Purification and Some Properties of the Endo α-1,4 Polygalactosaminidase from <i>Pseudomonas</i> sp.

Tamura, Jun’ichi; Takagi, Hiroaki; Kadowaki, Kiyoshi

doi:10.1080/00021369.1988.10869068

Cited by 2 publications

(4 citation statements)

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“…881 was shown to be an endo-␣-1,4-galactosaminidase, specific for ␣-1,4-GalN-GalN bonds using an ␣-1,4-GalNAc/GalN substrate isolated from Paecilomyces sp. (24,26). The sequence identity between Ega3 and the GH domain of GH114 Ps is 49%, with high identity around Asp-189 and Glu-247.…”

Section: Discussionmentioning

confidence: 99%

“…881 (GH114 Ps , GenBank TM accession no. D14846.1) is the only member of this family that has been functionally characterized to date (23)(24)(25). GH114 Ps is specific for poly-␣-1,4-GalN with no activity on poly-GalNAc substrates (24).…”

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confidence: 99%

“…D14846.1) is the only member of this family that has been functionally characterized to date (23)(24)(25). GH114 Ps is specific for poly-␣-1,4-GalN with no activity on poly-GalNAc substrates (24). The enzyme exhibits endo-galactosaminidase activity, releasing galactosamine disaccharides and trisaccharides from the nonreducing end of galactosamine polysaccharides (25).…”

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confidence: 99%

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Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms

Bamford

Mauff

Subramanian

et al. 2019

Journal of Biological Chemistry

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Edited by Gerald W. HartAspergillus fumigatus is an opportunistic fungal pathogen that causes both chronic and acute invasive infections. Galactosaminogalactan (GAG) is an integral component of the A. fumigatus biofilm matrix and a key virulence factor. GAG is a heterogeneous linear ␣-1,4 -linked exopolysaccharide of galactose and GalNAc that is partially deacetylated after secretion. A cluster of five co-expressed genes has been linked to GAG biosynthesis and modification. One gene in this cluster, ega3, is annotated as encoding a putative ␣-1,4-galactosaminidase belonging to glycoside hydrolase family 114 (GH114). Herein, we show that recombinant Ega3 is an active glycoside hydrolase that disrupts GAG-dependent A. fumigatus and Pel polysaccharide-dependent Pseudomonas aeruginosa biofilms at nanomolar concentrations. Using MS and functional assays, we demonstrate that Ega3 is an endo-acting ␣-1,4-galactosaminidase whose activity depends on the conserved acidic residues, Asp-189 and Glu-247. X-ray crystallographic structural analysis of the apo Ega3 and an Ega3-galactosamine complex, at 1.76 and 2.09 Å resolutions, revealed a modified (␤/␣) 8 -fold with a deep electronegative cleft, which upon ligand binding is capped to form a tunnel. Our structural analysis coupled with in silico docking studies also uncovered the molecular determinants for galactosamine specificity and substrate binding at the ؊2 to ؉1 binding subsites. The findings in this study increase the structural and mechanistic understanding of the GH114 family, which has >600 members encoded by plant and opportunistic human pathogens, as well as in industrially used bacteria and fungi.

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Section: Discussionmentioning

confidence: 99%

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Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms

Bamford

Mauff

Subramanian

et al. 2019

Journal of Biological Chemistry

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“…Moreover, ROC analysis revealed that serum TFF‐3 had outstanding, I‐FABP had excellent, and IAP had acceptable to distinguish the AE and TE groups based on the AUC values (Table 6). These findings may also be a result of more severe inflammatory activity and increased acute phase response (Tamura et al., 1988) considering the higher effusion WBC in the cats with thoracic effusion. Higher serum and effusion TFF‐3 and IAP concentrations in the cats with thoracic effusion may also be associated with hypoxia due to the presence of effusion (Furuta et al., 2001).…”

Section: Discussionmentioning

confidence: 98%

Intestinal injury and vasculitis biomarkers in cats with feline enteric coronavirus and effusive feline infectious peritonitis

Gülersoy,

Ok,

Üney

et al. 2023

Veterinary Medicine & Sci

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ObjectiveTo investigate intestinal injury, repair and vasculitis biomarkers that may illuminate the progression and/or pathogenesis of feline infectious peritonitis (FIP) or feline enteric coronavirus (FECV) infection.Materials and methodsA total of 40 cats with effusive FIP (30 with abdominal effusion, AE group; 10 with thoracic effusion, TE group) and 10 asymptomatic but FECV positive cats (FECV group), all were confirmed by reverse transcription polymerase chain reaction either in faeces or effusion samples. Physical examinations and effusion tests were performed. Trefoil factor‐3 (TFF‐3), intestinal alkaline phosphatase (IAP), intestinal fatty acid binding protein (I‐FABP), myeloperoxidase‐anti‐neutrophilic cytoplasmic antibody (MPO‐ANCA) and proteinase 3‐ANCA (PR3‐ANCA) concentrations were measured both in serum and effusion samples.ResultsRectal temperature and respiratory rate were highest in the TE group (p < 0.000). Effusion white blood cell count was higher in the AE group than TE group (p < 0.042). Serum TFF‐3, IAP and I‐FABP concentrations were higher in cats with effusive FIP than the cats with FECV (p < 0.05). Compared with the AE group, TE group had lower effusion MPO‐ANCA (p < 0.036), higher IAP (p < 0.050) and higher TFF‐3 (p < 0.016) concentrations.Clinical significanceMarkers of intestinal and epithelial surface injury were higher in cats with effusive FIP than those with FECV. Compared to cats with abdominal effusions, markers of apoptosis inhibition and immunostimulation to the injured epithelium were more potent in cats with thoracic effusion, suggesting the possibility of a poorer prognosis or more advanced disease in these patients.

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Purification and Some Properties of the Endo α-1,4 Polygalactosaminidase from Pseudomonas sp.

Cited by 2 publications

References 4 publications

Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms

Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms

Intestinal injury and vasculitis biomarkers in cats with feline enteric coronavirus and effusive feline infectious peritonitis

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