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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

PubMedScientific reports2026-06-13

Antibody repertoire associated with clinically diverse presentations of pediatric SARS-CoV-2 infection.

Bruiners Natalie N, Ukey Rahul R, Konvinse Katherine C KC, Harris Marlayna M et al.

Pediatric SARS-CoV-2 infection can give rise to a range of clinical presentations, from asymptomatic or mild cases to severe pulmonary COVID-19, and to multisystem inflammatory syndrome in children (MIS-C). The latter is characterized by hyperinflammation and involvement of multiple organs. Although various aspects of antibody responses to pediatric SARS-CoV-2 infection have been reported, there has been limited research on the parallel antibody responses to both viral and self-antigens. We examined whether clinical phenotypes were linked to particular antiviral antibody and autoantibody profiles. By using custom arrays, we discovered that all manifestations of SARS-CoV-2 infection were linked to increased autoantibody production when compared to uninfected subjects, suggesting that pediatric SARS-CoV-2 infection may predispose to immune dysregulation. We observed subtle differences in autoantibody patterns among infection groups, with some autoantibodies being more associated with mild symptoms and others linked to severe disease manifestations. In particular, subsets of subjects with MIS-C and/or severe COVID-19 exhibited elevated autoreactive antibody responses against thyroperoxidase, IL-13, and IFN-epsilon, although differences across clinical groups did not reach statistical significance. When we compared subjects with MIS-C to those with severe COVID-19, we noted differences in the abundance of IgG (primarily IgG1), but no differences in Fc-mediated effector functions. Our study shows that the antibody repertoire in children varies with the clinical presentation of SARS-CoV-2. Moreover, MIS-C may be linked to abnormal antibody function, indicating that this syndrome-and potentially other post-acute sequelae of SARS-CoV-2 infection-could be related to antibody dysfunction.

PMID 42286032
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PubMedJournal of immunological methods2026-06-13

Performance evaluation of Meso Scale Discovery (MSD) quantitative serological assays for detection of binding (IgG, IgA, IgM) and ACE2 inhibitory antibody levels for SARS-CoV-2.

Cincotta Camila Macedo CM, Coleman Dante D, Padilla Steven S, Enoch Jennifer J et al.

A performance evaluation of a quantitative research use only (RUO) immunological assay utilizing the Meso Scale Discovery (MSD) platform for assessing IgM, IgA, and IgG binding and SARS-CoV-2 pseudo-neutralization was performed. Comparative analyses of antibody quantification of IgA, IgG, and IgM isotypes against SARS-CoV-2 nucleocapsid, spike, Receptor Binding Domain (RBD) and N-Terminal Domain (NTD) antigens were performed using MSD multi-spot electro-chemiluminescent V-PLEX COVID-19 test kits, and two well characterized serological panels. Cross reactivity was assessed against COVID-19 negative/Influenza samples. Precision was assessed by comparing variation between duplicate values within run; accuracy was assessed by comparing values obtained across runs against expected values. The MSD IgG, IgA, and IgM binding, and ACE2 inhibitory antibody assays demonstrated acceptable precision and accuracy within the expected 20%/30% variability, respectively per manufacturer's protocol; no cross reactivity with influenza samples was observed. Different MSD plate configurations, multiple (two) MSD analysis instruments, and multiple operators did not impact antibody quantification; thus, confirming the robustness of both assays. Comparative analysis between MSD and commercial Euroimmun, Siemens ADVIA, and Beckman Coulter DXLTM ACCESS assays demonstrated better performance overall for the MSD assay. IMPORTANCE: This work describes and validates the MSD platform, as a highly flexible, customizable, operator independent, and reliable platform for antibody assessment of COVID-19 response which is highly adaptable to immune assessment of emerging or re-emerging pathogens.

PMID 42285427
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PubMedNature communications2026-06-13

Efficacy of Pam3CSK4 as a cross-species adjuvant for polysaccharide vaccines in humanized mouse and non-human primate models.

Jennings-Gee Jamie E JE, Adams-Sims Alexis E AE, Haas Karen M KM

Polysaccharide-based vaccines are essential for preventing bacterial infections, but their effectiveness is limited by weak antibody responses and lack of suitable adjuvants. TLR4 agonists enhance polysaccharide-specific antibody responses through B cell-intrinsic TLR4-MyD88 signaling in mice, but this mechanism is not conserved in primates, prompting the search for alternative MyD88-activating agonists. In vitro, the TLR1/2 agonist Pam3CSK4 synergizes with strong BCR crosslinking to enhance activation and antibody secretion by mouse and human B cells. In vivo, Pam3CSK4 in squalene emulsion increases protective pneumococcal polysaccharide-specific antibody responses in both immunocompetent and humanized mice. Although a dual TLR2/7 agonist shows strong in vitro activity, it fails to enhance polysaccharide-specific IgG responses in vivo, consistent with antagonism observed when Pam3CSK4 and TLR7 agonists are combined. In contrast, incorporating Pam3CSK4 into an adjuvant containing a TLR4 agonist, synthetic cord factor, and squalene emulsion further enhances memory B cell generation and protective antibody responses in mice and restores adjuvant activity in non-human primates, supporting Pam3CSK4-based formulations as promising adjuvants for polysaccharide vaccines.

PMID 42285953
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PubMedBlood advances2026-06-13

Delayed ADAMTS13 normalisation in caplacizumab/PEX treated patients associated with anti-ADAMTS13 IgG antibody boosting.

Prasannan Nithya N, Latif Arshia A, Westwood John-Paul JP, Thomas Mari Rebeca MR et al.

