet undefined duct or excretory system of adult worms. Murine infection serum showed major reactivity with this adult worm duct-system, which could be fully inhibited by pre-incubation with keyhole limpet haemocyanin (KLH). Clearly, the use of defined mAbs provides a quick and convenient way to map expression profiles of carbohydrate epitopes.

Amino Acid Motifs↗
PubMed2004

Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy.

Glycolipid transfer protein (GLTP) is a soluble 24 kDa protein that selectively accelerates the intermembrane transfer of glycolipids in vitro. Little is known about the GLTP structure and dynamics. Here, we report the cloning of human GLTP and characterize the environment of the three tryptophans (Trps) of the protein using fluorescence spectroscopy. Excitation at 295 nm yielded an emission maximum (lambda(max)) near 347 nm, indicating a relatively polar average environment for emitting Trps. Quenching with acrylamide at physiological ionic strength or with potassium iodide resulted in linear Stern-Volmer plots, suggesting accessibility of emitting Trps to soluble quenchers. Insights into reversible conformational changes accompanying changes in GLTP activity were provided by addition and rapid dilution of urea while monitoring changes in Trp or 1-anilinonaphthalene-8-sulfonic acid fluorescence. Incubation of GLTP with glycolipid liposomes caused a blue shift in the Trp emission maximum but diminished the fluorescence intensity. The blue-shifted emission maximum, centered near 335 nm, persisted after separation of glycolipid liposomes from GLTP, consistent with formation of a GLTP-glycolipid complex at a glycolipid-liganding site containing Trp. The results provide the first insights into human GLTP structural dynamics by fluorescence spectroscopy, including global conformational changes that accompany GLTP folding into an active conformational state as well as more subtle conformational changes that play a role in GLTP-mediated transfer of glycolipids between membranes, and establish a foundation for future studies of membrane rafts using GLTP.

Amino Acid Sequence↗
PubMed1979

Glycolipids and fatty acids of two dog kidney cell lines.

Glycolipid and fatty acid compositions were studied in whole cells and plasma membranes from two dog kidney cell lines (Madin-Darby and SV40-transformed cells) grown in monolayer and suspension cultures. Glycolipids, which account for 5% or less of the total lipids in dog kidney cells, were substantially increased in plasma membranes relative to whole cells. Sialoglycolipids more complex than a Tay-Sachs-like ganglioside were not found in any whole-cell or plasma-membrane preparation of this study. Dog kidney cells transformed by SV40 virus contained primarily a less complex sialoglycolipid, haematoside. Neutral glycolipids comprised 26-43% of the total glycolipid content in Madin-Darby preparations, whereas in transformed cells and membranes neutral glycolipids constituted only 1-22% of the total glycolipid content. Ceramide trihexoside was found in Madin-Darby cultures, but not in transformed cultures. The values for short-chain fatty acids from neutral glycolipids and for saturated fatty acids were generally higher than the values for these fatty acids in calf serum.

Animals↗
PubMed2004

Tissue-specific loss of fucosylated glycolipids in mice with targeted deletion of alpha(1,2)fucosyltransferase genes.

Glycolipids in epithelial tissues of the gastrointestinal tract act as receptors for enteric bacteria and are implicated in the activation of the intestinal immune system. To clarify the genes involved in the fucosylation of the major glycolipids, substrate glycolipids and fucosylated products were measured in tissues of wild-type and mutant mice lacking alpha(1,2)fucosyltransferase genes FUT1 or FUT2. Quantitative determination was performed by TLC-immunostaining for GA1 (Gg4Cer), FGA1 (fucosyl GA1), GM1 (II3NeuAc-Gg4Cer), FGM1 (fucosyl GM1), and Forssman glycolipids. Both FGM1 and FGA1 completely disappeared from the antrum, cecum, and colon of FUT2-null mice, but not those of FUT1-null and wild-type mice. Precursor glycolipids, GM1 and GA1, accumulated in tissues of FUT2-null mice, indicating that the FUT2-encoded enzyme preferentially participates in the fucosylation of GA1 and GM1 in these tissues. Female reproductive organs were similarly found to utilize FUT2 for the fucosylation of glycolipids FGA1 (uterus and cervix), and FGM1 (ovary), due to their absence in FUT2-null mice. In FUT1-null mice FGA1 was lost from the pancreas, but was present in wild-type and FUT2-null mice, indicating that FUT1 is essential for fucosylation of GA1 in the pancreas. Ulex europaeus agglutinin-I lectin histochemistry for alpha(1,2)fucose residues confirmed the absence of alpha(1,2)fucose residues from the apical surface of pancreatic acinar glands of FUT1-null mice. Ileum, epididymis, and testis retained specific fucosylated glycolipids, irrespective of targeted deletion of either gene, indicating either compensation for or redundancy of the alpha(1,2)fucosyltransferase genes in these tissues.

