A (1→3,1→4)‐β‐glucan‐specific monoclonal antibody and its use in the quantitation and immunocytochemical location of (1→3,1→4)‐β‐glucans

Meikle, Peter J.; Hoogenraad, Nicholas J.; Bönig, Ingrid; Clarke, Adrienne E.; Stone, Bruce

doi:10.1046/j.1365-313x.1994.5010001.x

Cited by 160 publications

(142 citation statements)

References 20 publications

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“…The principal differences were the enhanced amounts of glucomannans in epidermal cell walls, and an enhancement of the ␤-glucan in the mesophyll cell walls, about 4-fold higher than in epidermal walls (Table II). Meikle et al (1994) demonstrated the specificity of the monoclonal antibody BG1 against cereal mixed-linkage ␤-glucans, and found this epitope to be distributed uniformly across the aleurone walls of wheat (Triticum aestivum) endosperm cells but excluded from the middle lamella. The ␤-glucan is distributed uniformly across the thin walls of the mesophyll cells, whereas it is concentrated primarily on the innermost portion of the outer facing wall of the epidermis (Fig.…”

Section: Mesophyll Walls Have a Different Composition From Epidermal mentioning

confidence: 97%

Cell Wall Architecture of the Elongating Maize Coleoptile

et al. 2001

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The primary walls of grasses are composed of cellulose microfibrils, glucuronoarabinoxylans (GAXs), and mixed-linkage ␤-glucans, together with smaller amounts of xyloglucans, glucomannans, pectins, and a network of polyphenolic substances. Chemical imaging by Fourier transform infrared microspectroscopy revealed large differences in the distributions of many chemical species between different tissues of the maize (Zea mays) coleoptile. This was confirmed by chemical analyses of isolated outer epidermal tissues compared with mesophyll-enriched preparations. Glucomannans and esterified uronic acids were more abundant in the epidermis, whereas ␤-glucans were more abundant in the mesophyll cells. The localization of ␤-glucan was confirmed by immunocytochemistry in the electron microscope and quantitative biochemical assays. We used field emission scanning electron microscopy, infrared microspectroscopy, and biochemical characterization of sequentially extracted polymers to further characterize the cell wall architecture of the epidermis. Oxidation of the phenolic network followed by dilute NaOH extraction widened the pores of the wall substantially and permitted observation by scanning electron microscopy of up to six distinct microfibrillar lamellae. Sequential chemical extraction of specific polysaccharides together with enzymic digestion of ␤-glucans allowed us to distinguish two distinct domains in the grass primary wall. First, a ␤-glucan-enriched domain, coextensive with GAXs of low degrees of arabinosyl substitution and glucomannans, is tightly associated around microfibrils. Second, a GAX that is more highly substituted with arabinosyl residues and additional glucomannan provides an interstitial domain that interconnects the ␤-glucan-coated microfibrils. Implications for current models that attempt to explain the biochemical and biophysical mechanism of wall loosening during cell growth are discussed.Biochemical studies have provided a reasonably complete catalog of the major polysaccharides and phenolic substances that constitute the primary cell walls of angiosperms (McCann and Roberts, 1991;Carpita and Gibeaut, 1993). The walls of grasses and related monocots (commelinoids) have quite different compositions compared with those of all dicots and of the non-commelinoid monocot species (Carpita, 1996). The "type II" cell walls of commelinoid monocots are characterized by cellulose microfibrils cross-linked by glucuronoarabinoxylans (GAXs) and a network of polyphenolic substances (Carpita and Gibeaut, 1993;Carpita, 1996). Maize (Zea mays) and other members of the Poales also contain developmentally regulated polymers, the mixed-linkage (133),(134)-␤-dglucans (hereafter, called ␤-glucans). The ␤-glucans are initially absent from meristematic cells but accumulate up to about 20% dry mass of the cell wall coincident with the most rapid rates of coleoptile elongation (Kim et al., 2000). As the elongation rate slows, the ␤-glucan is hydrolyzed by exo-and endo-␤-d-glucanases located in the wall. Concomitant with th...

