Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity

Koen Wagner; Mark J. Kwakkenbos; Yvonne B. Claassen; Kelly Maijoor; Martino Böhne; Koenraad F. van der Sluijs; Martin D. Witte; Diana J. van Zoelen; Lisette A. Cornelissen; Tim Beaumont; Arjen Q. Bakker; Hidde L. Ploegh; Hergen Spits

doi:https://doi.org/10.1073/pnas.1408605111

Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity

Koen Wagner, Mark J. Kwakkenbos, Yvonne B. Claassen, Kelly Maijoor, Martino Böhne, Koenraad F. van der Sluijs, Martin D. Witte, Diana J. van Zoelen, Lisette A. Cornelissen, Tim Beaumont, Arjen Q. Bakker, Hidde L. Ploegh, Hergen Spits

Research output: Contribution to journal › Article › Academic › peer-review

63 Citations (Scopus)

Abstract

Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains into a single molecule. Here, we present a bispecific format where we have fused two full-sized IgG antibodies via their C termini using sortase transpeptidation and click chemistry to create a covalently linked IgG antibody heterodimer. By linking two potent anti-influenza A antibodies together, we have generated a full antibody dimer with bispecific activity that retains the activity and stability of the two fusion partners

Original language	English
Pages (from-to)	16820-16825
Journal	PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume	111
Issue number	47
DOIs	https://doi.org/10.1073/pnas.1408605111
Publication status	Published - 2014

Access to Document

https://doi.org/10.1073/pnas.1408605111

Cite this

Wagner, K., Kwakkenbos, M. J., Claassen, Y. B., Maijoor, K., Böhne, M., van der Sluijs, K. F., Witte, M. D., van Zoelen, D. J., Cornelissen, L. A., Beaumont, T., Bakker, A. Q., Ploegh, H. L., & Spits, H. (2014). Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111(47), 16820-16825. https://doi.org/10.1073/pnas.1408605111

@article{a20cef09acd548aa94e95152681e5ce2,

title = "Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity",

abstract = "Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains into a single molecule. Here, we present a bispecific format where we have fused two full-sized IgG antibodies via their C termini using sortase transpeptidation and click chemistry to create a covalently linked IgG antibody heterodimer. By linking two potent anti-influenza A antibodies together, we have generated a full antibody dimer with bispecific activity that retains the activity and stability of the two fusion partners",

author = "Koen Wagner and Kwakkenbos, {Mark J.} and Claassen, {Yvonne B.} and Kelly Maijoor and Martino B{\"o}hne and {van der Sluijs}, {Koenraad F.} and Witte, {Martin D.} and {van Zoelen}, {Diana J.} and Cornelissen, {Lisette A.} and Tim Beaumont and Bakker, {Arjen Q.} and Ploegh, {Hidde L.} and Hergen Spits",

year = "2014",

doi = "https://doi.org/10.1073/pnas.1408605111",

language = "English",

volume = "111",

pages = "16820--16825",

journal = "PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA",

issn = "0027-8424",

publisher = "National Acad Sciences",

number = "47",

}

Wagner, K, Kwakkenbos, MJ, Claassen, YB, Maijoor, K, Böhne, M, van der Sluijs, KF, Witte, MD, van Zoelen, DJ, Cornelissen, LA, Beaumont, T, Bakker, AQ, Ploegh, HL & Spits, H 2014, 'Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity', PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 111, no. 47, pp. 16820-16825. https://doi.org/10.1073/pnas.1408605111

Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity. / Wagner, Koen; Kwakkenbos, Mark J.; Claassen, Yvonne B. et al.
In: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol. 111, No. 47, 2014, p. 16820-16825.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity

AU - Wagner, Koen

AU - Kwakkenbos, Mark J.

AU - Claassen, Yvonne B.

AU - Maijoor, Kelly

AU - Böhne, Martino

AU - van der Sluijs, Koenraad F.

AU - Witte, Martin D.

AU - van Zoelen, Diana J.

AU - Cornelissen, Lisette A.

AU - Beaumont, Tim

AU - Bakker, Arjen Q.

AU - Ploegh, Hidde L.

AU - Spits, Hergen

PY - 2014

Y1 - 2014

N2 - Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains into a single molecule. Here, we present a bispecific format where we have fused two full-sized IgG antibodies via their C termini using sortase transpeptidation and click chemistry to create a covalently linked IgG antibody heterodimer. By linking two potent anti-influenza A antibodies together, we have generated a full antibody dimer with bispecific activity that retains the activity and stability of the two fusion partners

AB - Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains into a single molecule. Here, we present a bispecific format where we have fused two full-sized IgG antibodies via their C termini using sortase transpeptidation and click chemistry to create a covalently linked IgG antibody heterodimer. By linking two potent anti-influenza A antibodies together, we have generated a full antibody dimer with bispecific activity that retains the activity and stability of the two fusion partners

U2 - https://doi.org/10.1073/pnas.1408605111

DO - https://doi.org/10.1073/pnas.1408605111

M3 - Article

C2 - 25385586

SN - 0027-8424

VL - 111

SP - 16820

EP - 16825

JO - PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

JF - PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

IS - 47

ER -