Structure and Substrate Specificity of a Eukaryotic Fucosidase from Fusarium graminearum

Cao, Heidi B.; Walton, Jonathan D.; Brumm, Phillip J.; Phillips, George N.

doi:10.1074/jbc.m114.583286

Cited by 35 publications

(56 citation statements)

References 83 publications

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“…The protein sequence alignment predicted that D206 was the catalytic nucleophile in B. xylophilus ; the prediction was confirmed with structure analysis. The D206 is located at the same position as the catalytic nucleophile aspartate residue found in bacteria and fungus . Among two predicted acid/base residues E55 and E270 from sequence alignment, structurally E270 shares the same position as the catalytic acid/base glutamate residue in F. graminearum , but a hydrogen bond was found between E55 and fucose.…”

Section: Discussionmentioning

confidence: 99%

“…45 -L-fucosidase from the plant pathogenic fungus F. graminearum was found actively hydrolyzing the fucose from xyloglucan. 17 Pinus pinea is rich in -1,3-linked fucose and Lewis A N-glycans with fucose residue, 46 and fucose is also found in the xyloglucans, which is the major hemicellulosic matrix polysaccharides in the cell wall of pine. 47,48 It is likely that the Bxy-FUCA may act as a digestive enzyme in the intestine of B. xylophilus, and defucosylate the side groups and expose the hemicellulose backbone for further digestion.…”

Section: Bxy-fuca Is Mainly Expressed In Bwm and Intestine Throughoutmentioning

confidence: 99%

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Bxy‐fuca encoding α‐L‐fucosidase plays crucial roles in development and reproduction of the pathogenic pinewood nematode, Bursaphelenchus xylophilus

Tang

Zhu

et al. 2019

Pest Management Science

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BACKGROUND The pine wood nematode (PWN) Bursaphelenchus xylophilus is the causal agent of pine wilt disease (PWD). This disease is a serious threat to pine forests globally. The fuca gene encodes α‐L‐fucosidase, which plays crucial roles in numerous biological and pathological processes in bacteria, fungi, plants and animals. To find promising control strategies against PWD, we investigated the expression and functions of Bxy‐fuca in B. xylophilus. RESULTS Bxy‐fuca encoding α‐L‐fucosidase is highly conserved within the deduced functional domains and key residues. It is expressed continuously across all developmental stages of B. xylophilus. mRNA in situ hybridization demonstrated that Bxy‐fuca was mainly localized in the body wall muscles and intestine. RNA interference indicated that the zygotic expression of Bxy‐fuca was indispensable for embryogenesis. The rate of B. xylophilus egg hatch was significantly decreased after Bxy‐fuca was interfered. Postembryonic silence of Bxy‐fuca resulted in a dramatic decrease in the longevity of and the total number of eggs produced by B. xylophilus. In addition, the motility of the nematode was greatly hampered with a significant drop in head thrashing frequency. CONCLUSION Bxy‐fuca plays crucial roles in development, lifespan and reproduction of B. xylophilus. Our results provide promising hints for control of PWD by blocking embryogenesis and ontogenesis, decreasing nematode fecundity, and disrupting the connection between B. xylophilus and its vector beetle by preventing nematode movement into the tracheal system. © 2019 Society of Chemical Industry

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Section: Discussionmentioning

confidence: 99%

Section: Bxy-fuca Is Mainly Expressed In Bwm and Intestine Throughoutmentioning

confidence: 99%

Bxy‐fuca encoding α‐L‐fucosidase plays crucial roles in development and reproduction of the pathogenic pinewood nematode, Bursaphelenchus xylophilus

Tang

Zhu

et al. 2019

Pest Management Science

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“…S11), which is surprising since these highly sulfated polymers are found mostly in the cell wall matrix of brown algae (10). The putative fucoidanases in these genotypes have sequence similarities of 30-40% to the enzyme from Fusarium graminearum (AFR68935), which has been suggested to play a role in plant pathogenesis (45). This enzyme shows preference toward α-1,2-linked fucosyl substrates rather than fucan containing α-1,3 (4) linkages as reported for other GH29 fucosidases.…”

Section: Resultsmentioning

confidence: 53%

Genomic diversification of giant enteric symbionts reflects host dietary lifestyles