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Section: Mesophyll Walls Have a Different Composition From Epidermal mentioning

confidence: 97%

Cell Wall Architecture of the Elongating Maize Coleoptile

et al. 2001

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“…Grain samples from 10 to 28 DAP were prepared for microscopy and changes to the endosperm were monitored by taking transverse sections of the developing grains. The distribution and relative abundance of polysaccharides in the differentiating grain were detected on sections using monoclonal antibodies raised against specific polysaccharide epitopes including (1→3)-b-D-glucan (Meikle et al, 1991), xyloglucan LM15 (Marcus et al, 2008), (1→3,1→4)-b-D-glucan (Meikle et al, 1994), hetero-(1→4)-b-Dmannan (Pettolino et al, 2001), and arabino-(1-4)-b-D-xylan LM11 (McCartney et al, 2005). Sections for light microscopy (1 mm) were either stained in toluidine blue to highlight tissue architecture or processed for immunogold labeling.…”

Section: Immunolabeling For Light and Emmentioning

confidence: 99%

Pattern of Deposition of Cell Wall Polysaccharides and Transcript Abundance of Related Cell Wall Synthesis Genes during Differentiation in Barley Endosperm

Wilson

Burton²,

Collins³

et al. 2012

Plant Physiology

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Immunolabeling, combined with chemical analyses and transcript profiling, have provided a comprehensive temporal and spatial picture of the deposition and modification of cell wall polysaccharides during barley (Hordeum vulgare) grain development, from endosperm cellularization at 3 d after pollination (DAP) through differentiation to the mature grain at 38 DAP. (1→3)-β-d-Glucan appears transiently during cellularization but reappears in patches in the subaleurone cell walls around 20 DAP. (1→3, 1→4)-β-Glucan, the most abundant polysaccharide of the mature barley grain, accumulates throughout development. Arabino-(1-4)-β-d-xylan is deposited significantly earlier than we previously reported. This was attributable to the initial deposition of the polysaccharide in a highly substituted form that was not recognized by antibodies commonly used to detect arabino-(1-4)-β-d-xylans in sections of plant material. The epitopes needed for antibody recognition were exposed by pretreatment of sections with α-l-arabinofuranosidase; this procedure showed that arabino-(1-4)-β-d-xylans were deposited as early as 5 DAP and highlighted their changing structures during endosperm development. By 28 DAP labeling of hetero-(1→4)-β-d-mannan is observed in the walls of the starchy endosperm but not in the aleurone walls. Although absent in mature endosperm cell walls we now show that xyloglucan is present transiently from 3 until about 6 DAP and disappears by 8 DAP. Quantitative reverse transcription-polymerase chain reaction of transcripts for GLUCAN SYNTHASE-LIKE, Cellulose Synthase, and CELLULOSE SYNTHASE-LIKE genes were consistent with the patterns of polysaccharide deposition. Transcript profiling of some members from the Carbohydrate-Active Enzymes database glycosyl transferase families GT61, GT47, and GT43, previously implicated in arabino-(1-4)-β-d-xylan biosynthesis, confirms their presence during grain development.

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“…Thin sections (100 nm) were cut on an ultramicrotome (Leica) and picked up on carbon-coated and plastic-filmed gold grids. The (1/3),(1/4)-b-D-glucan epitopes were detected with the BG1 monoclonal antibody that specifically recognizes this mixed-linkage b-glucan (Meikle et al, 1994; available from Biosupplies Australia), and visualized by a 10-nm colloidal gold-conjugated rabbit anti-mouse secondary antibody (Sigma). The blocking solution was 1% (w/v) acetylated bovine serum albumen (Aurion) in phosphate-buffered saline plus 0.1% (w/v) Tween 20, and incubation solution for washes was 0.1% acetylated bovine serum albumen in phosphate-buffered saline plus 0.01% (w/v) Tween 20.…”

