Intramuscular administration of antivenoms in experimental envenomation by Bothrops asper: comparison between Fab and IgG.

Toxicon

Instituto Clodomiro Picado, Facultad de Microbiologi;a, Universidad de Costa Rica, San José, Costa Rica.

Published: February 2003

AI Article Synopsis

  • The study examined the effectiveness of intramuscular administration of sheep Fab and IgG antivenoms in mice envenomated by Bothrops asper, focusing on the absorption speed of Fab for improved venom neutralization.
  • Neither antivenom was successful in preventing death or extending survival time in mice when given immediately after envenomation, despite being effective against certain venom effects like defibrination.
  • While both antivenoms showed partial effectiveness in reducing local tissue damage when administered at the venom injection site, no significant differences were observed between Fab and IgG, undermining the idea that Fab could be a better option for treating B. asper bites.

Article Abstract

The efficacy of intramuscular (im) administration of sheep Fab and IgG antivenoms was assessed in a mouse experimental model of envenomation by Bothrops asper, in order to test if the more rapid absorption of Fab improves neutralization. Both antivenoms were adjusted to have a similar neutralizing potency in assays involving preincubation of venom and antivenom. Neither antivenom was effective in neutralizing lethality, nor in prolonging the time of death, in mice injected with either 3, 2 or 1.5 LD(50)s of venom by the intraperitoneal (ip) route, in experiments in which antivenoms were administered im immediately after envenomation. Antivenoms were effective in the neutralization of defibrinating activity, even if treatment was performed 30 min after envenomation, with no differences between IgG and Fab. Regarding neutralization of local effects, i.e. myonecrosis and hemorrhage, im administration of antivenoms at a site distant from the venom-injection site was completely ineffective in reducing the extent of local tissue damage. However, partial neutralization of these effects was achieved if antivenoms were administered im at the same site of venom injection, provided treatment was performed immediately after envenomation. Fab antivenom was slightly more effective than IgG antivenom in the neutralization of myotoxicity under these conditions, although a similar efficacy was observed between these antivenoms regarding neutralization of hemorrhagic effect. Our observations do not evidence major differences in the neutralizing ability of Fab and IgG antivenoms when applied by the im route, and do not support the hypothesis that im administration of Fab antivenoms constitutes an effective alternative to treat B. asper envenomations.

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0041-0101(02)00283-0DOI Listing

Publication Analysis

Top Keywords

fab igg
12
antivenoms
10
intramuscular administration
8
administration antivenoms
8
envenomation bothrops
8
bothrops asper
8
igg antivenoms
8
antivenom effective
8
antivenoms administered
8
treatment performed
8

Similar Publications

Half-Life Extension of the IgG-Degrading Enzyme (IdeS) Using Fc-Fusion Technology.

Eur J Immunol

December 2024

Institut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, CNRS, Sorbonne Université, Université Paris Cité, Paris, France.

Imlifidase (IdeS) is a bacterial protease that hydrolyzes human IgG in their hinge region, decreasing their half-life and abrogating their Fc-mediated properties. It is now successfully used in therapy to prevent graft rejection during kidney transplants and is being clinically evaluated in several IgG-mediated autoimmune diseases. IdeS short half-life however limits its clinical use, particularly in the case of chronic diseases that would request repeated administrations.

View Article and Find Full Text PDF
Article Synopsis
  • CMV reactivation is a significant health issue for patients who have undergone stem cell or organ transplants, leading to increased risks of illness and death.
  • Three CMV-specific Fab-antibodies (A6, C1, C7) have been developed to bind to particular MHC molecules, showing effectiveness in targeting and destroying CMV-infected cells, especially when used in combination with natural killer (NK) cells.
  • The TCR-like antibodies also demonstrated the ability to activate neutrophils to kill target cells, offering a promising treatment option for patients experiencing or at risk of CMV reactivation, with a broader potential patient application than previous methods.
View Article and Find Full Text PDF

Radioimmunotherapy (RIT) with α-particle-emitting, Ac complexed to trastuzumab may offer an alternative treatment for patients who progress on HER2-targeted therapies. Moreover, RIT with [Ac]Ac-DOTA-trastuzumab could be combined with SPECT/CT imaging with [In]In-DOTA-trastuzumab in a theranostic approach. In this study, we compared DOTA-conjugated trastuzumab IgG, F(ab') or Fab complexed to In or Ac for SPECT/CT imaging and α-particle RIT of subcutaneous (s.

View Article and Find Full Text PDF

The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its Omicron subvariants drastically amplifies transmissibility, infectivity, and immune escape, mainly due to their resistance to most neutralizing antibodies. Thus, exploring the mechanisms underlying antibody evasion is crucial. Although the full-length native form of antibody, immunoglobulin G (IgG), offers valuable insights into the neutralization, structural investigations primarily focus on the fragment of antigen-binding (Fab).

View Article and Find Full Text PDF

Unlabelled: The B cell antigen receptor (BCR) complex, comprised of antigen recognition and signaling components, functions in initiating B cell activation. While structural studies have described BCR domain organization, gaps remain in our understanding of its antigen binding domain (Fab, fragment antigen-binding) disposition, and how antigen binding is sensed to initiate signaling. Here, we report antigen affinity and signaling of the immunoglobulin (Ig) class IgM and IgG BCRs and define conformational states of full-length BCRs of two human broadly neutralizing antibodies, the glycan-specific, heavy chain domain-swapped, I-shaped 2G12, and a canonical Y-shaped antibody, CH31, that recognizes the CD4-binding site on the HIV-1 Envelope protein (Env).

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!