Janssen Biotech, Inc.

New York University

Jansson Biotech, Inc.

Brian Whitaker

John Wheeler

Alexey Teplyakov

Mark Chiu

John Kehoe

Mary Ryan

Sandra Santulli-Marotto

Eilyn Lacy

Alfred Del Vecchio

Lynne Murray

Ken Boakye

William Strohl

Victor J Torres

Randall J Brezski

Anthony S Lynch

Peter T Buckley

Keri Dorn

Michelle Kinder

David M Knight

Jinquan Luo

Raymond W Sweet

Juan C Almagro

Ping Tsui

Mark Tornetta

Jin Lu

Di Zhang

Qiang Chen

Bernard Amegadzie

Lei Shi

Lionella Borozdina-Birch

Ramachandra Reddy

The present invention relates to antibodies specifically binding CCL17, polynucleotides encoding the antibodies or fragments, and methods of making and using the foregoing.

Anti-CCL17 antibodies

FN3 domains that specifically bind Fc&#x3b3;RII, their conjugates and antibody fusions, isolated nucleotides encoding the molecules, vectors, host cells, and methods of making and using them.

Fc &#x3b3;  RIII binding fibronectin type III domains, their conjugates and multispecific molecules comprising them

The present application generally relates to multi-specific molecules that bind to multiple bacterial virulence factors, methods for producing these binding molecules, and the use of these binding molecules to treat bacterial infections. In particular, the binding molecules comprise at least two binding domains, preferably an antibody or antibody fragment and an alternative scaffold. The first binding domain is capable of binding to a glycosylated staphylococcal surface protein, preferably an SDR-containing protein. The second binding domain is capable of binding to a staphylococcal leukotoxin, preferably LukAB, LukD or LukE. These multi-specific binding compounds have killing activity against staphylococci and, thus, can be used in the treatment and/or amelioration of ainfection, including methicillin-resistant

Compositions and methods for phagocyte delivery of anti-staphylococcal agents

Described and claimed herein are combinatorial synthetic Fab libraries displayed on a phage pIX protein. The libraries were built on scaffolds representing the most frequently used genes in human antibodies, which were diversified to mirror the variability of natural antibodies. After selection using a diverse panel of proteins, numerous specific and high-affinity Fabs were isolated. By a process called in-line maturation the affinity of some antibodies was improved up to one hundred-fold yielding low pM binders suitable for in vivo use. This work thus demonstrates the feasibility of displaying complex Fab libraries as pIX-fusion proteins for antibody discovery and lays the foundations for studies on the structure-function relationship of antibodies.

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Brian Whitaker