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snake venom antibody-2 (ViperaTAb)

✓ Approved

MicroPharm · 多克隆抗体 · 多克隆抗体

什么是 snake venom antibody-2?

snake venom antibody-2 是一种多克隆抗体,由MicroPharm研发。该药已获批,用于治疗相关适应症,给药途径:Injectable (Others)、Intravenous (IV)。

药物档案

商品名ViperaTAb
公司MicroPharm
药物类别多克隆抗体, 抗体
给药途径Injectable (Others), Intravenous (IV)
状态Approved

治疗适应症

snake venom antibody-2 针对 1 个适应症,涉及 1 个治疗领域。

治疗领域疾病/病症分期
Injury, poisoning and procedural complicationsVenom poisoning✓ Approved

相关研究文献

PubMedBMC biology2026-10-26

A developmental shift in venom toxin expression underpins a major prey switch in Australian brown snakes.

van Thiel Jory J, Smith Cara F CF, Kazandjian Taline D TD, Patel Rohit N RN et al.

Many animals change traits over the course of their life history. It has been proposed that some of these developmental changes evolve in concert with shifts in ecology, but there are relatively few clear examples, and identifying the underlying molecular changes is challenging. Australian brown snakes (Pseudonaja spp.), one of Australia's most venomous snakes, may provide such an example, as previous work has shown that these species undergo a dietary shift from reptiles to mammals, accompanied by differences in venom activity. We show that the venom composition of adult brown snakes is distinguished by the collective expression of four procoagulant toxin families, which are absent in juvenile life stages, where venom composition is instead dominated by neurotoxins. The developmental onset of expression across all four procoagulant toxins correlates with a functional shift in venom activity to one that disrupts the blood-clotting system of mammalian prey. We further show that this developmental timing in both toxin expression and procoagulant venom activity coincides with a broader ecological transition in which Australian brown snakes begin to prey on mammals. In contrast, we found that the smallest brown snake species, a lizard specialist throughout its lifetime, only expresses neurotoxins and shows no comparable developmental shift in either procoagulant toxin expression or procoagulant activity. Our findings suggest that a coordinated shift in the expression of four procoagulant toxin gene families transitions the venom from a neurotoxic phenotype in lizard-feeding juveniles to a potent procoagulant phenotype in mammal-feeding adults. These results provide a clear example of how the concerted upregulation of multiple genes can drive a functional shift in a key ecological trait, linking changes in toxin gene expression to venom activity and, ultimately, to prey-capture strategy.

PMID 42928320
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PubMedBiotech (Basel (Switzerland))2026-10-26

Cell-Based Assay Development and Standardization for Antibody-Drug Conjugates.

Sun Dengyun D, Hsu Amy A, Long Hu H, Qin Ke K et al.

ADC-111 is an Antigen-1-targeting antibody-drug conjugate with approximately eight payloads conjugated to one monoclonal antibody. The primary mechanism of action of ADC-111 is payload-induced cytotoxicity after antigen-antibody binding-mediated internalization. A cell-based assay using T24 cells engineered with Antigen-1 expression was developed and phase-appropriately validated to measure the potency of ADC-111 drug substance and drug product. This specific and stability-indicating assay detected potency loss resulting from degradation in the complementarity-determining region of the antibody, and correlated closely with the results from the Antigen-1 binding enzyme-linked immunosorbent assay, demonstrating that the ADC-111 cell-based assay is antigen-binding dependent. The potency measured by the cell-based assay also showed good correlation with varying drug-antibody ratio values, but ELISA did not. Notably, the ready-to-use format of the cell-based assay had performance comparable to that of the continuous culture using the same procedure, allowing both formats to be used interchangeably. In addition, the same parental cell line T24 was engineered with other tumor antigens, and the corresponding cell-based assay also showed good specificity, demonstrating the proof-of-concept of using a single parental cell line for multiple ADCs to standardize and accelerate cell-based assay development.

PMID 42930073
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PubMedCurrent oncology (Toronto, Ont.)2026-10-26

Translational Challenges and Strategies for Antibody Therapeutics in Glioblastoma.

Zhou Yangyi Y, Li You Y, Chen Yu Y, Zhao Peiqi P et al.

Glioblastoma (GBM) remains difficult to control. Monoclonal antibodies (mAbs) have transformed the treatment of several extracranial cancers, but they have not consistently improved survival in GBM. This narrative review examines the main biological and translational barriers to antibody-based therapy. It also evaluates strategies to overcome them. We reviewed preclinical, translational, and clinical evidence on antibody delivery, target stability, the tumor microenvironment, target discovery, and emerging antibody formats. Heterogeneous blood-brain and blood-tumor barriers produce uneven intratumoral exposure, especially at infiltrative margins. Spatial and temporal heterogeneity promotes antigen loss and treatment escape. Lymphocyte dysfunction, myeloid dominance, and suppressive vascular and metabolic programs further limit immune activity. Receptor-mediated transcytosis and focused ultrasound may improve delivery. Single-cell and spatial profiling, surfaceome and endocytome proteomics, longitudinal sampling, and causal inference may improve target selection. Depending on their design, antibody-drug conjugates (ADCs) can deliver cytotoxic payloads, whereas bispecific constructs can enable immune redirection, dual-target recognition, or receptor-mediated transport. However, clinical benefit remains limited by construct design, target accessibility, regional exposure, toxicity, and inadequate biomarker selection. Successful translation requires modality-specific alignment of exposure at the relevant site of action, target requirements, immune dependence, molecular design, and safety. Biomarker-guided patient selection, spatial pharmacokinetic and pharmacodynamic validation, and early evidence of clinical benefit are also essential.

