Restricted access of proteins to mannan polysaccharides in intact plant cell walls

Marcus, Susan E.; Blake, Anthony W.; Benians, Thomas A.S.; Lee, Kieran J.D.; Poyser, Callum; Donaldson, Lloyd; Leroux, Olivier; Rogowski, Artur; Petersen, Henriette L.; Boraston, A.B.; Gilbert, Harry J.; Willats, William G.T.; Knox, John

doi:10.1111/j.1365-313x.2010.04319.x

Cited by 234 publications

(185 citation statements)

References 54 publications

(159 reference statements)

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“…As shown in Supplemental Figure S4, antibodies directed to the RG-I backbone, extensin, xylan, arabinan, and HG showed relatively strong binding to mucilage extracts, indicating the presence of these polymers in the mucilage. Other antibodies, including LM21 and CCRC-M170 directed to heteromannan (Marcus et al, 2010) and acetylated mannan (Zhang et al, 2014), respectively, showed very low binding to mucilage, confirming the low contents of these epitopes in mucilage. JIM5 and JIM7 can detect low methylesterified HG and high methylesterified HG (Clausen et al, 2003), respectively.…”

Section: The Biochemical Properties Of Nonmannan Polysaccharides Arementioning

confidence: 90%

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CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed

Shi

et al. 2014

Plant Physiol.

135

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Mannans are hemicellulosic polysaccharides that are considered to have both structural and storage functions in the plant cell wall. However, it is not yet known how mannans function in Arabidopsis (Arabidopsis thaliana) seed mucilage. In this study, CELLULOSE SYNTHASE-LIKE A2 (CSLA2; At5g22740) expression was observed in several seed tissues, including the epidermal cells of developing seed coats. Disruption of CSLA2 resulted in thinner adherent mucilage halos, although the total amount of the adherent mucilage did not change compared with the wild type. This suggested that the adherent mucilage in the mutant was more compact compared with that of the wild type. In accordance with the role of CSLA2 in glucomannan synthesis, csla2-1 mucilage contained 30% less mannosyl and glucosyl content than did the wild type. No appreciable changes in the composition, structure, or macromolecular properties were observed for nonmannan polysaccharides in mutant mucilage. Biochemical analysis revealed that cellulose crystallinity was substantially reduced in csla2-1 mucilage; this was supported by the removal of most mucilage cellulose through treatment of csla2-1 seeds with endo-b-glucanase. Mutation in CSLA2 also resulted in altered spatial distribution of cellulose and an absence of birefringent cellulose microfibrils within the adherent mucilage. As with the observed changes in crystalline cellulose, the spatial distribution of pectin was also modified in csla2-1 mucilage. Taken together, our results demonstrate that glucomannans synthesized by CSLA2 are involved in modulating the structure of adherent mucilage, potentially through altering cellulose organization and crystallization.Mannan polysaccharides are a complex set of hemicellulosic cell wall polymers that are considered to have both structural and storage functions. Based on the particular chemical composition of the backbone and the side chains, mannan polysaccharides are classified into four types: pure mannan, glucomannan, galactomannan, and galactoglucomannan (Moreira and Filho, 2008;Wang et al., 2012;Pauly et al., 2013). Each of these polysaccharides is composed of a b-1,4-linked backbone containing Man or a combination of Glc and Man residues. In addition, the mannan backbone can be substituted with side chains of a-1,6-linked Gal residues. Mannan polysaccharides have been proposed to cross link with cellulose and other hemicelluloses via hydrogen bonds (Fry, 1986;Iiyama et al., 1994;Obel et al., 2007;Scheller and Ulvskov, 2010). Furthermore, it has been reported that heteromannans with different levels of substitution can interact with cellulose in diverse ways (Whitney et al., 1998). Together, these observations indicate the complexity of mannan polysaccharides in the context of cell wall architecture.CELLULOSE SYNTHASE-LIKE A (CSLA) enzymes have been shown to have mannan synthase activity in vitro. These enzymes polymerize the b-1,4-linked backbone of mannans or glucomannans, depending on the substrates (GDP-Man and/or GDP-Glc) provided (Richmond and Some...

