Lead investigator: Scott Dessain, PhD, MD
Bacteria strains that are resistant to antibiotics represent a scourge in developed countries, the growing prevalence of which demands new approaches to combat. Biofilms deposited by multidrug-resistant bacteria on the surfaces they colonize offer an attractive target for therapeutic attack, based on their role in safeguarding cells against antibiotic treatment.
Patient and noscomial (hospital-borne) infections both contribute to antibiotic-resistant infections of immediate clinical concern. In particular, stubborn infections of patient infusion tubing and other clinical device surfaces are a primary challenge.
LIMR generated a unique, patient-derived, human monoclonal antibody (huMab) that recognizes a universal structural feature present in all amyloid proteins in nature. In the bacterial kingdom, the amyloid protein Curli is a vital component of the pathogenic biofilm that enforces bacterial drug resistance. LIMR’s huMab dissolves Curli-containing biofilms deposited on patient infusion tubing by drug-resistant bacteria. This finding offers a route for prevention and clearance of drug-resistant bacteria of any strain on clinical tubing or device surfaces.
The LIMR huMab binds a structural feature common to all amyloids in nature. This structural epitope is not readily accessed, and the huMab represents a rare antibody cloned from a patient. The huMab not only recognizes this common structure but also breaks up amyloid structures.
The huMab offers uses to clear drug-resistant bacteria by dissolving pathogenic biofilms.
Stage of development
The LIMR huMab has been cloned, and human hybridomas are stored. IgG gene sequences were determined to enable expression in any expression system. Preclinical proof of concept for biofilm clearance has been obtained in collaboration with co-inventors at Temple University.
Pending patent: U.S. provisional patent has been filed.
Develop a product to clear drug-resistant bacteria from clinical tubing or other clinical devices.
Levites Y, O’Nuallain B, Puligedda RD, Ondrejcak T, Adekar SP, Chen C, Cruz PE, Rosario AM, Macy S, Mably AJ, Walsh DM, Vidal R, Solomon A, Brown D, Rowan MJ, Golde TE, Dessain SK (2015). A human monoclonal IgG that binds aß assemblies and diverse amyloids exhibits anti-amyloid activities in vitro and in vivo. J. Neurosci. 35(16):6265-76.
Institutional contact: George C. Prendergast, PhD, LIMR President and CEO, 484.476.8475, email@example.com
L2C Partners contact: Merle Gilmore, 610.662.0940, firstname.lastname@example.org