mAbs最新文献

{"title":"Physiochemical and functional evaluation of the first-in-class anti-cancer IgE antibody drug, MOv18, through process development and good manufacturing practice production.","authors":"Heather J Bax, Jitesh Chauhan, Alexandra J McCraw, Melanie Grandits, Chara Stavraka, Heike Lentfer, Tim Hillyer, Simon Carroll, Kim Vigor, Chris Selkirk, Mariangela Figini, Jack Cheeseman, Paulina A Urbanowicz, Richard A Gardner, Daniel I R Spencer, Nigel Westwood, Sarah Mellor, James Spicer, Debra H Josephs, Sophia N Karagiannis","doi":"10.1080/19420862.2025.2451295","DOIUrl":"10.1080/19420862.2025.2451295","url":null,"abstract":"<p><p>Antibodies used for cancer therapy are monoclonal IgGs, but tumor-targeting IgE antibodies have shown enhanced effector cell potency against cancer in preclinical models. Research-grade recombinant IgE antibodies have been generated and studied for several decades. The recent Phase 1 clinical trial of the first-in-class MOv18 IgE, however, necessitated the inaugural process development and scaled manufacture of a recombinant IgE to clinical quality standards. During the process development and scaled Good Manufacturing Practice production, we demonstrate the retention of glycosylation state, biophysical profile, and functional characteristics of MOv18 IgE, including Fc-mediated mast cell degranulation and tumor cell killing. Assessment of manufacturing parameters shows expected pH, purity, concentration, and stability properties, as well as below threshold levels of known biological manufacturing contaminants. We confirm the suitability of the pipeline described for generating intact, functionally active, clinical-grade material for this novel therapeutic class as an Investigational Medicinal Product (IMP), with comparable characteristics to the original research-grade antibody. Furthermore, we screened patient blood <i>ex vivo</i> for potential type I hypersensitivity reaction to MOv18 IgE, using the basophil activation test, to identify patients not predicted to be hypersensitive to MOv18 IgE administration. This study supports the production of functionally active clinical grade (IMP) recombinant IgE and paves the way for the development of a new therapeutic antibody class for a range of antigenic specificities and disease settings.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2451295"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143007982","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Proceedings of the 15^th European immunogenicity platform open symposium on immunogenicity of biopharmaceuticals.","authors":"Sophie Tourdot, Karien Bloem, Lysie Champion, Anne S De Groot, Axel Ducret, Patrick Garidel, Joanna Grudzinska-Goebel, Michael Gutknecht, Timothy Hickling, Frank Horling, Marina Ichetovkin, Alison Johnson, Issa Jyamubandi, Anette Karle, Arno Kromminga, Ebru Aydin Kurtulmus, Floris Loeff, Bernard Maillere, Lydia Michaut, Francesca Minelli, Morten Nielsen, Vivek Nayak, Robert Nelson, Marc Pallardy, Sofie Pattyn, Joao Pedras-Vasconelos, Elise Pepermans, Alain Poyau, Matthias Reichel, Amy Rosenberg, Zuben Sauna, Manisha Saxena, Noel Smith, Veerle Snoeck, Lester Thoo, Michael Tovey, Daniela Verthelyi, Rene Wuttke, Daniel Yerly, Daniel Kramer","doi":"10.1080/19420862.2025.2487604","DOIUrl":"10.1080/19420862.2025.2487604","url":null,"abstract":"<p><p>The European Immunogenicity Platform (EIP) celebrated the 15th edition of its Open Symposium on Immunogenicity of Biopharmaceuticals and its associated one-day workshop on 22-24 February 2024 in Lisbon. The meeting attracted experts and newcomers across industry, regulatory agencies, and academia, who actively participated in 3 days of discussion on risk assessment, monitoring, and mitigation of unwanted immunogenicity of biologics. Besides oral presentations, poster sessions were held to maximize scientific exchange and networking opportunities. Therapeutic proteins and emerging gene and cell-based therapies present promising therapeutic options for addressing unmet medical needs or when conventional treatment approaches have failed. Nonetheless, the development of an immune response against these therapeutic agents is a significant concern, as it occurs in a considerable number of cases across various products and indications. The specific anti-drug antibodies that develop can lead to adverse safety events, inhibition of drug activity, or accelerated clearance, all of which result in a loss of treatment efficacy. The EIP serves as a forum for experts and newcomers in the immunogenicity field, fostering discussion among scientists from industry and academia, encouraging interactions with regulatory agencies, and disseminating knowledge and advancements in immunogenicity sciences to the broader scientific community. This report covers the main topics discussed during the EIP 15th Open Symposium on Immunogenicity of Biopharmaceuticals, and the one-day workshop on practical aspects of immunogenicity held prior to the conference. Key topics included immunogenicity testing, clinical relevance of immunogenicity, immunogenicity risk assessment and mitigation, and current regulatory considerations.