mAbs最新文献 - Book学术

T cell margination: investigating the detour of T cells following forimtamig treatment in humanized mice.

IF 5.6 2区医学

mAbs Pub Date : 2025-12-01 Epub Date: 2024-12-16 DOI: 10.1080/19420862.2024.2440578

Nils O'Brien, Joerg P J Mueller, Ann-Marie E Bröske, Jan Attig, Franz Osl, Cylia Crisand, Ann-Katrin Wolf, Richard Rae, Stefanie Lechner, Thomas Pöschinger, Christian Klein, Pablo Umaña, Sara Colombetti, Andreas Beilhack, Jan Eckmann

{"title":"T cell margination: investigating the detour of T cells following forimtamig treatment in humanized mice.","authors":"Nils O'Brien, Joerg P J Mueller, Ann-Marie E Bröske, Jan Attig, Franz Osl, Cylia Crisand, Ann-Katrin Wolf, Richard Rae, Stefanie Lechner, Thomas Pöschinger, Christian Klein, Pablo Umaña, Sara Colombetti, Andreas Beilhack, Jan Eckmann","doi":"10.1080/19420862.2024.2440578","DOIUrl":"https://doi.org/10.1080/19420862.2024.2440578","url":null,"abstract":"T cell bispecific antibodies (TCBs) are a promising new class of therapeutics for relapsed/refractory multiple myeloma. A frequently observed, yet incompletely understood effect of this treatment is the transient reduction of circulating T cell counts, also known as T cell margination (TCM). After administration of the GPRC5D-targeting TCB forimtamig (RG6234), TCM occurred in patients and correlated with cytokine release and soluble B cell maturation antigen decrease. We demonstrate that TCM is accurately represented in the humanized NSG mouse model and occurs at a lower threshold of target expression than systemic cytokine release. Application of whole-mouse tissue clearing and 3D imaging revealed that T cells accumulate in the bone marrow after treatment. We hypothesize that low amounts of targets are sufficient to rapidly redirect T cells upon TCB engagement. Therefore, we propose TCM as a beneficial, highly sensitive and early effect of forimtamig that leads T cells to likely sites of bone marrow tumor lesions.","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2440578"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142837183","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}

引用次数: 0

Analysis of how antigen mutations disrupt antibody binding interactions toward enabling rapid and reliable antibody repurposing. 分析抗原突变如何破坏抗体结合相互作用，以实现快速可靠的抗体再利用。

IF 5.6 2区医学

mAbs Pub Date : 2025-12-01 Epub Date: 2024-12-17 DOI: 10.1080/19420862.2024.2440586

Sumaiya Islam, Varun M Chauhan, Robert J Pantazes

{"title":"Analysis of how antigen mutations disrupt antibody binding interactions toward enabling rapid and reliable antibody repurposing.","authors":"Sumaiya Islam, Varun M Chauhan, Robert J Pantazes","doi":"10.1080/19420862.2024.2440586","DOIUrl":"https://doi.org/10.1080/19420862.2024.2440586","url":null,"abstract":"Antibody repurposing is the process of changing a known antibody so that it binds to a mutated antigen. One of the findings to emerge from the Coronavirus Disease 2019 (COVID-19) pandemic was that it was possible to repurpose neutralizing antibodies for Severe Acute Respiratory Syndrome, a related disease, to work for COVID-19. Thus, antibody repurposing is a possible pathway to prepare for and respond to future pandemics, as well as personalizing cancer therapies. For antibodies to be successfully repurposed, it is necessary to know both how antigen mutations disrupt their binding and how they should be mutated to recover binding, with this work describing an analysis to address the first of these topics. Every possible antigen point mutation in the interface of 246 antibody-protein complexes were analyzed using the Rosetta molecular mechanics force field. The results highlight a number of features of how antigen mutations affect antibody binding, including the effects of mutating critical hotspot residues versus other positions, how many mutations are necessary to be likely to disrupt binding, the prevalence of indirect effects of mutations on binding, and the relative importance of changing attractive versus repulsive energies. These data are expected to be useful in guiding future antibody repurposing experiments.","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2440586"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142847028","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}

