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You are here: Home / Archives for Antibody Engineering & Therapeutics

Greetings, antibody enthusiasts and AE&T 2024 attendees!

December 12, 2024 by Joshua Dorai

As an international non-profit supporting antibody related research and development, we invite you to explore our extensive resources and the latest insights in the field.

Learn more about what we offer:

  • The latest research and breakthroughs in antibody science.
  • Educational webinars and symposia.
  • Networking opportunities with our society members.
  • Access to the Adaptive Immune Receptor Repertoire (AIRR) Community.

Whether you’re a long-time member or a first-time visitor, there’s something here for everyone passionate about antibody research and development.

Attending AE&T 2024?

We’re happy to be a proud scientific program partner at AE&T 2024 in San Diego from December 15-18! If you’re around, we’d love to connect with you at our booth (#113). Stop by to grab a goodie and learn more about the latest in Antibody Engineering and Therapeutics.

If you’re in or around the San Diego area and are a member of The Antibody Society, don’t forget that TAbS members receive a 15% discount on registration for all AE&T meetings! For more information about AE&T San Diego 2024, visit: https://informaconnect.com/antibody-engineering-therapeutics/ we look forward to seeing you there!

Not a member yet?

If you’re an employee of one of our corporate sponsors, you can sign up for free and gain access to all the exclusive resources and benefits available to our members. If you’re not an employee of a corporate sponsor and are interested in getting involved, explore our membership levels and sign up today to become part of a global community dedicated to advancing antibody science.

Happy Holidays!

Filed Under: Antibody Engineering & Therapeutics

Visit us at Antibody Engineering & Therapeutics, Booth #113!

December 8, 2023 by Janice Reichert

The Antibody Society

Antibody Engineering & Therapeutics commences on Thursday, December 14, 2023! Visit us at Booth #113 for a free T shirt and networking.

And don’t miss the keynote address by Dr. Heather Bax, the 2023 Huston Award recipient.

See you there!

Filed Under: Antibody Engineering & Therapeutics, Uncategorized Tagged With: antibody engineering, antibody therapeutics, Huston Award

Ultralong CDR H3-based knobs: the smallest antibody fragment

March 6, 2023 by Janice Reichert

Photo from Adam Morse.

Summary written by Czeslaw Radziejewski, Ph.D.

Antibody Engineering & Therapeutics, held in December 2022, offered many opportunities to hear exciting and informative presentations by experts in the field, including Vaughn Smider, Ph.D., President, Applied Biomedical Science Institute, who discussed ultralong CDR H3-based knobs as the smallest antibody fragment and Jeff Allen, Ph.D. Vice President, Protein Sciences, Pelican Expression Technology, who discussed Large-scale production of knob peptides.

In 1997 Osvaldo Lopez and his colleagues [1] at the University of Nebraska analyzed transcripts encoding the variable regions of immunoglobulin heavy chains from adult and fetal bovine splenocytes. They were the first to notice the presence of long heavy chain CDR3s. The bovine CDR3s ranged in length from 13 to 28 amino acids, with the average length of CDR H3 being 21 residues in both adults and fetuses. This was longer than had been previously reported for other mammals. In a subset of bovine antibodies, CDR H3s are ultralong (50-70 AA).[2] The structure of ultralong CDR H3s was solved by Wang et al. [2] and the results demonstrated that ultralong CDR H3s all adopt similar architectures, with each composed of a long protruding beta-ribbon “stalk” and diverse disulfide-bonded “knob” (PDB: 4K3D). Up to six cysteine residues can be found in sequences of bovine CDR H3, all involved in disulfide bridges. The loops within the knob domain are thought to be involved in antigen binding. This contrasts with human antibodies where the antigen binding surface is formed from six CDR loops. Bovine CDR H3s are enormously diverse, and the diversity is generated by somatic hypermutation. [3] There is little diversity in CDR H1 and CDR H2, and cows use one light chain. Cows are not unique in having antibodies characterized by long CDR H3s. Other animals with these antibodies include zebu, yak, American and European bison.

It was previously observed that some broadly neutralizing antibodies against HIV also have longer CDR3s. Sok et al. [4] showed that immunization in cows could elicit rapid generation of neutralizing anti-HIV antibodies. Using x-ray crystallography, cryo-electron microscopy, and site-directed mutagenesis, Stanfield et al. [5] elucidated the structure of one monoclonal antibody elicited in cows by immunization with the HIV envelope trimer and showed molecular details of the knob mini-domain binding to a cryptic site on the gp120 CD4 receptor.