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2487604"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12054923/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143780427","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Artificial intelligence-driven computational methods for antibody design and optimization.","authors":"Luiz Felipe Vecchietti, Bryan Nathanael Wijaya, Azamat Armanuly, Begench Hangeldiyev, Hyunkyu Jung, Sooyeon Lee, Meeyoung Cha, Ho Min Kim","doi":"10.1080/19420862.2025.2528902","DOIUrl":"10.1080/19420862.2025.2528902","url":null,"abstract":"<p><p>Antibodies play a crucial role in our immune system. Their ability to bind to and neutralize pathogens opens opportunities to develop antibodies for therapeutic and diagnostic use. Computational methods capable of designing antibodies for a target antigen can revolutionize drug discovery, reducing the time and cost required for drug development. Artificial intelligence (AI) methods have recently achieved remarkable advancements in the design of protein sequences and structures, including the ability to generate scaffolds for a given motif and binders for a specific target. These generative methods have been applied to antigen-conditioned antibody design, with experimental binding confirmed for de novo-designed antibodies. This review surveys current AI methods used in antibody development, focusing on those for antigen-conditioned antibody design. The results obtained by AI-based methodologies in antibody and protein research suggest a promising direction for generating de novo binders for various target antigens.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2528902"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12279266/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144659593","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development and preclinical characterization of AMG 329: a human antibody neutralizing FLT3 ligand.","authors":"Annie Lau-Kilby, Michele Gunsior, Agata Bartczak, Susan Chyou, James Hester, Dorothy Sims, Xiaodong Xiao, Peter Pavlik, Yan Chen, Kerry A Casey, Kamelia Zerrouki, Qian Wang, M Jack Borrok, Anna M Hansen, William A Rees","doi":"10.1080/19420862.2025.2527677","DOIUrl":"10.1080/19420862.2025.2527677","url":null,"abstract":"<p><p>The feline McDonough sarcoma-like tyrosine kinase 3 (FLT3)/FLT3 ligand (FLT3L) signaling pathway regulates the development and activity of dendritic cells (DCs) and other myeloid cells, including monocytes. FLT3L, DCs, and monocytes have been implicated in several autoimmune diseases. Here, we describe the development and characterization of a human immunoglobulin G1λ monoclonal antibody (AMG 329; formerly MEDI1116/VIB-1116/HZN-1116) targeting human FLT3L. AMG 329 was derived from a large human combined antibody display library; it was optimized to enhance affinity for FLT3L and reduce antibody dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity. Binding affinity was determined by surface plasmon resonance interaction analysis. Specificity of FLT3L was measured using cell-based flow cytometry and an in vitro functional neutralization assay. ADCC activity was measured using an in vitro cell culture system. Toxicity and toxicokinetics were evaluated in cynomolgus monkeys during AMG 329 dosing (5-100 mg/kg; ≤ 27 weeks) and recovery (≤32 weeks). The AMG 329 antigen-binding region selectively bound to human and cynomolgus monkey FLT3L with affinities of 170 and 63 pM, respectively. AMG 329 specifically bound to and neutralized soluble and cell-bound human FLT3L and did not induce ADCC. AMG 329 administration generally reduced circulating plasmacytoid, conventional DC, and classical monocyte relative proportions in cynomolgus monkeys in a non-dose-dependent manner. Disruption of the FLT3/FLT3L signaling pathway presents a new potential therapeutic approach to treat autoimmune and inflammatory diseases. AMG 329 is a selective human monoclonal antibody antagonist of FLT3L that is currently being investigated in clinical studies.