PMID 42930186
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PubMedNature communications2026-10-26

Reoviridae-derived short trimerization domain for stabilizing homo-trimerization of vaccine immunogens and therapeutic proteins.

Wei Min M, Bu Qingfang Q, Xiao Jin J, Yuan Lunzhi L et al.

Trimerization motifs play pivotal roles in structural biology and therapeutic protein engineering. Here, we describe a short trimerization motif (rFd1303) derived from the Reoviridae family reovirus σ1 protein. Compared with the widely used T4-Foldon, the rFd1303 increased recombinant protein yields. The rFd1303-fused immunogens of SARS-CoV-2 spike and influenza hemagglutinin elicited antibody responses comparable to T4-Foldon-fused controls in mice. Using this tag, we engineered a trimeric ACE2-Ig fusion protein (TriACE2-Ig) that remained stable after 30 days at room temperature and neutralized a broad range of ACE2-utilizing sarbecoviruses, including 19 SARS-CoV-2 variants, SARS-CoV, and pangolin coronaviruses GD and GX, with higher potency than monomeric ACE2-Ig. In the hamster model challenged with various SARS-CoV-2 variants, our data demonstrated that intranasal TriACE2-Ig administration markedly reduced viral loads, virus-induced body-weight loss, lung pathology, and decreased within-cage virus transmission. These findings highlight rFd1303 as a versatile trimerization platform for vaccine and therapeutic protein development.

PMID 42928093
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PubMedJournal of biological engineering2026-10-26

A stealth-body Fc engineering platform enables complete effector silencing in antibody and ADC therapeutics.

Kim Suyeon S, Jo Migyeong M, Kyung Munsu M, Ko Woo Hyung WH et al.

The development of next-generation antibody therapeutics requires Fc scaffolds that suppress unwanted effector functions while preserving core developability attributes. Existing effector-attenuated Fc backbones, however, retain residual interactions with Fcγ receptors (FcγRs) and C1q, highlighting a persistent design limitation in achieving complete effector silencing without compromising glycosylation, FcRn-mediated persistence, and manufacturability. This is particularly relevant for formats in which Fc effector function is undesirable, including immune-engaging antibodies, CD47 blockers, and antibody-drug conjugates (ADCs). Accordingly, a robust Fc engineering framework enabling complete and transferable effector silencing across antibody modalities is required. We developed Stealth-Body (SB) Fc variants, a fully effector-silenced Fc platform that abolishes Fc-mediated immune engagement while maintaining native-like glycosylation, pharmacokinetics, and manufacturability. Using a CHO cell display system with directed evolution guided by cross-species sequence features from goat IgG, we identified human glycosylated IgG1 variants (SB1, SB5, SB6) that abrogated binding to all human FcγRs and C1q, and to all murine and cynomolgus FcγRs. SB Fc retained pH-dependent FcRn binding, antigen recognition, thermostability, and expression, with in vivo persistence comparable to wild-type IgG1. Incorporation of SB Fc into trastuzumab, rituximab, and ADCs abolished ADCC, ADCP, and CDC, while integration into a CD47-targeting IgG-CD40L fusion protein mitigated hematologic toxicity without impairing immune activation. Collectively, SB Fc variants represent a generalizable, effector-null Fc scaffold that enables complete and transferable silencing of Fc-mediated immune functions while preserving key developability attributes. This platform expands the therapeutic window of antibody therapeutics through precise control of Fc activity across diverse modalities.

PMID 42928316
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PubMedMicrobiology spectrum2026-10-26

Functional and protective capacity of a human monoclonal antibody against Shigella sonnei O-Antigen produced in fungal cells.

Vezzani Giacomo G, Mäkinen Mari M, Boero Elena E, Nannini Francesco F et al.

The number of bacterial species acquiring antimicrobial resistance to the most widely used antibiotics is steadily increasing. Monoclonal antibodies (mAbs) are among the most promising therapeutic options to tackle antimicrobial resistance. A major hurdle that prevents broader applicability of mAb therapy is represented by high production costs. Here, we describe the manufacturing of a human mAb targeting the O-Antigen of Shigella sonnei by a fungal production platform (Thermothelomyces heterothallica C1, formerly Myceliophthora thermophila). The antibody, produced with either native fungal or humanized glycosylation, had functional activity in vitro and protective efficacy in vivo comparable to the antibody generated in standard mammalian cells. The use of the C1 platform reduces production time and accelerates release, thus significantly lowering production costs. This approach can favor equitable access to novel therapeutics that can counteract global health challenges. This study demonstrates that a fungal production platform can produce a human monoclonal antibody (mAb) targeting the O‑antigen of Shigella sonnei with equivalent functional activity and protective effects to antibodies made in mammalian cells. The use of the C1 platform reduces production time and accelerates release, thus significantly lowering production costs. This approach can favor equitable access to novel therapeutics and support global efforts to control antimicrobial resistance.

PMID 42929515
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