William Dall’Acqua supervises a group in the Department of Antibody Discovery and Protein Engineering, R&D at AstraZeneca.

His team of 29 scientists is working on the discovery of new therapeutic antibody drugs and establishing novel antibody technology platforms. In particular, William’s group has developed a novel and ground-breaking strategy to improve the serum half-life of human IgG. Such long-lasting molecules have the potential to make an impact in the field of antibody-based therapy.

William has been studying protein structure, function and engineering for over 20 years and has co-authored over 45 papers and one book chapter in the field. He has also been named inventor on 16 issued patents. He has Bachelor and Masters’ Degrees in Biochemistry from the University of Paris, and a PhD in Immunology from the University of Paris in conjunction with the University of Maryland. He also spent two and a half years as a postdoctoral fellow at Genentech’s Molecular Oncology Department, before joining AstraZeneca.

  Extending the half-life of antibodies

As soon as we got the early data, it was clear the YTE platform was very robust. We ended up improving the antibody half life by up to 2-4 times.

William Dall’Acqua Vice President, Antibody Discovery and Protein Engineering, R&D

LATEST PROJECT

The YTE leap in technology

POSITION

Head, Antibody Lead Generation, Gaithersburg

PEER RECOGNITION

Elsevier publication co-editor, peer publication reviewer, NIH site reviewer, panellist, SAB member and speaker at multiple conferences

  Featured publications

Enhancement of antibody-dependent cell-mediated cytotoxicity

Borrok MJ, Luheshi NM, Beyaz N et al. Enhancement of antibody-dependent cell-mediated cytotoxicity by endowing IgG with FcαRI (CD89) binding. MAbs. 2015 4; 7(4):743-51.

Structural Insights into Sifalimumab

Oganesyan V, Peng L, Woods RM, Wu H, Dall'Acqua WF. Structural Insights into the Neutralization Properties of the Fully Human, Anti-interferon Monoclonal Antibody Sifalimumab. J Biol Chem. 2015; 290(24):14979-85.

Molecular basis of bispecific antibody's target selectivity

Mazor Y, Hansen A, Yang C et al. Insights into the molecular basis of a bispecific antibody's target selectivity. MAbs. 2015; 7(3):461-9.

Improving target cell specificity

Mazor Y, Oganesyan V, Yang C et al. Improving target cell specificity using a novel monovalent bispecific IgG design. MAbs. 2015; 7(2):377-89.

Antagonistic activity of anifrolumab

Peng L, Oganesyan V, Wu H, Dall'Acqua WF, Damschroder MM. Molecular basis for antagonistic activity of anifrolumab, an anti-interferon-α receptor 1 antibody. MAbs. 2015; 7(2):428-39.

FcRn affinity threshold that governs IgG recycling

Borrok MJ, Wu Y, Beyaz N et al. pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling. J Biol Chem. 2015 ; 290(7):4282-90.

It is an amazing feeling to see something you've worked on in the lab make it to patients and make a difference.

William Dall’Acqua