Delayed ADAMTS13 normalisation was previously reported in a subgroup of caplacizumab/PEX-treated patients. To further explain this finding, we analysed anti-ADAMTS13 IgG antibody levels at multiple time points during the acute TTP episode in 59 caplacizumab/PEX and 50 non-caplacizumab/PEX cases. Caplacizumab/PEX cases required fewer PEX, taking longer to achieve ADAMTS13 activity >20% than non-caplacizumab/PEX cases (median 33 days vs 17.5 days, p<0.0001). More caplacizumab/PEX cases increased anti-ADAMTS13 IgG antibody after stopping PEX (40% vs 25.5% in non-caplacizumab/PEX cases, p=0.14). Cases requiring more than thirty days of caplacizumab had a higher presenting anti-ADAMTS13 IgG antibody compared to less than 30 days (63.5% vs 25%, p=0.02). 50% of cases requiring more than 30 days of caplacizumab, increased anti-ADAMTS13 IgG antibody post PEX, with median 101 days to ADAMTS13 activity >20%, compared to 28 days (p<0.0001) in patients without an antibody increase. Fifty-four percent of all caplacizumab cases had presenting anti-ADAMTS13 IgG antibody >40% and 47% had an increased antibody post PEX, taking longer to achieve an ADAMTS13 activity >20%. 33% with presenting anti-ADAMTS13 IgG antibody <40% increased their antibody following PEX, taking 97.5 days to achieve ADAMTS13 activity >20%. Cases with presenting anti-ADAMTS13 antibody <40% and no increase in antibody post PEX took a median of 14 days (p=0.0005). Therefore, delayed normalisation of ADAMTS13 activity in a subgroup of caplacizumab/PEX cases was associated with antibody boosting, more common with a higher presenting anti-ADAMTS13 IgG antibody and subsequently, longer caplacizumab use. These findings were subsequently confirmed in 93 cases receiving caplacizumab/PEX over 3 years.

PMID 42284700
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PubMedBiomedicine & pharmacotherapy = Biomedecine & pharmacotherapie2026-06-13

SU056 potentiates SULF2 antibody in suppressing cholangiocarcinoma metastasis via SULF2-YBX1-CXCR4 signaling axis.

Han Mengzhen M, Pan Yonglong Y, Li Xinxin X, Huang Qibo Q et al.

Intrahepatic cholangiocarcinoma (iCCA), the second most common subtype of primary liver cancer around the world, is an aggressive neoplasm with high metastastic potential, which leads to a low rate of curative resections and dismal prognosis. In previous studies, Sulfatase 2 (SULF2) has been reported to regulate various important oncogenic signaling pathways and promote iCCA progression. Further research is needed to explore the role of SULF2 in iCCA metastasis. In this study, we verified the overexpression of SULF2 in iCCA tissues and its positive correlation with advanced stage and poor prognosis. Trans-well migration and invasion assay and mouse models explored the impact of SULF2 on iCCA metastasis in vitro and in vivo. We also demonstrated that SULF2 facilitated iCCA metastasis through upregulating CXCR4 transcription mediated by the transcription factor YBX1. Moreover, SULF2 could recruit USP7 to interact with YBX1 and inhibit Lys48-polyubiquitination of YBX1, stabilizing YBX1 and promoting a functional YBX1/CXCR4 axis. Combining SULF2 monoclonal antibody with SU056 had a synergistic effect in suppressing iCCA progression and metastasis of mouse models. In conclusion, SULF2 promotes iCCA progression and metastasis through an intracellular SULF2-YBX1-CXCR4 axis, and SULF2 monoclonal antibody combined with YBX1 inhibitor SU056 may be a potentially promising treatment strategy for iCCA.

PMID 42284889
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PubMedThe Journal of biological chemistry2026-06-13

Structure of a MenB de-N-acetyl polysialic acid antibody and mechanism of immune cell inhibition.

Moe Gregory R GR, Agirre Jon J, Beernink Peter T PT

The Neisseria meningitidis serogroup B (MenB) polysaccharide, α(2-8) polysialic acid (polySia), is essential for resistance to complement-mediated bacteriolysis and inhibition of opsonophagocytosis. The monoclonal antibody SEAM 3 binds de-N-acetyl polySia (dPSA) but not polySia, yet still recognizes encapsulated MenB, indicating the capsule contains dPSA derivatives. Since SEAM 3 also recognizes other pathogens as well as human cancers, we have explored its biological role and mapped the SEAM 3 epitope. We compared binding of N-acetylated and de-N-acetylated polySia and ganglioside GD3 derivatives to Siglecs (sialic-acid-binding immunoglobulin-like lectins) on leukocytes. Siglec-9 showed higher affinity for dPSA and dGD3 (KD ∼2.6-3.1 nM) than for their acetylated counterparts, while Siglec-5 bound polySia and GD3 derivatives with similar and moderate (KD∼40-60nM and 7.9nM, respectively) affinity. Siglecs-2, -3, -7, -10, and -11 showed negligible binding. T cells, NK cells, and monocytes incubated with live dPSA-expressing MenB acquired dPSA and bacterial protein. A lipophilic dPSA derivative also suppressed endotoxin-induced secretion of IL-1β, IL-6, and TNFα from human PBMC. To map the SEAM 3 epitope, we co-crystallized a humanized SEAM 3 Fab with a dPSA derivative, resolving the structure at 1.83 Å (Rfree = 0.230) with good geometry. The epitope comprises four residues, with a de-N-acetylated residue at the non-reducing end. These findings suggest that dPSA may help mediate MenB immune evasion by engaging the inhibitory Siglec receptors 5 and 9 and confirm the utility of SEAM 3 as a structural probe of dPSA biology and the role of Siglecs in MenB pathogenesis.

PMID 42285517
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