Endoscopic Revision (StomaphyX) versus Formal Surgical Revision (Gastric Bypass) for Failed Vertical Band Gastroplasty

Background. Weight regain secondary to VBG pouch dilation is a typical referral for Bariatric surgeons. In this study we compare an endoluminal pouch reduction (Stomaphyx) to RYGB for revision. Methods. A retrospective review was completed for patients with a previous VBG presenting with weight regain between 2003–2010. Results. Thirty patients were identified for study 23 RYGB, 14 StomaphyX. Significant post procedure BMI loss was seen in each cohort (RYGB, 47.7 ± 7 kg/m2 to 35 ± 7 kg/m2; StomaphyX 43 ± 10 kg/m2 to 40 ± 9 kg/m2, P=0.0007). Whereas nausea and headache were the only complications observed in StomaphyX patients, the RYGB group had a 43.5% complication rate and 1 mortality. Complications following RYGB include: incisional hernia (13%), anastomotic leak (8.7%), respiratory failure (8.7%), fistula (8.7%), and perforation (4.35%). The median length of stay following RYGB was 6 days compared to 1.5 ± 0.5 days following StomaphyX. Conclusion. This study suggests that while RYGB revision may achieve greater weight loss, the complication rates and severity is discouraging. StomaphyX may be a safe alternative. Further technical modifications of the device and longer follow-up may clarify the role of this approach

Clinical Study Endoscopic Revision (StomaphyX) versus Formal Surgical Revision (Gastric Bypass) for Failed Vertical Band Gastroplasty

Background. Weight regain secondary to VBG pouch dilation is a typical referral for Bariatric surgeons. In this study we compare an endoluminal pouch reduction (Stomaphyx) to RYGB for revision. Methods. A retrospective review was completed for patients with a previous VBG presenting with weight regain between 2003-2010. Results. Thirty patients were identified for study 23 RYGB, 14 StomaphyX. Significant post procedure BMI loss was seen in each cohort (RYGB, 47.7 ± 7 kg/m 2 to 35 ± 7 kg/m 2 ; StomaphyX 43 ± 10 kg/m 2 to 40 ± 9 kg/m 2 , = 0.0007). Whereas nausea and headache were the only complications observed in StomaphyX patients, the RYGB group had a 43.5% complication rate and 1 mortality. Complications following RYGB include: incisional hernia (13%), anastomotic leak (8.7%), respiratory failure (8.7%), fistula (8.7%), and perforation (4.35%). The median length of stay following RYGB was 6 days compared to 1.5 ± 0.5 days following StomaphyX. Conclusion. This study suggests that while RYGB revision may achieve greater weight loss, the complication rates and severity is discouraging. StomaphyX may be a safe alternative. Further technical modifications of the device and longer follow-up may clarify the role of this approach

Molecular Basis of Arabinobio-hydrolase Activity in Phytopathogenic Fungi CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF FUSARIUM GRAMINEARUM GH93 EXO-alpha-L-ARABINANASE

The phytopathogenic fungus Fusarium graminearum secretes a very diverse pool of glycoside hydrolases (GHs) aimed at degrading plant cell walls. alpha-L-Arabinanases are essential GHs participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production. Arb93A, the exo-1,5-alpha-arabinanase of F. graminearum encoded by the gene fg03054.1, belongs to the GH93 family, for which no structural data exists. The enzyme is highly active (1065 units/mg) and displays a strict substrate specificity for linear alpha-1,5-L-arabinan. Biochemical assays and NMR experiments demonstrated that the enzyme releases alpha-1,5-L-arabinobiose from the nonreducing end of the polysaccharide. We determined the crystal structure of the native enzyme and its complex with alpha-1,5-L-arabinobiose, a degradation product of alpha-Me-1,5-L-arabinotetraose, at 1.85 and 2.05 angstrom resolution, respectively. Arb93A is a monomeric enzyme, which presents the six-bladed beta-propeller fold characteristic of sialidases of clan GHE. The configuration of the bound arabinobiose is consistent with the retaining mechanism proposed for the GH93 family. Catalytic residues were proposed from the structural analysis, and site-directed mutagenesis was used to validate their role. They are significantly different from those observed for GHE sialidases

Molecular Basis of Arabinobio-hydrolase Activity in Phytopathogenic Fungi: CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF FUSARIUM GRAMINEARUM GH93 EXO-α-l-ARABINANASE*S⃞

The phytopathogenic fungus Fusarium graminearum secretes a very diverse pool of glycoside hydrolases (GHs) aimed at degrading plant cell walls. α-l-Arabinanases are essential GHs participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production. Arb93A, the exo-1,5-α-l-arabinanase of F. graminearum encoded by the gene fg03054.1, belongs to the GH93 family, for which no structural data exists. The enzyme is highly active (1065 units/mg) and displays a strict substrate specificity for linear α-1,5-l-arabinan. Biochemical assays and NMR experiments demonstrated that the enzyme releases α-1,5-l-arabinobiose from the nonreducing end of the polysaccharide. We determined the crystal structure of the native enzyme and its complex with α-1,5-l-arabinobiose, a degradation product of α-Me-1,5-l-arabinotetraose, at 1.85 and 2.05Å resolution, respectively. Arb93A is a monomeric enzyme, which presents the six-bladed β-propeller fold characteristic of sialidases of clan GHE. The configuration of the bound arabinobiose is consistent with the retaining mechanism proposed for the GH93 family. Catalytic residues were proposed from the structural analysis, and site-directed mutagenesis was used to validate their role. They are significantly different from those observed for GHE sialidases

Multiple wheat genomes reveal global variation in modern breeding.

Advances in genomics have expedited the improvement of several agriculturally important crops but similar efforts in wheat (Triticum spp.) have been more challenging. This is largely owing to the size and complexity of the wheat genome1, and the lack of genome-assembly data for multiple wheat lines2,3. Here we generated ten chromosome pseudomolecule and five scaffold assemblies of hexaploid wheat to explore the genomic diversity among wheat lines from global breeding programs. Comparative analysis revealed extensive structural rearrangements, introgressions from wild relatives and differences in gene content resulting from complex breeding histories aimed at improving adaptation to diverse environments, grain yield and quality, and resistance to stresses4,5. We provide examples outlining the utility of these genomes, including a detailed multi-genome-derived nucleotide-binding leucine-rich repeat protein repertoire involved in disease resistance and the characterization of Sm16, a gene associated with insect resistance. These genome assemblies will provide a basis for functional gene discovery and breeding to deliver the next generation of modern wheat cultivars