9th Annual European Antibody Congress,November 11–13, 2013, Geneva,Switzerland

The annual European Antibody Congress (EAC) has traditionally been the key event for updates on critical scientific advances in the antibody field, and 2013 was no exception. Organized by Terrapinn, the well-attended meeting featured presentations on considerations for developing antibodies and antibody-like therapeutics, with separate tracks for antibody-drug conjugates, naked antibodies, and multispecific antibodies or protein scaffolds. The overall focus of the EAC was current approaches to enhance the functionality of therapeutic antibodies or other targeted proteins, with the ultimate goal being improvement of the safety and efficacy of the molecules as treatments for cancer, immune-mediated disorders and other diseases. Roundtable discussion sessions gave participants opportunities to engage in group discussions with industry leaders from companies such as Genmab, Glenmark Pharmaceuticals, MedImmune, Merrimack Pharmaceuticals, and Pierre Fabre. As the 2013 EAC was co-located with the World Biosimilar Congress, participants also received an update on European Medicines Agency guidelines and thoughts on the future direction and development of biosimilar antibodies in the European Union.     

4th European Antibody Congress 2008: December 1–3, 2008, Geneva,Switzerland

The Fourth European Antibody meeting, organized by Terrapin Ltd., was held in Geneva, a center of the European biopharmaceutical industry. Merck-Serono, NovImmune, Pierre Fabre and Therapeomic are located nearby, as are R&D centers of Boehringer-Ingelheim, Novartis, Roche and Sanofi-Aventis. Over 40 speakers and more than 200 delegates attended the event. Companies represented included Abbott, Ablynx, Adnexus/ BMS, Astra-Zeneca/ CAT/ Medimmune, BiogenIdec, BioRad, Centocor (Johnson & Johnson), Crucell/DSM, Domantis, Dyax, Genmab, Genzyme, Glycart/ Roche, Haptogen, Immunogen, Kyowa-Kirin, LFB, Medarex, Merck-Serono, Micromet, Novartis, Pierre Fabre Laboratories, Roche, Sanofi-Aventis, Seattle-Genetics, Transgene, UCB Celltech and Wyeth. Other attendees included those based in academe or government (University of Amsterdam, University of Zurich, Univeristy Hospital-Lyon, Ecole Polytechnique Federale de Lausanne, INSERM, Tufts University, US National Institutes of Health), consultants, and patent attorneys (Edwards, Angell, Palmer & Dodge). The meeting was very interactive and included exchanges during the many scheduled networking times (exhibitions, speed-networking, lunches and evening receptions). The first day of the three day conference was dedicated to advances in understanding antibody structure-function relationships. Challenges and opportunities in antibody development were the focus of the second day and the third day featured discussion of innovative antibodies and antibody alternatives.

• MAbs. 2009 Mar-Apr; 1(2): 93–103.
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• December 1, 2008 Day 1, Therapeutic antibodies: Advances in dissecting structure-function relationships

MAbs. 2009 Mar-Apr; 1(2): 93–103.

December 1, 2008 Day 1, Therapeutic antibodies: Advances in dissecting structure-function relationships

Alain BeckAuthor information Article notes Copyright and License information DisclaimerDepartment of Physico-Chemistry; Center of Immunology Pierre Fabre; Saint-Julien-en-Genevois, FranceCorresponding author.Correspondence to: Alain Beck; Centre d''Immunologie Pierre Fabre; 5 avenue Napoleon III; Saint-Julien-en-Genevois 74160 France; Email: moc.erbaferreip@kceb.nialaReceived 2009 Jan 20; Accepted 2009 Jan 20.Copyright © 2009 Landes BioscienceThe chairman, Alain Beck (Centre d''Immunologie Pierre Fabre), opened the meeting with the following remarks: Monoclonal antibodies (mAbs) and related-products (immunoconjugates, radioimmuno-conjugates, Fab fragments and Fc-fusion proteins) are the fastest growing class of pharmaceuticals, with nearly 30 products currently approved for a wide range of indications.^3,14 In just the last three years, six new antibodies and derivatives have reached the market. These included molecules that are novel formats, as well as first in class drugs in new therapeutic indications. In 2006, panitumumab (Vectibix) was the first fully human IgG2 mAb generated by immunization of humanized transgenic mice and the second anti-EGFR mAb to gain approval. Also in 2006, ranibizumab (Lucentis), the first E. coli-produced Fab fragment and the first affinity matured antibody, was approved as a treatment age-related macular degeneration. Later, tocilizumab (Actemra) a conventional IgG1, but directed against a new target (IL-6R), was registered in Japan; BLAs are pending both in the US and in Europe. In 2007, eculizumab (Soliris) was approved for paroxysmal nocturnal hemoglobinuria. Eculizumab was constituted by an original IgG2/4 hybrid format, and is unable to bind Fc receptors or activate the complement cascade. In 2008, rinolacept (Arcalyst), an IL-1R-Fc fusion protein also called IL-1 trap, was registered for cryopyrin-associated periodic syndromes. Also in 2008, certolizumab pegol (Cimzia) became the first PEGylated Fab fragment to gain approval. The product, indicated for Crohn disease, is produced in E. coli and conjugated to large PEG residues (40 kDa). Interestingly, from a structure-function standpoint, certolizumab was crystallized and the 3D model of this original PEG-Fab was recently reported.⁴ In addition to these six new antibody or antibody-related product approvals, the first two biosimilar antibodies, Reditux (a copy of rituximab developed by Dr Reddy) and Clotinab (a biogeneric of abciximab developed by ISU ABXIS), were recently launched in India and in South Korea, respectively. Active discussions are ongoing regarding whether such generic biopharmaceuticals may also be approved in Europe, following approval of other glycoproteins such as erythropoietin.¹⁶     