Section: Transmission Electron Microscopy and Immunocytochemistrymentioning

confidence: 99%

“…The BG1 monoclonal antibody recognizes the (1/3),(1/4)-b-D-glucan with high specificity (Meikle et al, 1994). This monoclonal antibody has been used to show dramatic changes in epitope abundance of (1/3),(1/4)-b-D-glucan in the cell walls of developing tissues (Meikle et al, 1994;Trethewey et al, 2005;McCann et al, 2007) and its appearance in the cell walls of Arabidopsis (Arabidopsis thaliana) following heterologous expression of genes thought to encode its synthases Doblin et al, 2009).…”

mentioning

confidence: 99%

“…This monoclonal antibody has been used to show dramatic changes in epitope abundance of (1/3),(1/4)-b-D-glucan in the cell walls of developing tissues (Meikle et al, 1994;Trethewey et al, 2005;McCann et al, 2007) and its appearance in the cell walls of Arabidopsis (Arabidopsis thaliana) following heterologous expression of genes thought to encode its synthases Doblin et al, 2009). The failure to detect (1/3),(1/4)-b-D-glucan in Golgi membranes and only in the cell wall prompted Fincher (2009) to conclude that cellodextrin oligomers of the (1/3),(1/4)-b-D-glucan may be initiated in the Golgi membrane, but the actual polymerization of the polysaccharide occurs at the plasma membrane.…”

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confidence: 99%

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The Maize Mixed-Linkage (1→3),(1→4)-β-d-Glucan Polysaccharide Is Synthesized at the Golgi Membrane

Carpita

McCann

2010

Plant Physiology

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With the exception of cellulose and callose, the cell wall polysaccharides are synthesized in Golgi membranes, packaged into vesicles, and exported to the plasma membrane where they are integrated into the microfibrillar structure. Consistent with this paradigm, several published reports have shown that the maize (Zea mays) mixed-linkage (1→3),(1→4)-β-d-glucan, a polysaccharide that among angiosperms is unique to the grasses and related Poales species, is synthesized in vitro with isolated maize coleoptile Golgi membranes and the nucleotide-sugar substrate, UDP-glucose. However, a recent study reported the inability to detect the β-glucan immunocytochemically at the Golgi, resulting in a hypothesis that the mixed-linkage β-glucan oligomers may be initiated at the Golgi but are polymerized at the plasma membrane surface. Here, we demonstrate that (1→3),(1→4)-β-d-glucans are detected immunocytochemically at the Golgi of the developing maize coleoptiles. Further, when maize seedlings at the third-leaf stage were pulse labeled with [14C]O2 and Golgi membranes were isolated from elongating cells at the base of the developing leaves, (1→3),(1→4)-β-d-glucans of an average molecular mass of 250 kD and higher were detected in isolated Golgi membranes. When the pulse was followed by a chase period, the labeled polysaccharides of the Golgi membrane diminished with subsequent transfer to the cell wall. (1→3),(1→4)-β-d-Glucans of at least 250 kD were isolated from cell walls, but much larger aggregates were also detected, indicating a potential for intermolecular interactions with glucuronoarabinoxylans or intermolecular grafting in muro.

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A (1→3,1→4)‐β‐glucan‐specific monoclonal antibody and its use in the quantitation and immunocytochemical location of (1→3,1→4)‐β‐glucans

Cited by 160 publications

References 20 publications

Cell Wall Architecture of the Elongating Maize Coleoptile

Cell Wall Architecture of the Elongating Maize Coleoptile

Pattern of Deposition of Cell Wall Polysaccharides and Transcript Abundance of Related Cell Wall Synthesis Genes during Differentiation in Barley Endosperm

The Maize Mixed-Linkage (1→3),(1→4)-β-d-Glucan Polysaccharide Is Synthesized at the Golgi Membrane

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