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Section: The Biochemical Properties Of Nonmannan Polysaccharides Arementioning

confidence: 90%

“…6, D and J). The LM21 antibody, which recognizes heteromannan specifically (Marcus et al, 2010), labeled adherent mucilage in a similar manner as Calcofluor White. The LM21 immunolabeling results between wild-type and csla2-1 seeds were similar to the Calcofluor White results (Fig.…”

Section: The Biochemical Properties Of Nonmannan Polysaccharides Arementioning

confidence: 99%

CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed

Shi

et al. 2014

Plant Physiol.

135

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“…In this study, mannan was detected with the LM21 and LM22 monoclonal antibodies, which are known to bind to mannan, glucomannan, legume seed galactomannan, and mannan/glucomannan (Marcus et al, 2010). Both LM21 and LM22 bound in an equivalent manner to three samples of galactoglucomannan obtained from pine wood (data not shown).…”

Section: Immunolocalization Of Cell Wall Polysaccharides In Normal Anmentioning

confidence: 99%

“…Polysaccharides were examined by ELISA analysis as described by Marcus et al (2010) to confirm binding of LM21 and LM22 to pine mannan.…”

Section: Determination Of Binding To Pine Galactoglucommananmentioning

confidence: 99%

Localization of Cell Wall Polysaccharides in Normal and Compression Wood of Radiata Pine: Relationships with Lignification and Microfibril Orientation

Donaldson

Knox²

2011

Plant Physiology

123

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The distribution of noncellulosic polysaccharides in cell walls of tracheids and xylem parenchyma cells in normal and compression wood of Pinus radiata, was examined to determine the relationships with lignification and cellulose microfibril orientation. Using fluorescence microscopy combined with immunocytochemistry, monoclonal antibodies were used to detect xyloglucan (LM15), b(1,4)-galactan (LM5), heteroxylan (LM10 and LM11), and galactoglucomannan (LM21 and LM22). Lignin and crystalline cellulose were localized on the same sections used for immunocytochemistry by autofluorescence and polarized light microscopy, respectively. Changes in the distribution of noncellulosic polysaccharides between normal and compression wood were associated with changes in lignin distribution. Increased lignification of compression wood secondary walls was associated with novel deposition of b(1,4)-galactan and with reduced amounts of xylan and mannan in the outer S2 (S2L) region of tracheids. Xylan and mannan were detected in all lignified xylem cell types (tracheids, ray tracheids, and thickwalled ray parenchyma) but were not detected in unlignified cell types (thin-walled ray parenchyma and resin canal parenchyma). Mannan was absent from the highly lignified compound middle lamella, but xylan occurred throughout the cell walls of tracheids. Using colocalization measurements, we confirmed that polysaccharides containing galactose, mannose, and xylose have consistent correlations with lignification. Low or unsubstituted xylans were localized in cell wall layers characterized by transverse cellulose microfibril orientation in both normal and compression wood tracheids. Our results support the theory that the assembly of wood cell walls, including lignification and microfibril orientation, may be mediated by changes in the amount and distribution of noncellulosic polysaccharides.

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“…6B). The PL buffer (pH 10) was included because the high pH has been demonstrated previously to degrade pectin backbones that break down under basic conditions (50). Moreover, arabinan can contain various esters (e.g.…”

Section: Ecp Interaction With Spinach Arabinosyl Residues In Pectin-mentioning

confidence: 99%

Escherichia coli Common Pilus (ECP) Targets Arabinosyl Residues in Plant Cell Walls to Mediate Adhesion to Fresh Produce Plants

Rossez

Holmes

Lodberg-Pedersen

et al. 2014

Journal of Biological Chemistry

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Background: Bacterial fimbriae mediate binding to host tissue through specific interactions. Results: ECP interacts with arabinosyl residues in pectin and other plant cell wall components. Conclusion: ECP-arabinan interactions facilitate binding of E. coli to plant hosts. Significance: The prevalence of arabinan targets in produce plants together with ECP expression may explain the association of pathogenic bacteria in edible plants.

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Restricted access of proteins to mannan polysaccharides in intact plant cell walls

Cited by 234 publications

References 54 publications

CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed

CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed

Localization of Cell Wall Polysaccharides in Normal and Compression Wood of Radiata Pine: Relationships with Lignification and Microfibril Orientation

Escherichia coli Common Pilus (ECP) Targets Arabinosyl Residues in Plant Cell Walls to Mediate Adhesion to Fresh Produce Plants

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