6th Annual European Antibody Congress 2010: November 29–December 1, 2010, Geneva,Switzerland

The 6^th European Antibody Congress (EAC), organized by Terrapinn Ltd., was held in Geneva, Switzerland, which was also the location of the 4^th and 5^th EAC.^1,2 As was the case in 2008 and 2009, the EAC was again the largest antibody congress held in Europe, drawing nearly 250 delegates in 2010. Numerous pharmaceutical and biopharmaceutical companies active in the field of therapeutic antibody development were represented, as were start-up and academic organizations and representatives from the US Food and Drug Administration (FDA). The global trends in antibody research and development were discussed, including success stories of recent marketing authorizations of golimumab (Simponi^®) and canakinumab (Ilaris^®) by Johnson & Johnson and Novartis, respectively, updates on antibodies in late clinical development (obinutuzumab/GA101, farletuzumab/MORAb-003 and itolizumab/T1 h, by Glycart/Roche, Morphotek and Biocon, respectively) and success rates for this fast-expanding class of therapeutics (Tufts Center for the Study of Drug Development). Case studies covering clinical progress of girentuximab (Wilex), evaluation of panobacumab (Kenta Biotech), characterization of therapeutic antibody candidates by protein microarrays (Protagen), antibody-drug conjugates (sanofi-aventis, ImmunoGen, Seattle Genetics, Wyeth/Pfizer), radio-immunoconjugates (Bayer Schering Pharma, Université de Nantes) and new scaffolds (Ablynx, AdAlta, Domantis/GlaxoSmithKline, Fresenius, Molecular Partners, Pieris, Scil Proteins, Pfizer, University of Zurich) were presented. Major antibody structural improvements were showcased, including the latest selection engineering of the best isotypes (Abbott, Pfizer, Pierre Fabre), hinge domain (Pierre Fabre), dual antibodies (Abbott), IgG-like bispecific antibodies (Biogen Idec), antibody epitope mapping case studies (Eli Lilly), insights in FcγRII receptor (University of Cambridge), as well as novel tools for antibody fragmentation (Genovis). Improvements of antibody druggability (Abbott, Bayer, Pierre Fabre, Merrimack, Pfizer), enhancing IgG pharmacokinetics (Abbott, Chugai), progress in manufacturing (Genmab, Icosagen Cell Factory, Lonza, Pierre Fabre) and the development of biosimilar antibodies (Biocon, Sandoz, Triskel) were also discussed. Last but not least, identification of monoclonal antibodies (mAbs) against new therapeutic targets (Genentech, Genmab, Imclone/Lilly, Vaccinex) including Notch, cMet, TGFβRII, SEMA4D, novel development in immunotherapy and prophylaxis against influenza (Crucell), anti-tumor activity of immunostimulatory antibodies (MedImmune/Astra Zeneca) and translations to clinical studies including immunogenicity issues (Amgen, Novartis, University of Debrecen) were presented.Key words: therapeutic antibodies, antibody-drug conjugates, protein scaffolds, biosimilars, bioproduction

• MAbs. 2011 Mar-Apr; 3(2): 111–132.
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• Day 1: November 29, 2010

