Open Access. Powered by Scholars. Published by Universities.®

Ophthalmology Commons

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 2 of 2

Full-Text Articles in Ophthalmology

Neuro-Ophthalmology Diseases In Elderly, Aishwarya Gatiganti Jan 2023

Neuro-Ophthalmology Diseases In Elderly, Aishwarya Gatiganti

School of Medicine Publications and Presentations

It is well understood that as the body begins to age, its ability to adapt and sustain itself decreases. The eyes are not immune to this effect, and the complex interplay between the eyes and the brain deteriorates insidiously over time. There has been a notable increase in the elderly population, and diseases such as the ones described above need to be at the forefront of an ophthalmologist's mind when treating this population. Neuro-ophthalmology diseases in the elderly are not well known to general practitioners but should be included in the differential due to the potential of rapid deterioration and …


Dmbt1 Inhibition Of Pseudomonas Aeruginosa Twitching Motility Involves Its N-Glycosylation And Cannot Be Conferred By The Scavenger Receptor Cysteine-Rich Bacteria-Binding Peptide Domain., Jianfang Li, Stephanie J Wan, Matteo M E Metruccio, Sophia Ma, Kamran Nazmi, Floris J Bikker, David J. Evans, Suzanne M J Fleiszig Sep 2019

Dmbt1 Inhibition Of Pseudomonas Aeruginosa Twitching Motility Involves Its N-Glycosylation And Cannot Be Conferred By The Scavenger Receptor Cysteine-Rich Bacteria-Binding Peptide Domain., Jianfang Li, Stephanie J Wan, Matteo M E Metruccio, Sophia Ma, Kamran Nazmi, Floris J Bikker, David J. Evans, Suzanne M J Fleiszig

Faculty Publications & Research of the TUC College of Pharmacy

The scavenging capacity of glycoprotein DMBT1 helps defend mucosal epithelia against microbes. DMBT1 binding to multiple bacterial species involves its conserved Scavenger Receptor Cysteine-Rich (SRCR) domains, localized to a 16-mer consensus sequence peptide, SRCRP2. Previously, we showed that DMBT1 bound Pseudomonas aeruginosa pili, and inhibited twitching motility, a pilus-mediated movement important for virulence. Here, we determined molecular characteristics required for twitching motility inhibition. Heat-denatured DMBT1 lost capacity to inhibit twitching motility and showed reduced pili binding (~40%). Size-exclusion chromatography of Lys-C-digested native DMBT1 showed that only high-Mw fractions retained activity, suggesting involvement of the N-terminal containing repeated SRCR domains with …