the official website of the antibody society
For World Cancer Day 2024, The Antibody Society has prepared a snapshot of the clinical development of therapeutic antibodies for cancer indication.
The infographic gives an overview on the trends in first in human studies and approvals, as well as on the active early and late stage pipelines (as of January 2024).
The Communication & Membership Committee selected one entrant for honorable mention:
Rodrigo Garcia Valiente (Amsterdam UMC, University of Amsterdam, the Netherlands)
Image title: A(b) field of dandelions.
The image was not produced using microscopy and therefore didn’t meet the entry requirements. However, the Committee recognised both its scientific and artistic value and decided to give it honorable mention.
Image description: Visual representation of a B-cell clonal repertoire using the programming language R. Each non-singleton clone is indicated with a line and represented as a radial plot whose number of elements correlates with the number of subclones that compose it. Singleton clones are represented as single points.
600 dpi, 28×40 cm. Digital technique.
Antibodies used: The repertoire sequencing database subset from Laserson and Vigneault et al, 2014 contained in the ExampleDb function of the alakazam package, part of the Immcantation pipeline.
Instrument used: R 4.3.0 in an Ubuntu 18.04.6 LTS system. Full sessionInfo(), description, references and script can be found in https://github.com/EDS-Bioinformatics-Laboratory/Clonal_aRt_visualization
Based on the results of our online poll, the winning image is “Surrounded” by Federica Riccio (King’s College London).
Title: Surrounded
Description: A human iPSC-derived cortical neuron (MAP2 – Cyan Hot) sits happily surrounded by astrocytes (GFAP – Red Hot)
Antibodies used: rat anti-GFAP (Invitrogen 13-0300) represented in Red Hot and rabbit anti-MAP2 (Antibodies-Online ABIN1742387) represented in Cyan Hot
Instrument used: confocal laser scanning microscope Leica TCS SP8 (Leica Microsystems)
The winner will receive:
The winning image will be featured as the cover image for the 2024 volume of mAbs, and also as the cover image of the calendar. The calendar will be distributed at the 2023 Antibody Engineering & Therapeutics, in San Diego, in December.
Virginia Metrangolo (University of Copenhagen), image title “Lightening up cancer cells with antibodies”
Jessica Anania (University of Southampton), image title “Cytoskeletal structures following FcR stimulation”
Gabriel Emilio Herrera-Oropeza (King’s College London), image title “Structure of an Unpatterned Cerebral Organoid”
Nathaniel Lam (GSK), image title “Vascularised tumour-on-chip model”
Josefa Chuh (Genentech), image title “Preclinical optimization of Ly6E-targeted ADCs for increased durability and efficacy of anti-tumor response”
Irene Rosa (University of Florence), image title “Double immunofluorescence staining of human tongue, with DAPI nuclear counterstain”
Peng Zhao (AstraZeneca), image title “Enhanced anti-angiogenetic effect of transferrin receptor-mediated delivery of VEGF-trap in a glioblastoma mouse model”
Sandra Lara (AstraZeneca), image title “Antibody dependent phagocytosis of 3D tumour spheroids opsonized with Rituximab anti-CD20”
Danielle Fails (Fortis Life Sciences), image title “Immune profiling of axillary lymph tissues”
Lorna Stewart (Fusion Antibodies), image title “Expression bottlenecks and antibody localisation in stably transfected CHO cells with a GFP marker”
Isabel Uwagboe (King’s College London), image title “”RAGE” against the machine”
We thank everyone who participated, and all our members and followers for taking the time to vote for the best image!
Our student winner is:
Mr. Matheus Oliveira De Souza (Ragon institute of MGH, MIT and Harvard, MIT, The University of Kansas)
Poster title: Enhanced antibody recognition against HIV resistant strains by directed evolution
Our post-doc winner is:
Dr. Nayara Braga Emidio (National Institutes of Health (NIH))
Poster title: Generation of neurokinin receptor ligands with specialized signalling properties via nanobody conjugation
The Antibody Society sponsors competitions each year to recognize and encourage the research activities of promising student/postdoctoral fellows. For the Research Competition, participants submitted a summary of their work on a topic related to antibody research. Winners (1 student and 1 post-doc) were selected based on originality, creativity, scientific merit, clarity of their research and its presentation.