2011 Mar-Apr; 3(2): 111–132. Published online 2011 Mar 1. doi: 10.4161/mabs.3.2.14788

Day 1: November 29, 2010

Alain Beck Copyright and License information DisclaimerCopyright notice The EAC chairman, Alain Beck (Centre d''Immunologie Pierre Fabre), opened the meeting with a presentation on strategies and challenges for the next generation of therapeutic antibodies.³ By analyzing the regulatory approvals of IgG-based biotherapeutic agents in the past ten years, we can gain insights into the successful strategies used by pharmaceutical companies so far to bring innovative drugs to the market. Strategies to optimize the structure of IgG antibodies and to design related or new structures with additional functions were presented. A detailed knowledge of antibody structure and activity now allows researchers to engineer primary antibodies on a more rational basis. Most approved antibodies are chimeric, humanized or human IgGs with similar constant domains. Numerous studies looking at the structure-function relationships of these antibodies have been published in the past five years with the aim of identifying antibody microvariants⁴ and investigating the influence of these variants on antigen binding, stability, pharmacokinetics (PK) and pharmacodynamics (PD). This knowledge is now being used to increase homogeneity and mitigate the chemistry, manufacture and control (CMC) liabilities of preclinical antibody candidates by genetic engineering. The removal by mutation of instability or aggregation hot spots in the antibody complementarity-determining regions (CDRs), and the use of hinge-stabilized or aglycosylated IgG4, are just a few examples of antibodies with improved pharmacological properties, including decreased heterogeneity, that are currently in development.Dr. Beck explained that the variable fragment (Fv) of an antibody is responsible for interactions with antigens and dictates essential properties such as binding affinity and target specificity. The origin of the Fv in therapeutic antibodies can be diverse, e.g., hybridomas, human antibody libraries, rodents with a human antibody repertoire or primatized or humanized antibodies from various species. Affinity maturation allows the binding affinity of the Fv to be improved or target selectivity to be modulated. The constant fragment (Fc) of an antibody is responsible for interactions with immune cells, and the associated properties of the Fc can also be modulated by engineering at several levels:⁵ altering the glycosylation status to regulate anti- and pro-inflammatory properties, modulating antibody-dependent cellular cytotoxicity (ADCC) by site-directed mutagenesis to alter binding to Fc receptors, increasing the serum half-life by Fc engineering to increase binding to the neonatal Fc receptor (FcRn), thereby preventing IgG degradation, and increasing complement activation by isotype chimerism. Additional functions can be endowed on antibodies by conjugation to other drugs. To date, the clinical success of antibody-drug conjugates (ADCs) has been limited. Nevertheless, promising new ADCs that include linkers with optimized properties (e.g., hydrolysable in the cytoplasm, resistant or susceptible to proteases or resistant to multi-drug resistance efflux pumps) and highly cytotoxic drugs are being studied in advanced clinical trials (e.g., trastuzumab emtansine, inotuzumab ozogamicin and brentuximab vedotin).⁶ IgGs have also been engineered to contain unique drug conjugation positions to obtain uniform and more homogeneous drug conjugates, such as ThioMab-drug conjugates, which have a uniform stoichiometry of approximately two coupled drugs per antibody molecule. Collectively, these advances should open new therapeutic avenues to deliver highly cytotoxic drugs with increased tolerability.     

7th Annual European Antibody Congress 2011: November 29–December 1, 2011, Geneva,Switzerland

The 7^th European Antibody Congress (EAC), organized by Terrapin Ltd., was again held in Geneva, Switzerland, following on the tradition established with the 4^th EAC. The 2011 version of the EAC was attended by nearly 250 delegates who learned of the latest advances and trends in the global development of antibody-based therapeutics. The first day focused on advances in understanding structure-function relationships, choosing the best format, glycoengineering biobetter antibodies, improving the efficacy and drugability of mAbs and epitope mapping. On the second day, the discovery of novel targets for mAb therapy, clinical pipeline updates, use of antibody combinations to address resistance, generation and identification of mAbs against new targets and biosimilar mAb development were discussed. Antibody-drug conjugates, domain antibodies and new scaffolds and bispecific antibodies were the topics of the third day. In total, nearly 50 speakers provided updates of programs related to antibody research and development on-going in the academic, government and commercial sectors.Key words: therapeutic antibodies, antibody-drug conjugates, protein scaffolds, bispecific antibodies, biosimilar antibodies     

24th International Ornithological Congress, Hamburg, Germany, 13–19 August 2006

Announcement

24th International Ornithological Congress, Hamburg, Germany, 13–19 August 2006     

Human Proteome Organisation’s 7th World Congress, 2008

The annual world congress of Human Proteome Organisation (HUPO) is one of the premier meetings in proteomics. Rotating between Europe, North America and Asia/Oceana, this year’s host city was Amsterdam, The Netherlands. Proteomics still being a rapidly evolving field, HUPO meetings provide a platform for technical advancements in protein purification and separation techniques, innovations in mass spectrometry and applications in bioinformatics and computational biology. A special focus of this year’s meeting was on proteome biology, indicating that the state of technology has progressed to a level permitting interrogation of biological systems in a meaningful way.     

Are populations of European earwigs,Forficula auricularia,density dependent?

Biocontrol using naturally occurring predators is often limited by population parameters of those predators. Earwigs, Forficula auricularia L. (Dermaptera: Forficulidae), are important predators in fruit orchards. They are capable of suppressing outbreaks of pest species, such as pear psyllid and various apple aphid species. Earwigs therefore play an important role in integrated pest management in fruit orchards and are essential in organic top fruit cultures. However, earwig populations are very unstable, showing large between-year variation in densities, which limits their practical use. Extensive knowledge of regulating processes of populations is therefore crucial for efficient orchard management. A 2-year phenological study in several apple and pear orchards in Belgium showed a significant displacement of third instars during the second brood in relation to the presence of adults. We also observed a yearly population crash at the time of moulting into adults. This population decrease was correlated with earwig numbers at peak density. The crash occurred at lower earwig densities in apple orchards than in pear orchards. Six possible regulating mechanisms for this density-dependent decrease are discussed: (1) migration, (2) pesticides or orchard management, (3) starvation, (4) pathogens, (5) parasites and parasitoids, and (6) predation or cannibalism. If we can identify these regulating processes, specific management activities could be developed to prevent the population crash, hereby increasing population densities in the orchards.     

Closing lecture — ISPMB Congress

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Closing lecture — ISPMB Congress