引用次数: 0

Sequence-based engineering of pH-sensitive antibodies for tumor targeting or endosomal recycling applications. 基于序列的 pH 值敏感抗体工程，用于肿瘤靶向或内体循环。

IF 5.3 2区医学

mAbs Pub Date : 2024-09-17 DOI: 10.1080/19420862.2024.2404064

Wanlei Wei,Traian Sulea

{"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}

引用次数: 0

Systematic analysis of Fc mutations designed to reduce binding to Fc-gamma receptors 对旨在减少与 Fc-gamma 受体结合的 Fc 突变的系统分析

IF 5.3 2区医学

mAbs Pub Date : 2024-09-15 DOI: 10.1080/19420862.2024.2402701

Geoff Hale, Jelle De Vos, Alastair Douglas Davy, Koen Sandra, Ian Wilkinson

引用次数: 0

Navigating large-volume subcutaneous injections of biopharmaceuticals: a systematic review of clinical pipelines and approved products 探索生物制药的大容量皮下注射：临床管线和已批准产品的系统回顾

IF 5.3 2区医学

mAbs Pub Date : 2024-09-15 DOI: 10.1080/19420862.2024.2402713

Philip Green, Andreas Schneider, Jakob Lange

引用次数: 0

Antibody association in solution: cluster distributions and mechanisms 溶液中的抗体关联：集群分布与机制

IF 5.3 2区医学

mAbs Pub Date : 2024-04-26 DOI: 10.1080/19420862.2024.2339582

Sandi Brudar, Leonid Breydo, Elisha Chung, Ken A. Dill, Nasim Ehterami, Ketan Phadnis, Samir Senapati, Mohammed Shameem, Xiaolin Tang, Muhammmad Tayyab, Barbara Hribar-Lee

引用次数: 0

Reducing neonatal Fc receptor binding enhances clearance and brain-to-blood ratio of TfR-delivered bispecific amyloid-β antibody 减少新生儿Fc受体结合可提高TfR递送的双特异性淀粉样蛋白-β抗体的清除率和脑血比

IF 5.3 2区医学

mAbs Pub Date : 2024-04-18 DOI: 10.1080/19420862.2024.2339337

Eva Schlein, Ken G. Andersson, Tiffany Dallas, Stina Syvänen, Dag Sehlin

引用次数: 0

Can antibodies be “vegan”? A guide through the maze of today’s antibody generation methods 抗体可以 "素食 "吗？穿越当今抗体生成方法迷宫的指南

IF 5.3 2区医学

mAbs Pub Date : 2024-04-18 DOI: 10.1080/19420862.2024.2343499

Stefan Dübel

引用次数: 0

Enrichment strategy and initial characterization of heterodimers enriched from a co-formulated cocktail of therapeutic antibodies against SARS-COV-2 从共同配制的抗SARS-COV-2治疗性抗体鸡尾酒中富集的异源二聚体的富集策略和初步特征描述

IF 5.3 2区医学

mAbs Pub Date : 2024-04-09 DOI: 10.1080/19420862.2024.2338301

Sophia Liu, Yuetian Yan, Cody M. Secor, Zachary R. Oberholtzer, Donna J. Skow, Mushhood Sheikh, Youmi Moon, Yue Fu, Cristinel Sandu, Shunhai Wang, Ning Li, Jennifer B. Nguyen, Michael P. Rosconi, Erica A. Pyles

引用次数: 0

Application of quantitative protein mass spectrometric data in the early predictive analysis of membrane-bound target engagement by monoclonal antibodies 定量蛋白质质谱数据在单克隆抗体膜结合目标参与早期预测分析中的应用

IF 5.3 2区医学

mAbs Pub Date : 2024-03-04 DOI: 10.1080/19420862.2024.2324485

Armin Sepp, Morris Muliaditan

引用次数: 0