Animals↗
PubMed1996

Characterization of the glycolipid associated with Alzheimer paired helical filaments.

In the present study, analytical techniques including gas chromatography/mass spectrometry (GC/MS)-assisted carbohydrate linkage-analysis, one- and two-dimensional NMR, and matrix-assisted laser desorption/ionization time of flight mass spectroscopy (MALDI-MS) have been used to characterize the structure of the glycolipid associated with the paired helical filaments (PHF) isolated from the neurofibrillary tangles of Alzheimer's diseased brain. The 1H NMR spectrum of acid-hydrolyzed protein-resistant core PHF (prcPHF) displays resonances that can be assigned to fatty acid and glucose. There are no resonances present that would indicate the presence of protein, amino acids, or a sphingosine base. Using two-dimensional homonuclear correlated spectroscopy, homonuclear Hartmann-Hahn, and heteronuclear multiple quantum coherence experiments, resonances in the 1H and 13C NMR spectrum of native PHF were assigned to a nonreducing terminal alpha-1,6-glycosidically linked glucose, an internal alpha-1,6-linked glucose, and an alpha-1,2,6-linked glucose. The narrow line-widths observed for these residues suggest that they arise from glucose residues undergoing rapid segmental motion. The carbohydrate portion of the PHF-associated glycolipid was analyzed using GC/MS linkage analysis and confirmed the presence of terminal and internal alpha-1,6-linked glucose and alpha-1,2,6-linked glucose in a molar ratio of 2:1:1. Three components of the PHF-associated glycolipid fraction having masses 2,416, 2,325, and 2,237 Da were observed using MALDI-MS. The least abundant, heavier mass component (2,416 Da) was best fit to a structure with a tridecamer of glucose having a single esterified C20 fatty acid (Glc13 + C20 or Glc13 + C20:1), whereas the more abundant, lower mass components were best fit to noncovalently associated glycolipid dimers, each with a glucose pentamer or hexamer having two C14, C16, or C18 esterified fatty acids {D[(Glc5 + C18) + (Glc6 + C16)] or D[(Glc5 + C14) + (Glc6 + C14)]}. The ratio of glucose to fatty acid calculated from these best-fit structures of the more abundant mass components (5.5 +/- 1.1:1.0) is in reasonable agreement with the same ratio calculated from peak integrations in the NMR spectra of acid-hydrolyzed prcPHF (6.2 +/- 1.6). Structural similarities between PHF-associated glycolipid and other glycolipid amphiphiles known to form PHF-like filaments indirectly suggest that this unique glycolipid may be an integral component of the PHF suprastructure.

Alzheimer Disease↗
PubMed1972

Glycolipid synthesis in normal and virus-transformed hamster cell lines.

Studies have been continued on the synthesis of glycolipids by the NIL 2 line of hamster cells. Several clones were isolated from this line. These clones vary in morphology, saturation density, and glycolipid composition. Contrary to expectation there was no correlation between saturation density and complexity of the glycolipid pattern. In fact, the clone with the highest saturation density was the only one to show the complete set of glycolipids found previously in NIL 2 cells. All untransformed NIL clones show an increase in the level of "higher" (more than two saccharides/ceramide) glycolipids as the cells approach confluence. In the line containing all three "higher" neutral glycolipids, all three increased as cells approached saturation density. In the line containing only hematoside, this compound increased at confluence. Cells transformed by hamster sarcoma virus or polyoma virus showed no density-dependent glycolipid synthesis.

Animals↗
PubMed1983

Sequential change of carbohydrate antigen associated with differentiation of murine leukemia cells: i-I antigenic conversion and shifting of glycolipid synthesis.

