Identification of a novel protective human monoclonal antibody, LXY8, that targets the key neutralizing epitopes of staphylococcal enterotoxin B

Hu, Naijing; Qiao, Chun‐Feng; Wang, Jing; Wang, Zhihong; Li, Xinying; Zhou, Liuzhong; Wu, Jiaguo; Zhang, Dingmu; Feng, Jie; Shen, Beifen; Zhang, Jinghai; Luo, Longlong

doi:10.1016/j.bbrc.2021.02.057

Cited by 13 publications

(6 citation statements)

References 18 publications

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“…Despite this, S008 showed better therapeutic protection than 10D8. Compared with another neutralizing anti-SEB antibody reported previously (26), S008 had a longer therapeutic window for efficient treatment, suggesting ample time to acquire S008 after exposure. It was also suggested a longer therapeutic window period than the reported data of the chimeric antibodies, e.g.…”

Section: Discussionmentioning

confidence: 78%

A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

Peng

Shi

et al. 2022

Front. Immunol.

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Abrin, a type-II ribosome inactivating protein from the seed of Abrus precatorius, is classified as a Category B bioterrorism warfare agent. Due to its high toxicity, ingestion by animals or humans will lead to death from multiple organ failure. Currently, no effective agents have been reported to treat abrin poisoning. In this study, a novel anti-abrin neutralizing antibody (S008) was humanized using computer-aided design, which possessed lower immunogenicity. Similar to the parent antibody, a mouse anti-abrin monoclonal antibody, S008 possessed high affinity and showed a protective effect against abrin both in vitro and in vivo, and protected mice that S008 was administered 6 hours after abrin. S008 was found that it did not inhibit entry of abrin into cells, suggesting an intracellular blockade capacity against the toxin. In conclusion, this work demonstrates that S008 is a high affinity anti-abrin antibody with both a neutralizing and protective effect and may be an excellent candidate for clinical treatment of abrin poisoning.

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Section: Discussionmentioning

confidence: 78%

A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

Peng

Shi

et al. 2022

Front. Immunol.

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“…In order to determine the protective efficacy of Hm0487 against SEB, we next employed the D-galactosamine-sensitized mouse, which is a widely accepted model, 16 , 18 , 25 , 26 to test the protective efficacy of Hm0487 in vivo . As shown in Figure 5a , all mice in PBS group ( n = 8) died within 24 h after being challenged with 10 μg of SEB, underscoring the lethal effect of SEB.…”

Section: Resultsmentioning

confidence: 99%

A highly neutralizing human monoclonal antibody targeting a novel linear epitope on staphylococcal enterotoxin B

Fan,

Zhao,

Wang

et al. 2024

Human Vaccines & Immunotherapeutics

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“…To date, there is no licensed treatment or vaccine for Marburg infection, although a panel of antibodies with the potentials of neutralization has been isolated from a survivor subjected to MARV infection ( Flyak et al, 2015 ). Herein, we utilized phage display technology to screen an antibody in a well-established antibody library ( Hu et al, 2021 ; Wang et al, 2022 ) and obtained a novel human antibody with prominent neutralizing activity. Furthermore, NPC2 fusion at the N terminus of the light chain of this antibody potentiates broad-spectrum inhibition of cell entry of filovirus species and mutants.…”

Section: Introductionmentioning

confidence: 99%

A novel MARV glycoprotein-specific antibody with potentials of broad-spectrum neutralization to filovirus

Zhang,

et al. 2024

eLife

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Marburg virus (MARV) is one of the filovirus species that causes a deadly hemorrhagic fever in humans, with mortality rates up to 90%. Neutralizing antibodies represent ideal candidates to prevent or treat virus disease. However, no antibody has been approved for MARV treatment to date. In this study, we identified a novel human antibody named AF-03 that targeted MARV glycoprotein (GP). AF-03 possessed a high binding affinity to MARV GP and showed neutralizing and protective activities against the pseudotyped MARV in vitro and in vivo. Epitope identification, including molecular docking and experiment-based analysis of mutated species, revealed that AF-03 recognized the Niemann-Pick C1 (NPC1) binding domain within GP1. Interestingly, we found the neutralizing activity of AF-03 to pseudotyped Ebola viruses (EBOV, SUDV, and BDBV) harboring cleaved GP instead of full-length GP. Furthermore, NPC2-fused AF-03 exhibited neutralizing activity to several filovirus species and EBOV mutants via binding to CI-MPR. In conclusion, this work demonstrates that AF-03 represents a promising therapeutic cargo for filovirus-caused disease.

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Identification of a novel protective human monoclonal antibody, LXY8, that targets the key neutralizing epitopes of staphylococcal enterotoxin B

Cited by 13 publications

References 18 publications

A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

A highly neutralizing human monoclonal antibody targeting a novel linear epitope on staphylococcal enterotoxin B

A novel MARV glycoprotein-specific antibody with potentials of broad-spectrum neutralization to filovirus

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