Effects of laser procedure for female urodynamic stress incontinence on pad weight, urodynamics, and sexual function.

INTRODUCTION AND HYPOTHESIS: The impact of the IncontiLaseTM procedure on lower urinary tract symptoms (LUTS) remains unclear. Our aim was to evaluate the effects of the IncontiLaseTM procedure for urodynamic stress incontinence (USI). METHODS: All consecutive women with USI prospectively underwent the IncontiLaseTM procedure. Urodynamic studies, pad testing, LUTS, and sexual function questionnaires were assessed before and after treatment. RESULTS: Thirty-five women underwent the IncontiLaseTM procedure. Among the 28 women with baseline pad weights >1 g, 11 (39.3 %) were objectively cured and 11 (39.3 %) improved. Among the 18 women with mild USI (i.e., baseline pad weight 1-10 g), nine (50 %) were cured and five (27.8 %) improved. Among ten women with baseline pad weight >10 g, two (20 %) were cured and six (60 %) improved. Among the 32 women with complete questionnaire data at 6 months, seven (21.9 %) were subjectively cured, and four (12.5 %) improved. Regarding LUTS, the majority of domains on the King's Health Questionnaire and female sexual desire and function exhibited significant improvements. Forty percent (12/30) of the partners of these patients felt their sexual function had improved at 6 months. Nonetheless, urodynamic values did not differ across the timeline. CONCLUSIONS: The effect of the IncontiLaseTM procedure for mild USI was moderate at 6-month follow-up but was not effective for pad weight >10 g. Moreover, it improved LUTS, quality of life, QoL, and sexual function of both partners. Further studies should be performed to assess long-term sustained efficacy.

Crystal structure of Staphylococcus aureus transglycosylase in complex with a lipid II analog and elucidation of peptidoglycan synthesis mechanism.

Bacterial transpeptidase and transglycosylase on the surface are essential for cell wall synthesis, and many antibiotics have been developed to target the transpeptidase; however, the problem of antibiotic resistance has arisen and caused a major threat in bacterial infection. The transglycosylase has been considered to be another excellent target, but no antibiotics have been developed to target this enzyme. Here, we determined the crystal structure of the Staphylococcus aureus membrane-bound transglycosylase, monofunctional glycosyltransferase, in complex with a lipid II analog to 2.3 Å resolution. Our results showed that the lipid II-contacting residues are not only conserved in WT and drug-resistant bacteria but also significant in enzymatic activity. Mechanistically, we proposed that K140 and R148 in the donor site, instead of the previously proposed E156, are used to stabilize the pyrophosphate-leaving group of lipid II, and E100 in the acceptor site acts as general base for the 4-OH of GlcNAc to facilitate the transglycosylation reaction. This mechanism, further supported by mutagenesis study and the structure of monofunctional glycosyltransferase in complex with moenomycin in the donor site, provides a direction for antibacterial drugs design.