Cell surface carbohydrate antigens and their metabolism were investigated during the course of differentiation of murine cultured leukemia cells (M1) into macrophage-like cells. The major glycolipids in undifferentiated M1 cells were of the ganglio series, with a small amount of lacto-series glycolipids. A novel branched structure was found as a tetraosylceramide of M1- cells. Upon differentiation, synthesis of lacto-series glycolipids was significantly enhanced and synthesis of globo-series glycolipids was newly induced but the ganglio-series synthesis was much reduced. Undifferentiated cells expressed only i antigen (i+I-Pk-); differentiated macrophage-like cells became I-antigen dominant and Pk-antigen positive (i+/-I+Pk+). The changes proceeded in two sequential steps: (i) an enhancement of lacto-series glycolipid synthesis associated with the conversion of i antigen to I antigen, and (ii) subsequent induction of globo-series glycolipid synthesis accompanied by the appearance of Pk antigen. The experimental system offers a clue for studies on the process of branching (i-to-I conversion) as well as the biological significance of three major glycolipids (globo-, lacto-, and ganglio-series) as markers of cell differentiation.

Animals↗
PubMed1985

Polyneuropathy with monoclonal gammopathy: glycolipids are frequently antigens for IgM paraproteins.

Immunoglobulins from patients with paraproteinemic polyneuropathy were screened for reactivity with nerve and brain glycolipids by ELISA and/or a thin-layer-chromatogram-overlay technique. The myelin-associated glycoprotein (MAG) has been shown to be an antigen in many neuropathy patients with IgM gammopathy, but this study focused on seven neuropathy patients in which the IgM paraproteins had been shown not to react with this glycoprotein. Five of these seven had IgM that reacted with components in the acidic glycolipid fraction of human sciatic nerve, and three of these IgMs also reacted with components in the acidic glycolipid fraction of human brain. Little or no reactivity with glycolipids was detected for two patients with neuropathy and IgG gammopathy or for two with neuropathy and IgA gammopathy. The results suggest that neuropathy-patient IgM paraproteins not reactive with MAG often react with acidic glycolipids and thus define a subset of paraproteinemic neuropathies. Since the IgM paraproteins that react with MAG also react with acidic glycolipids of nerve, glycolipid antigens appear to be quite common among the IgM paraproteinemic neuropathies.

Autoantibodies↗
PubMed1983

Interaction of concanavalin A with spin-labeled glycolipid incorporated into liposomes.

Using a synthetic glycolipid derived from maltotetraose and a spin-labeled fatty acid, the lateral distribution and molecular motion of the spin-labeled glycolipid on phosphatidylcholine liposomes in the presence and absence of concanavalin A were examined. When the spin-labeled glycolipid was added to preformed egg yolk phosphatidylcholine-dicetyl phosphate (molar ratio, 10 : 1) liposomes, most of the spin-labeled glycolipid molecules could be incorporated into liposomes as shown by their concanavalin A-induced agglutination. Concanavalin A also caused a change in line width of the ESR signal of liposome-bound spin-labeled glycolipid, whereas the overall splitting value 2A parallel did not change significantly. It is suggested that the binding of glycolipid molecules to concanavalin A increased the interactions among the radicals of the probe but that the mobility of the acyl chain off glycolipids was not affected. These signal changes were also observed with succinyl-concanavalin A. However, in contrast to concanavalin A, no appreciable agglutination of liposomes could be induced by the latter concanavalin A derivative. Both the agglutination of liposomes and the change in line width of the ESR signal were completely inhibited by alpha-methyl-D-mannoside.

Agglutination Tests↗
PubMed1989

Glycolipids of recent clinical isolates of Mycobacterium tuberculosis: chemical characterization and immunoreactivity.

Five distinct glycolipids were readily detected in isolates of Mycobacterium tuberculosis. Spectroscopic methods and chemical degradation techniques allowed the structural identification of four of these glycolipids. The specific phenolic glycolipid antigen previously characterized from the Canetti strain was found in all the strains examined, with identical structural features (triglycosyl phenol phthiocerol dimycocerosate). The other three glycolipids identified were acylated trehaloses: penta-acyl trehalose (containing phthienoyl substituents), tetra-acyl trehalose 2'-sulphate (with C40-C50 hydroxyphthioceranoyl substituents) and diacyl trehalose 2'-sulphate (with C16 and C18 substituents). The two latter glycolipids as well as the phenolic glycolipid immunoreacted with whole-cell antiserum, indicating their surface location. The occurrence of these glycolipid antigens in recent clinical isolates suggests their possible utilization in the serodiagnosis of tuberculosis and the rapid identification of M. tuberculosis with specific antisera.

Chromatography, Thin Layer↗