scholarly journals Midgut transcriptome assessment of the cockroach-hunting wasp Ampulex compressa (Apoidea: Ampulicidae)

PLoS ONE ◽  
2021 ◽  
Vol 16 (6) ◽  
pp. e0252221
Author(s):  
Jovana M. Jasso-Martínez ◽  
Alexander Donath ◽  
Dieter Schulten ◽  
Alejandro Zaldívar-Riverón ◽  
Manuela Sann
Keyword(s):  
Stress Response ◽  
Candidate Genes ◽  
Glycosyl Hydrolase ◽  
Cytochrome P450s ◽  
Life Stages ◽  
Glycosyl Hydrolase Family ◽  
Ampulex Compressa ◽  
Hymenopteran Species ◽  
Alpha Glucosidase ◽  
Hydrolase Family

The emerald jewel wasp Ampulex compressa (Hymenoptera: Ampulicidae) is a solitary wasp that is widely known for its specialized hunting of cockroaches as larvae provision. Adult wasps mainly feed on pollen and nectar, while their larvae feed on the cockroachs’ body, first as ecto- and later as endoparsitoids. Little is known about the expression of digestive, detoxification and stress-response-related genes in the midgut of A. compressa, or about its transcriptional versatility between life stages. To identify gut-biased genes related to digestion, detoxification, and stress response, we explored the midgut transcriptome of lab-reared A. compressa, for both adults and larvae, by focusing on the top 100 significantly up- and down-regulated genes. From the top 100 significantly differentially expressed genes (DEGs), we identified 39 and 36 DEGs putatively related to digestion and detoxification in the adult wasps and larvae, respectively. The two carbohydrases alpha-glucosidase (containing an alpha-amylase domain) and glycosyl hydrolase family 31, as well as the two proteinases chymotrypsin and trypsin, revealed the highest gene diversity. We identified six significant DEGs related to detoxification, which comprise glutathione S-transferase, cytochrome P450s and UDP-glucuronosyltransferase. The gene expression levels that were significantly expressed in both life stages vary strongly between life stages, as found in genes encoding for chymotrypsin and trypsin or glycosyl hydrolases family 31. The number of genes related to alpha-glucosidase, glycosyl hydrolase family 31, and cytochrome P450s was found to be similar across nine reference hymenopteran species, except for the identified glycosyl hydrolase family 31 gene, which was absent in all reference bee species. Phylogenetic analyses of the latter candidate genes revealed that they cluster together with their homologous genes found in the reference hymenopteran species. These identified candidate genes provide a basis for future comparative genomic and proteomic studies on (ontogenetic) dietary transitions in Hymenoptera.

scholarly journals New Chitosan-Degrading Strains That Produce Chitosanases Similar to ChoA of Mitsuaria chitosanitabida

2005 ◽  
Vol 71 (9) ◽  
pp. 5138-5144 ◽  
Author(s):  
ChoongSoo Yun ◽  
Daiki Amakata ◽  
Yasuhiro Matsuo ◽  
Hideyuki Matsuda ◽  
Makoto Kawamukai
Keyword(s):  
Southern Hybridization ◽  
Glycosyl Hydrolase ◽  
Pcr Amplification ◽  
Rrna Gene ◽  
16S Rrna Gene Sequences ◽  
Glycosyl Hydrolase Family ◽  
Broad Variety ◽  
Hydrolase Family ◽  
The 16S Rrna Gene ◽  
Sequence Similarities

ABSTRACT The betaproteobacterium Mitsuaria chitosanitabida (formerly Matsuebacter chitosanotabidus) 3001 produces a chitosanase (ChoA) that is classified in glycosyl hydrolase family 80. While many chitosanase genes have been isolated from various bacteria to date, they show limited homology to the M. chitosanitabida 3001 chitosanase gene (choA). To investigate the phylogenetic distribution of chitosanases analogous to ChoA in nature, we identified 67 chitosan-degrading strains by screening and investigated their physiological and biological characteristics. We then searched for similarities to ChoA by Western blotting and Southern hybridization and selected 11 strains whose chitosanases showed the most similarity to ChoA. PCR amplification and sequencing of the chitosanase genes from these strains revealed high deduced amino acid sequence similarities to ChoA ranging from 77% to 99%. Analysis of the 16S rRNA gene sequences of the 11 selected strains indicated that they are widely distributed in the β and γ subclasses of Proteobacteria and the Flavobacterium group. These observations suggest that the ChoA-like chitosanases that belong to family 80 occur widely in a broad variety of bacteria.