Winners will receive:
Information on past competitions and winners can be found here.
Therapeutic antibodies have been successfully used for decades to treat various diseases. For antibodies targeting soluble antigens, however, a so-called “antibody buffering” effect, which can prolong the persistence of the target in the blood instead of clearing it, was observed. When a conventional IgG is injected into the body and binds to its corresponding antigen, the immune complexes are taken up into the cell where a certain amount of the antigen dissociates from the antibody in the endosomal compartments. The dissociated antigen is directed to the lysosomes for degradation, but the remaining amount of antigen (still bound to the IgG molecules) is recycled out of the cell by the neonatal Fc receptor (FcRn), and this can lead to an extension rather than a decrease of the antigen half-life in the bloodstream (1-5).
To overcome this buffering effect, antibodies with pH-dependent antigen binding characteristics were developed. These IgGs bind the soluble target molecules at physiological pH, but release antigen at the acidic pH in the endosomes. Antigen will then be directed into lysosomes for degradation and free antibodies will be recycled out of the cell, available for consecutive rounds of antigen binding and intracellular delivery. This method has been successfully applied to target different soluble antigens, demonstrating enhanced antigen clearance from the bloodstream compared to a conventional IgG with no pH-dependent antigen binding characteristics (6-9). Furthermore, to facilitate even more efficient antigen elimination, pH-dependent antibodies with additional modifications were generated. By increasing the antibody affinity for FcRn or FcyRIIb, soluble antigen bound to the engineered antibodies will enter the cell much more efficiently than by fluid-phase uptake. The combined effects of increased uptake and pH-dependent antigen dissociation resulted in a remarkable decrease of antigen levels following injection of engineered “sweeping” antibodies, opening possibilities for improved therapeutic applications in the future (10-13). We look forward to receiving further news about pH-dependent antibodies already in development (9, 14-15).
References:
1, Finkelman et al, J Immunol. 1993 Aug 1;151(3):1235-44.
2, O’Hear and Foote, Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):40-4.
3, Phelan et al, J Immunol. 2008 Jan 1;180(1):44-8.
4, Davda and Hansen, MAbs. 2010 Sep-Oct;2(5):576-88. doi: 10.4161/mabs.2.5.12833.
5, Xiao et al, AAPS J. 2010 Dec;12(4):646-57. doi: 10.1208/s12248-010-9222-0.
6, Igawa et al, Nat Biotechnol. 2010 Nov;28(11):1203-7. doi: 10.1038/nbt.1691.
7, Chaparro-Riggers et al, J Biol Chem. 2012 Mar 30;287(14):11090-7. doi: 10.1074/jbc.M111.319764.
8, Devanaboyina et al, MAbs. 2013 Nov-Dec;5(6):851-9. doi: 10.4161/mabs.26389.
9, Fukuzawa et al, Sci Rep. 2017 Apr 24;7(1):1080. doi: 10.1038/s41598-017-01087-7.
10, Igawa et al, PLoS One. 2013 May 7;8(5):e63236. doi: 10.1371/journal.pone.0063236.
11, Iwayanagi et al, J Immunol. 2015 Oct 1;195(7):3198-205. doi: 10.4049/jimmunol.1401470.
12, Igawa et al, Immunol Rev. 2016 Mar;270(1):132-51. doi: 10.1111/imr.12392.
13, Yang et al, accepted manuscript, MAbs. 2017 Aug 8:0. doi: 10.1080/19420862.2017.1359455.
14, ALXN1210, https://clinicaltrials.gov/ct2/show/NCT02946463
15, SA237, https://clinicaltrials.gov/ct2/show/NCT02028884