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2527677"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12239813/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144584297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Impact of antibody Fc engineering on translational pharmacology, and safety: insights from industry case studies.","authors":"Frank R Brennan, J Ryan Polli, Jean Sathish, Melissa Ramones, Babette Wolf, Tilman Schlothauer, Shirley J Peters, Curtis C Maier, Changhua Ji, David L Wensel, Derrick Witcher, Patricia C Ryan, T Scott Manetz, Adriano Flora, Brian Soper, Birgit Fogal, Lindsey Dzielak, Xiaoting Wang, Prathap Nagaraja Shastri, Karen Price, Michael Doyle, Nidhi Sharda, Mary Struthers, Maximilian Brinkhaus, Bianca Balbino, Eric Stefanich, Masaki Honda, Jan Terje Andersen, Shermaine Mitchell-Ryan, David P Humphreys","doi":"10.1080/19420862.2025.2505092","DOIUrl":"10.1080/19420862.2025.2505092","url":null,"abstract":"<p><p>Therapeutic monoclonal antibodies (mAbs) are often designed to not only bind targets via their antigen-binding domains (Fabs) but to also engage with cell surface receptors, FcγRs and FcRn, through their Fc regions, which may result in a variety of functional outcomes, including antibody- dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), complement-dependent cytotoxicity (CDC) and alteration of circulating half-lives. Engineering the Fc regions to achieve desirable pharmacology and pharmacokinetics is a widely adopted strategy in drug development. Fc regions can be modified through amino acid substitutions and glycoengineering, resulting in enhanced or reduced effector functions, preferential binding to FcR subtypes, or pH-dependent binding to FcRns. These alterations in binding and effector activities of mAbs may potentially also be accompanied by undesirable effects or safety concerns. Critical assessment of pharmacology and safety in the nonclinical setting is essential before exposing humans to the engineered mAb. For Fc-modified mAbs, the choice of in vitro and in vivo nonclinical pharmacology and safety models need to account for species differences in FcR expression and function, potentially divergent effects of Fc modifications in humans versus nonclinical species, impact of target and cognate ligand expression patterns, and potential impact of emergent anti-drug antibodies directed against the mAb. Using a variety of industry case studies, we highlight key aspects of nonclinical pharmacology and toxicology testing strategies, factors that influence choice of nonclinical models, translatability of findings, input from health authorities and suggest best practice approaches for nonclinical testing of Fc modified mAbs.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2505092"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12239809/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144584298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rational design of antibodies with pH-dependent antigen-binding properties using structural insights from broadly neutralizing antibodies against α-neurotoxins.","authors":"Jack Wade, Nina Štrancar, Monica L Fernández-Quintero, Suzana Siebenhaar, Tom Jansen, Edward P W Meier, Timothy P Jenkins, Sara P Bjørn, Giang T T Nguyen, Bruno Lomonte, José Maria Gutiérrez, Christoffer V Sørensen, Johannes R Loeffler, Arijit Paul, Tulika Tulika, Johnny Arnsdorf, Sanne Schoffelen, Emil V S Lundquist, Jennifer Sørensen, Andrew B Ward, Bjørn G Voldborg, Markus-Frederik Bohn, Esperanza Rivera-de-Torre, J Preben Morth, Andreas H Laustsen","doi":"10.1080/19420862.2025.2553624","DOIUrl":"10.1080/19420862.2025.2553624","url":null,"abstract":"<p><p>Antibodies that bind in a pH-dependent manner to their antigens show promise for enhanced neutralization potency and blocking capacity against extracellular targets. However, because the mechanisms governing pH-dependent antigen binding remain poorly understood, engineering approaches are often limited to incorporating histidine residues in the antibody complementarity-determining regions. Here, we use a panel of human monoclonal antibodies with neutralizing activity to long-chain α-neurotoxins (LNTxs) to investigate pH-dependent antigen binding. The antibodies vary in their light chains but have conserved histidine residues in their variable domains, allowing us