Variants of glycosyl hydrolase family 2 β-glucuronidases have increased activity on recalcitrant substrates

2021 ◽  
Vol 145 ◽  
pp. 109742
Author(s):  
Caleb R. Schlachter ◽  
Amanda C. McGee ◽  
Pongkwan N. Sitasuwan ◽  
Gary C. Horvath ◽  
Nanda G. Karri ◽  
...  
Keyword(s):  
Glycosyl Hydrolase ◽  
Glycosyl Hydrolase Family ◽  
Increased Activity ◽  
Hydrolase Family

scholarly journals A constitutive expression system for glycosyl hydrolase family 7 cellobiohydrolases in Hypocrea jecorina

2015 ◽  
Vol 8 (1) ◽  
Author(s):  
Jeffrey G Linger ◽  
Larry E Taylor ◽  
John O Baker ◽  
Todd Vander Wall ◽  
Sarah E Hobdey ◽  
...  
Keyword(s):  
Glycosyl Hydrolase ◽  
Expression System ◽  
Constitutive Expression ◽  
Hypocrea Jecorina ◽  
Glycosyl Hydrolase Family ◽  
Hydrolase Family

scholarly journals Detecting the structural determinants of glycosyl hydrolase family 11 xylanase inhibition

2005 ◽  
Vol 61 (a1) ◽  
pp. c197-c197
Author(s):  
C. De Ranter ◽  
S. Sansen ◽  
K. Gebruers ◽  
K. Brijs ◽  
C. M. Courtin ◽  
...  
Keyword(s):  
Glycosyl Hydrolase ◽  
Glycosyl Hydrolase Family ◽  
Structural Determinants ◽  
Hydrolase Family

scholarly journals A novel α-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile

2005 ◽  
Vol 391 (2) ◽  
pp. 269-276 ◽  
Author(s):  
Manuel Ferrer ◽  
Olga V. Golyshina ◽  
Francisco J. Plou ◽  
Kenneth N. Timmis ◽  
Peter N. Golyshin
Keyword(s):  
Glycosyl Hydrolase ◽  
Soluble Starch ◽  
Glycoside Hydrolases ◽  
Site Directed Mutagenesis ◽  
Preference Order ◽  
Glycosyl Hydrolase Family ◽  
Significant Similarity ◽  
Transglycosylation Activity ◽  
Membrane Bound ◽  
Hydrolase Family

Ferroplasma acidiphilum strain Y (DSM 12658), a ferrous iron-oxidizing, acidophilic and mesophilic archaeon, was found to produce a membrane-bound α-glucosidase (αGluFa) showing no significant similarity to any of the known glycoside hydrolases classified in different families and having an unusual catalytic site consisting of a threonine and a histidine residue. The highest α-glucosidase activity was found at low pH, 2.4–3.5, and the substrate preference order was: sucrose>maltose>maltotriose ≫maltotetraose≫malto-oligosaccharides from maltopentaose to maltoheptaose⋙soluble starch (kcat/Km was 293.0, 197.0, 18.8, 0.3 and 0.02 s−1·mM−1 respectively). The enzyme was able to transfer glucosyl groups from maltose as donor, to produce exclusively maltotriose (up to 300 g/l). Chemical modification and electrospray ionization MS analysis of 5-fluoro-α-D-glucopyranosyl-enzyme derivatives, coupled with site-directed mutagenesis, strongly suggested that the putative catalytic nucleophile in this enzyme is Thr212. Iron was found to be essential for enzyme activity and integrity, and His390 was shown to be essential for iron binding. These results suggest that the metalloenzyme αGluFa is a new member of the glycosyl hydrolase family that uses a novel mechanism for sugar glycosylation and/or transglycosylation.

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