Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-tetrodotoxin humanized antibody and use thereof. The humanized antibody has a heavy-chain variable region and a light-chain variable region with amino acid sequences shown in SEQ ID NO: 1 to SEQ ID NO: 2, respectively. Affinity analysis shows that the antibody of the present disclosure has prominent affinity. It is proved by experiments that, after mice in an antibody protection group pre-injected with the antibody of the present disclosure are injected with tetrodotoxin, most of the mice show no toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the antibody of the present disclosure shows excellent anti-tetrodotoxin effects, excellent preventive or therapeutic effects on puffer fish-related biological injuries, and promising clinical application prospects.

Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-tetrodotoxin humanized antibody and use thereof. The humanized antibody has a heavy-chain variable region and a light-chain variable region with amino acid sequences shown in SEQ ID NO: 1 to SEQ ID NO: 2, respectively. Affinity analysis shows that the antibody of the present disclosure has prominent affinity. It is proved by experiments that, after mice in an antibody protection group pre-injected with the antibody of the present disclosure are injected with tetrodotoxin, no mice shows toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the antibody of the present disclosure shows excellent anti-tetrodotoxin effects, excellent preventive or therapeutic effects on puffer fish-related biological injuries, and promising clinical application prospects.

Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-tetrodotoxin humanized antibody Y126C and use thereof. The humanized antibody has a heavy-chain variable region and a light-chain variable region with amino acid sequences shown in SEQ ID NO: 1 to SEQ ID NO: 2, respectively. Affinity analysis shows that the antibody of the present disclosure has prominent affinity. It is proved by experiments that, after mice in an antibody protection group pre-injected with the antibody of the present disclosure are injected with tetrodotoxin, most of mice do not show toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the antibody of the present disclosure shows excellent anti-tetrodotoxin effects, excellent preventive or therapeutic effects on puffer fish-related biological injuries, and promising clinical application prospects.

Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-physaliatoxin nanobody, and a preparation method and use thereof. The nanobody is a VHH antibody with an amino acid sequence shown in SEQ ID NO. 1. Affinity analysis shows that the nanobody of the present disclosure has prominent affinity. It is proved by small animal experiments that, after mice in an antibody protection group pre-injected with the nanobody of the present disclosure are injected with physaliatoxin, no mice shows toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the nanobody of the present disclosure shows excellent anti-physaliatoxin effects, excellent preventive or therapeutic effects on jellyfish stings, and promising clinical application prospects.