Ngugi

Miyake

Cahill

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Herbivorous surgeonfishes are an ecologically successful group of reef fish that rely on marine algae as their principal food source. Here, we elucidated the significance of giant enteric symbionts colonizing these fishes regarding their roles in the digestive processes of hosts feeding predominantly on polysiphonous red algae and brown Turbinaria algae, which contain different polysaccharide constituents. Using metagenomics, single-cell genomics, and metatranscriptomic analyses, we provide evidence of metabolic diversification of enteric microbiota involved in the degradation of algal biomass in these fishes. The enteric microbiota is also phylogenetically and functionally simple relative to the complex lignocellulose-degrading microbiota of terrestrial herbivores. Over 90% of the enzymes for deconstructing algal polysaccharides emanate from members of a single bacterial lineage, "Candidatus Epulopiscium" and related giant bacteria. These symbionts lack cellulases but encode a distinctive and lineage-specific array of mostly intracellular carbohydrases concurrent with the unique and tractable dietary resources of their hosts. Importantly, enzymes initiating the breakdown of the abundant and complex algal polysaccharides also originate from these symbionts. These are also highly transcribed and peak according to the diel lifestyle of their host, further supporting their importance and host-symbiont cospeciation. Because of their distinctive genomic blueprint, we propose the classification of these giant bacteria into three candidate genera. Collectively, our findings show that the acquisition of metabolically distinct "Epulopiscium" symbionts in hosts feeding on compositionally varied algal diets is a key niche-partitioning driver in the nutritional ecology of herbivorous surgeonfishes.piscine herbivores | marine algae | carbohydrases | giant enteric symbionts | Epulopiscium M arine herbivorous fishes are an ecologically dominant force, structuring tropical reef ecosystem functions and relationships through their grazing activities (1-3). However, they are one of the least understood guilds of herbivores regarding the mechanisms by which they digest and assimilate algal biomass, especially in contrast to plant material assimilation by terrestrial vertebrate herbivores and insects (1, 4). In terrestrial herbivores, the community of microbes inhabiting an organism's gut-the gut microbiota-is considered to play a significant role in the organism's ability to digest plant matter. It is thought to be a major factor leading to the evolution of vertebrate and insect-based herbivory (1-3, 5) and constitutes a potentially critical component of diet-driven speciation in mammals (1,4,6). Contrary to the immense literature on the nutritional ecology and plant biomass assimilation by mammals, ruminants, and arthropods (4,7,8), mechanistic insights into the digestive physiology of marine herbivores, especially the roles of gastrointestinal microbes of piscine herbivores in gut digestive processes, remain largely uncharacteriz...

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“…The kinetic data suggested that the active site of fucosidases might have some differences. However, the only available structures of α‐ l ‐fucosidase are from bacteria (Shaikh, Lammerts van Bueren, Davies, & Withers, ) and F. graminearum (Cao, Walton, Brumm, & Phillips, ). Although results obtained by molecular homology modeling are limited and they result in a less confident prediction, the comparison of α‐ l ‐fucosidase models from different animal species seems a faster route to identify the active site for this enzyme, which may be informative (Dolan, Noah, & Hurt, ; Nayeem, Sitkoff, & Krystek, ).…”

Section: Discussionmentioning

confidence: 99%

First characterization of fucosidases in spiders

Perrella

Fuzita

Moreti

et al. 2018

Arch Insect Biochem Physiol

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l-fucose is a constituent of glycoconjugates in different organisms. Fucosidases catalyze the removal of fucose residues, and have been correlated to different physiological and pathological processes, such as fertilization, cancer, fucosidosis, and digestion in molluscs and ticks. An α-l-fucosidase sequence was identified from the transcriptome and proteome from the midgut diverticula of the synanthropic spider Nephilingis cruentata. In this article, we describe the isolation of this α-l-fucosidase and the characterization of its activity using substrates and inhibitors demonstrating different specificities among fucosidases. The enzyme had a K of 32 and 400 μM for 4-methylumbelliferyl α-l-fucopyranoside and 4-nitrophenyl α-l-fucopyranoside, respectively; and was unable to hydrolyze fucoidan. Nephilingis cruentata α-l-fucosidase was inhibited competitively by fucose and fuconojyrimycin. The fucosidase had two distinct pH optima even in the isolated form, due to oligomerization dependent on pH, as previously described to other fucosidases. Alignment and molecular homology modeling of the protein sequence with other fucosidases indicated that the active sites and catalytic residues were different, including residues involved in acid/base catalysis. Phylogenetic analysis showed, for the first time, gene-duplication events for fucosidases in Arachnida species. All these data reveal that studies on fucosidases in organisms distinct from bacteria, fungi, and humans are important.

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Structure and Substrate Specificity of a Eukaryotic Fucosidase from Fusarium graminearum

Cited by 35 publications

References 83 publications

Bxy‐fuca encoding α‐L‐fucosidase plays crucial roles in development and reproduction of the pathogenic pinewood nematode, Bursaphelenchus xylophilus

Bxy‐fuca encoding α‐L‐fucosidase plays crucial roles in development and reproduction of the pathogenic pinewood nematode, Bursaphelenchus xylophilus

Genomic diversification of giant enteric symbionts reflects host dietary lifestyles

First characterization of fucosidases in spiders

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