Digestive enzymes of two brachyuran and two anomuran land crabs from Christmas Island, Indian Ocean

Linton, Stuart M.; Saborowski, Reinhard; Shirley, Alicia J.; Penny, Jake A.

doi:10.1007/s00360-014-0815-2

Cited by 17 publications

(10 citation statements)

References 70 publications

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“…Hemicellulases have been previously characterized in several crustaceans [ 96 – 98 ], but not yet in terrestrial isopods. The main chain of hemicellulose is composed of xylose, glucose, and mannose, which is often branched with arabinose, galactose, and other acidic sugars.…”

Section: Discussionmentioning

confidence: 99%

Lignocellulose degradation at the holobiont level: teamwork in a keystone soil invertebrate

et al. 2018

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BackgroundWoodlice are recognized as keystone species in terrestrial ecosystems due to their role in the decomposition of organic matter. Thus, they contribute to lignocellulose degradation and nutrient cycling in the environment together with other macroarthropods. Lignocellulose is the main component of plants and is composed of cellulose, lignin and hemicellulose. Its digestion requires the action of multiple Carbohydrate-Active enZymes (called CAZymes), typically acting together as a cocktail with complementary, synergistic activities and modes of action. Some invertebrates express a few endogenous lignocellulose-degrading enzymes but in most species, an efficient degradation and digestion of lignocellulose can only be achieved through mutualistic associations with endosymbionts. Similar to termites, it has been suspected that several bacterial symbionts may be involved in lignocellulose degradation in terrestrial isopods, by completing the CAZyme repertoire of their hosts.ResultsTo test this hypothesis, host transcriptomic and microbiome shotgun metagenomic datasets were obtained and investigated from the pill bug Armadillidium vulgare. Many genes of bacterial and archaeal origin coding for CAZymes were identified in the metagenomes of several host tissues and the gut content of specimens from both laboratory lineages and a natural population of A. vulgare. Some of them may be involved in the degradation of cellulose, hemicellulose, and lignin. Reconstructing a lignocellulose-degrading microbial community based on the prokaryotic taxa contributing relevant CAZymes revealed two taxonomically distinct but functionally redundant microbial communities depending on host origin. In parallel, endogenous CAZymes were identified from the transcriptome of the host and their expression in digestive tissues was demonstrated by RT-qPCR, demonstrating a complementary enzyme repertoire for lignocellulose degradation from both the host and the microbiome in A. vulgare.ConclusionsOur results provide new insights into the role of the microbiome in the evolution of terrestrial isopods and their adaptive radiation in terrestrial habitats.Electronic supplementary materialThe online version of this article (10.1186/s40168-018-0536-y) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Lignocellulose degradation at the holobiont level: teamwork in a keystone soil invertebrate

et al. 2018

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“…This species consumes seeds and fleshy fibrous fruits that are high in either protein, carbohydrate or lipid (Wilde et al, 2004). It also possesses both β-1,3-glucanase and endo-β-1,4-glucanase activities, but would derive little energy from the digestion of cellulose and hemicellulose, compared to the other nutrients (Wilde et al, 2004;Linton et al, 2014). B. latro also lacks a β-1,4-glucosidase and thus the ability to hydrolyse cellulose to glucose (Linton et al, 2014).…”

Section: Physical Disruption Of Fungal and Plant Cell Wallsmentioning

confidence: 99%

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Linton

Cameron

Gray

et al. 2015

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To identify the gene responsible for the production of a β-1,3-glucanase (laminarinase) within crustacea, a glycosyl hydrolase family 16 (GHF16) gene was sequenced from the midgut glands of the gecarcinid land crab, Gecarcoidea natalis and the freshwater crayfish, Cherax destructor. An open reading frame of 1098 bp for G. natalis and 1095 bp for C. destructor was sequenced from cDNA. For G. natalis and C. destructor respectively, this encoded putative proteins of 365 and 364 amino acids with molecular masses of 41.4 and 41.5 kDa. mRNA for an identical GHF16 protein was also expressed in the haemolymph of C. destructor. These putative proteins contained binding and catalytic domains that are characteristic of a β-1,3-glucanase from glycosyl hydrolase family 16. The amino acid sequences of two short 8-9 amino acid residue peptides from a previously purified β-1,3-glucanase from G. natalis matched exactly that of the putative protein sequence. This plus the molecular masses of the putative proteins matching that of the purified proteins strongly suggests that the sequences obtained encode for a catalytically active β-1,3-glucanase. A glycosyl hydrolase family 16 cDNA was also partially sequenced from the midgut glands of other amphibious (Mictyris platycheles and Paragrapsus laevis) and terrestrial decapod species (Coenobita rugosus, Coenobita perlatus, Coenobita brevimanus and Birgus latro) to confirm that the gene is widely expressed within this group. There are three possible hypothesised functions and thus evolutionary routes for the β-1,3-glucanase: 1) a digestive enzyme which hydrolyses β-1,3-glucans, 2) an enzyme which cleaves β-1,3-glycosidic bonds within cell walls to release cell contents or 3) an immune protein which can hydrolyse the cell walls of potentially pathogenic micro-organisms.

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“…The lineage-specific expansions were partly driven by directional selection, and gains and losses of genes were lineage dependent (Da Lage et al 2013 ). In realty, the intestine environment also plays a role in positive selections of fungal α-amylase in ants (Bacci et al 2013 ) as witnessed in local diet (Linton et al 2014 ), and gene encoding amylases in marine yeasts versus terrestrial yeasts (Chi et al 2009 ).…”

Section: Discussionmentioning

confidence: 99%

Analysis on evolutionary relationship of amylases from archaea, bacteria and eukaryota

Yan

2016

World J Microbiol Biotechnol

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Amylase is one of the earliest characterized enzymes and has many applications in clinical and industrial settings. In biotechnological industries, the amylase activity is enhanced through modifying amylase structure and through cloning and expressing targeted amylases in different species. It is important to understand how engineered amylases can survive from generation to generation. This study used phylogenetic and statistical approaches to explore general patterns of amylases evolution, including 3118 α-amylases and 280 β-amylases from archaea, eukaryota and bacteria with fully documented taxonomic lineage. First, the phylogenetic tree was created to analyze the evolution of amylases with focus on individual amylases used in biofuel industry. Second, the average pairwise p-distance was computed for each kingdom, phylum, class, order, family and genus, and its diversity implies multi-time and multi-clan evolution. Finally, the variance was further partitioned into inter-clan variance and intra-clan variance for each taxonomic group, and they represent horizontal and vertical gene transfer. Theoretically, the results show a full picture on the evolution of amylases in manners of vertical and horizontal gene transfer, and multi-time and multi-clan evolution as well. Practically, this study provides the information on the surviving chance of desired amylase in a given taxonomic group, which may potentially enhance the successful rate of cloning and expression of amylase gene in different species.Electronic supplementary materialThe online version of this article (doi:10.1007/s11274-015-1979-y) contains supplementary material, which is available to authorized users.

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Digestive enzymes of two brachyuran and two anomuran land crabs from Christmas Island, Indian Ocean

Cited by 17 publications

References 70 publications

Lignocellulose degradation at the holobiont level: teamwork in a keystone soil invertebrate

Lignocellulose degradation at the holobiont level: teamwork in a keystone soil invertebrate

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Analysis on evolutionary relationship of amylases from archaea, bacteria and eukaryota

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