to explore how other residues may affect pH dependence. Comparative structural and molecular dynamics studies between two antibodies with and without pH-dependent antigen-binding properties reveal that both antibodies neutralize LNTxs by mimicking LNTx-receptor interactions through their heavy chains. We hypothesize that part of the pH-dependency can be controlled by the light chain through modulation of water access to residues at the heavy-light-chain interface. We show that pH-dependent antigen-binding properties can be introduced into monoclonal antibodies through the substitution of selected residues at the heavy-light-chain interface. Specifically, we replaced tyrosine residues in the light chain with small polar and apolar amino acid residues in a structurally related anti-LNTx antibody with limited inherent pH-dependent antigen-binding properties, and found that these smaller substitutions enhanced pH-dependence more effectively than histidine substitutions alone. Our findings suggest a strategy for engineering pH-dependent antigen binding in antibodies that goes beyond the exclusive use of histidine doping.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2553624"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12439581/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145040099","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ManNAc attenuates Man5 glycoform abundance through GNE-mediated metabolic channeling of UDP-GlcNAc to N-glycosylation modifications via CMP-Neu5Ac biosynthesis.","authors":"Ruiqiang Sun, Miaomiao Chai, Jiahao Man, Guiju Yang, Hai Shu, Qiancheng Wang, Cong Tian, Linlin Wang, Shanhui Liao, Yifeng Zhang, Yanyan Cao, Lisha Xia, Haili Yang, Ting Zhang, Luoyan Ma, Shenwang Cao, Qiao Gao, Yichen Le, Mingli Shi, Quanxue Li, Yinmao Fan, Hang Zhou","doi":"10.1080/19420862.2025.2561823","DOIUrl":"10.1080/19420862.2025.2561823","url":null,"abstract":"<p><p>N-glycosylation, a critical quality attribute of monoclonal antibodies, plays a pivotal role in regulating pharmacokinetics and pharmacodynamics through high-mannose (Man5) glycoform modulation. While our previous work demonstrated that N-acetyl-D-mannosamine (ManNAc) supplementation effectively reduces Man5 levels without compromising antibody yield or other critical quality attributes, the mechanistic basis remained unclear. This study systematically investigates ManNAc's regulatory mechanism through a multi-parametric analysis. Cellular uptake studies revealed a 3-day latency period preceding Man5 reduction post-ManNAc administration. Subsequent transcriptional profiling showed no significant alterations in Man5-associated enzyme expression (Mgat1, Mgat2, Man2a1, SLC35A3), while metabolomic analysis demonstrated marked elevation of intracellular ManNAc, uridine-diphosphate-N-acetylglucosamine (UDP-GlcNAc), and cytidine-5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac) levels. Mechanistic studies revealed two critical findings: (1) Chinese hamster ovary cells exhibit minimal endogenous N-acetyl-D-glucosamine-2-epimerase expression, and (2) CMP-Neu5Ac exerts potent inhibition on glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase (GNE) activity <i>in vitro</i>, despite ManNAc's lack of transcriptional regulation on GNE. We propose a metabolic flux redirection model, where ManNAc-derived CMP-Neu5Ac accumulation inhibits GNE activity, thereby shunting UDP-GlcNAc from sialic acid biosynthesis toward N-glycosylation pathways to reduce Man5 levels. This work not only identifies UDP-GlcNAc substrate limitation as a key constraint in antibody glycosylation but also establishes exogenous monosaccharide supplementation as a novel metabolic engineering strategy for Man5 optimization. These findings provide critical mechanistic insights for precision glycoengineering of therapeutic antibodies.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2561823"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12452475/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145081184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"iBody-mediated tuning of synthetic cytokine receptor activation via rational nanobody interface engineering.","authors":"Richard Kunze, Fabian Navratil, Joana Beichert, Felix Geyer, Doreen M Floss, Harald Kolmar, Jürgen Scheller, Silke Pudewell","doi":"10.1080/19420862.2025.2563009","DOIUrl":"10.1080/19420862.2025.2563009","url":null,"abstract":"<p><p>Nanobodies are small, single-domain antibody fragments derived from heavy chain - only