Knob domains are reasonably similar in size and shape to cyclotides/knottins, such as prototypic Cyclotide Kalata B1 and other disulfide-bonded peptides. Clinical applications for T cell immunotherapies are now emerging for analogs of cyclotides, for example, inhibition of the Kv1.3 channel. The Kv1.3 potassium channel is expressed abundantly on activated T cells and mediates the cellular immune responses. Sea anemone ShK cyclotide peptide was grafted into the β-ribbon ‘stalk’ of the ultralong CDR H3 scaffold of a humanized bovine IgG and showed the ability to block the Kv1.3. [6] The analog of the ShK peptide called ShK-186 or dalazatide blocks this channel, suppresses T-cell activation and is in human trials as a therapeutic for autoimmune disease.

[Read more…]

Filed Under: Antibody Engineering & Therapeutics Tagged With: ultralong CDR

IgE Class Antibody Immunotherapy for Solid Tumors

March 1, 2023 by Janice Reichert

Summary written by Alicia Chenoweth, PhD, King’s College London; Image from Ref. 7.

Antibody Engineering & Therapeutics, held in December 2022, offered many opportunities to hear exciting and informative presentations by experts in the field, including Professor Sophia Karagiannis from King’s College London, who discussed “IgE Class Antibody Immunotherapy for Solid Tumours”.

Although IgE is notorious for its role in allergic pathogenesis and anti-parasitic immune responses, there is increasing evidence that IgE may also play a role in protection against cancer. IgE deficiency is associated with increased risk of cancer, while higher total serum IgE levels may be protective against certain forms of cancer [1]. Thus, IgE biology may be of interest to cancer therapy. There are many desirable properties of IgE over the traditionally used IgG for cancer therapeutics, such as engaging powerful FceR receptors that are not shared with other classes of Ig, a very high-affinity for its high-affinity receptor FceRI which removes the need for immune complex formation allowing lower-expressing antigens to be targeted, high tissue penetration and persistence (around 1-2 weeks half-life in tissues, compared to a few days for IgG), and the lack of inhibitory receptors.

For IgE therapies, it is important to select a target which is highly expressed in tumor tissue and lowly expressed in normal tissues to enhance safety, as well as making sure that the antigen is not shed in large, multivalent formats in the circulation. Folate receptor alpha (FRa) was selected as a potential target for IgE immunotherapy, as it is overexpressed in several solid tumors, including ovarian cancer, basal breast cancer, and mesotheliomas, while also demonstrating low expression in normal tissues by transcriptomic and immunohistochemical studies [2]. An anti-FRa antibody that had already been in clinical trials and showed safety and efficacy as an IgG format was selected to engineer into an IgE format.

[Read more…]

Filed Under: Antibody Engineering & Therapeutics Tagged With: IgE

Efgartigimod: A Novel FcRn Antagonist in the Treatment of Autoimmune Diseases

February 1, 2023 by Janice Reichert

Summary written by Alicia Chenoweth, PhD, King’s College London

Antibody Engineering & Therapeutics, held in December 2022, offered many opportunities to hear exciting and informative presentations by experts in the field, including Dr. Hans de Haard, Chief Scientific Officer at argenx.

Dr. de Haard’s talk, Efgartigimod: A Novel FcRn Antagonist in the Treatment of Autoimmune Diseases, detailed the mechanism of action and clinical trial results of the FcRn antagonist efgartigimod. Efgartigimod is a human IgG1 Fc fragment with five “Abdeg” mutations (M252Y, S254T, T256E, H433K, N434F) to increase its affinity for FcRn at both low pH and neutral pH (1,2). It is designed to outcompete the binding of serum IgG for FcRn, leading to degradation of the unbound IgG and recycling of efgartigimod back to the surface of the cell to be released back into circulation.

Dr. de Haard discussed the findings of a recent publication in which the biochemical, structural, and in vivo properties of efgartigimod and a full-length antibody counterpart containing the same Abdeg mutations were compared (3). Crystallographic studies of FcRn in complex with the full-length antibody demonstrated that the antigen-binding fragment projects towards the membrane, leading to a potential steric clash hindering binding. This hypothesis was confirmed using a bioassay measuring receptor occupancy, showing that efgartigimod gave a better FcRn occupancy and had improved uptake compared to the full-length antibody. Furthermore, in cynomolgus monkeys, the Fc fragment gave a much faster clearance of tracer antibody and a more potent pharmacodynamic effect compared to full-length antibody. Thus, the Fc fragment was determined to be the better performing FcRn antagonist over the full-length antibody due to improved blocking of IgG recycling in vitro and the more potent PD effect in vivo.

[Read more…]

Filed Under: Antibody Engineering & Therapeutics Tagged With: antibody therapeutics, efgartigimod, generalized myasthenia gravis

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