University of Massachusetts

Douglas T Golenbock

Alberto Visintin

Eicke Latz

Sanjay Ram

Jutamas Shaughnessy

Brian G Monks

Fusion proteins comprising human FH domains 18-20 (FH18-20) linked via an optional linker to IgG Fc, wherein the FH has mutation of D to G at position 1119 in domain 19; FHD1119G/Fc), and methods of use thereof, e.g., to treat pathogen infections.

Factor H-Fc immunotheraphy

The invention includes fusion polypeptides including a first fluorescent protein, e.g., a FRET donor protein, a second fluorescent protein, e.g., a FRET acceptor protein, and, linked to at least one of the fluorescent (e.g., FRET donor or FRET acceptor) proteins, an Fc-region of an immunoglobulin. The polypeptide can be immobilized with respect to a surface via the Fc-region even in the absence of antibodies to either the FRET donor protein or FRET acceptor protein, and can be used as a calibration standard for fluorescence resonance energy transfer includes a polypeptide.

Fluorescent proteins and related methods and compounds

Methods of identifying compounds that modulate the interaction between a TLR and a molecule that interacts with the TLR by direct binding or by inclusion in a complex that associates with the TLR are described. Methods of identifying molecules that interact with a TLR are also described.

Toll-like receptor assays

Chimeric molecules that include a pathogen recognition module derived from a pathogen binding domain of a pathogen recognition protein, e.g., a toll-like receptor (TLR), CD14, BPI, MD-2, scavenger receptors (SRs), surfactant proteins (SP), C-reactive protein (CRP), Mannan-binding lectin (MBL), or complement Clq globular binding domain, an optional linker, and an Fc portion of an antibody are described and are useful for, e.g., drug discovery and treatment of conditions related to TLR signaling.

Anti-pathogen immunoadhesins

TLR9 is localized to endoplasmic reticulum and upon stimulation with a TLR9 ligand, is transported to a tubular lysosomal compartment as is CpG-DNA. Furthermore, it is shown that TLR9 and CpG-DNA directly bind. It was also found that the MyD88 translocates in response to activation of TLR9-mediated signaling. Methods of identifying compounds that affect translocation and activity of TLR9 and MyD88 are described.

Growing community of inventors

Wellesley, MA, United States of America

Douglas T Golenbock