antibodies. They combine high binding affinity with advantages such as compact size, stability, solubility, and flexible epitope recognition, making them attractive tools in molecular biology and therapeutic applications. In this study, we engineered and optimized nanobodies for controlled activation of synthetic cytokine receptors, aiming to expand options for receptor customization. Specifically, we used nanobodies as extracellular domains of the gp130 receptor to induce dimerization upon antigen binding. To enable receptor activity, we introduced framework mutations that promote the formation of an i-shaped nanobody (iBody) dimer, adapted from i-shaped antibodies. These mutations enhanced dimerization and enabled low-level ligand-independent receptor activation. AlphaFold modeling identified the key amino acids responsible for forming the iBody interface. Additional modifications reduced intermolecular affinity, thereby minimizing background activation while preserving the structural features necessary for ligand-induced stimulation. This approach effectively broadened the receptor's activation range. Importantly, these framework mutations were not limited to the gp130-specific nanobody GP11 but were also functional in AIP3, an anti-idiotypic nanobody targeting palivizumab. Here, the modified nanobody fusion receptor could be activated by palivizumab, overcoming prior steric hindrance.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2563009"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12477867/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145138031","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sequence-based engineering of pH-sensitive antibodies for tumor targeting or endosomal recycling applications.","authors":"Wanlei Wei,Traian Sulea","doi":"10.1080/19420862.2024.2404064","DOIUrl":"https://doi.org/10.1080/19420862.2024.2404064","url":null,"abstract":"The engineering of pH-sensitive therapeutic antibodies, particularly for improving effectiveness and specificity in acidic solid-tumor microenvironments, has recently gained traction. While there is a justified need for pH-dependent immunotherapies, current engineering techniques are tedious and laborious, requiring repeated rounds of experiments under different pH conditions. Inexpensive computational techniques to predict the effectiveness of His pH-switches require antibody-antigen complex structures, but these are lacking in most cases. To circumvent these requirements, we introduce a sequence-based in silico method for predicting His mutations in the variable region of antibodies, which could lead to pH-biased antigen binding. This method, called Sequence-based Identification of pH-sensitive Antibody Binding (SIpHAB), was trained on 3D-structure-based calculations of 3,490 antibody-antigen complexes with solved experimental structures. SIpHAB was parametrized to enhance preferential binding either toward or against the acidic pH, for selective targeting of solid tumors or for antigen release in the endosome, respectively. Applications to nine antibody-antigen systems with previously reported binding preferences at different pHs demonstrated the utility and enrichment capabilities of this high-throughput computational tool. SIpHAB, which only requires knowledge of the antibody primary amino-acid sequence, could enable a more efficient triage of pH-sensitive antibody candidates than could be achieved conventionally. An online webserver for running SipHAB is available freely at https://mm.nrc-cnrc.gc.ca/software/siphab/runner/.","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"4 1","pages":"2404064"},"PeriodicalIF":5.3,"publicationDate":"2024-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142251356","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Systematic analysis of Fc mutations designed to reduce binding to Fc-gamma receptors","authors":"Geoff Hale, Jelle De Vos, Alastair Douglas Davy, Koen Sandra, Ian Wilkinson","doi":"10.1080/19420862.2024.2402701","DOIUrl":"https://doi.org/10.1080/19420862.2024.2402701","url":null,"abstract":"Elimination of the binding of immunoglobulin Fc to Fc gamma receptors is highly desirable for the avoidance of unwanted inflammatory responses to therapeutic antibodies and fusion proteins. Many di...","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"1 1","pages":"2402701"},"PeriodicalIF":5.3,"publicationDate":"2024-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142251297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}