A comparison of in vitro methods for assessing the potency of therapeutic antisera against the venom of the coral snake Micrurus nigrocinctus

Alape-Girón, Alberto; Miranda-Arrieta, Keyna; Cortes-Bratti, ximena; Stiles, Bradley G.; Gutiérrez, José Marı́a

doi:10.1016/s0041-0101(96)00150-x

Cited by 24 publications

(25 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, it was noticeable that Hum1 and Hum2 sera displayed the highest neutralizing ability, although they had moderate antibody titres against both N-terminal and basic regions. It is well known that the neutralizing potential of serum antibodies to a given antigen does not systematically correlate with antibody titres measured in ELISA (Alape-Giron et al, 1997;Simonsen et al, 1987) but to the antibody affinity for the target antigen (Olszewska et al, 2000). Hum1 and Hum2 antibodies are likely to display a high affinity for rTat protein.…”

Section: Discussionmentioning

confidence: 99%

Important B-cell epitopes for neutralization of human immunodeficiency virus type 1 Tat in serum samples of humans and different animal species immunized with Tat protein or peptides

Moreau

Belliard

Partidos

et al. 2004

Journal of General Virology

View full text Add to dashboard Cite

The Tat regulatory protein of human immunodeficiency virus type 1 (HIV-1) is secreted by infected cells and plays a key role in viral pathogenesis and replication. Tat protein has been proposed as a target antigen for vaccine design since anti-Tat antibodies may interfere with virus spread and disease progression. The aim of this study was to analyse the serum antibody response of mice, rabbits, macaques and humans immunized with recombinant Tat, synthetic Tat, Tat toxoid or Tat peptides and to examine the biological properties of these antibodies in terms of Tat-induced transactivation and HIV-1 replication. Only sera with antibody specificity to both N-terminal and basic functional domains were able to inhibit extracellular Tat-dependent transactivation significantly in vitro. Antibodies from a human subject immunized with Tat also reduced HIV-1 replication in acutely infected T cells and blocked reactivation of virus replicating low levels in chronically infected cells by exogenous Tat. These results demonstrate that immunization with Tat protein or a combination of synthetic Tat peptides elicits the production of Tat-neutralizing serum antibodies and suggest that Tat vaccination could be used to block in vivo extracellular Tat autocrine/paracrine transactivation of HIV-1 replication.

show abstract

Section: Discussionmentioning

confidence: 99%

Important B-cell epitopes for neutralization of human immunodeficiency virus type 1 Tat in serum samples of humans and different animal species immunized with Tat protein or peptides

Moreau

Belliard

Partidos

et al. 2004

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…However, this in vitro assay requires the preparation of chick biventer cervicis muscles and the assay is laborious and time-consuming. In vitro neutralization of some venom enzymatic activities have been studied for use in AV potency assay 12 . It was shown that the neutralization of phospholipase A 2 activities by antivenom against Micrurus nigrocinctus highly correlated with the in vivo neutralization activity.…”

Section: Introductionmentioning

confidence: 99%

A novel in vitro potency assay of antisera against Thai Naja kaouthia based on nicotinic acetylcholine receptor binding

Ratanabanangkoon

Simsiriwong

Pruksaphon

et al. 2017

Sci Rep

View full text Add to dashboard Cite

Snake envenomation is an important medical problem. One of the hurdles in antivenom development is the in vivo assay of antivenom potency which is expensive, gives variable results and kills many animals. We report a novel in vitro assay involving the specific binding of the postsynaptic neurotoxins (PSNTs) of elapid snakes with purified Torpedo californica nicotinic acetylcholine receptor (nAChR). The potency of an antivenom is determined by its antibody ability to bind and neutralize the PSNT, thus preventing it from binding to nAChR. The PSNT of Naja kaouthia (NK3) was immobilized on microtiter wells and nAChR was added to bind with it. The in vitro IC50 of N. kaouthia venom that inhibited 50% of nAChR binding to the immobilized NK3 was determined. Varying concentrations of antisera against N. kaouthia were separately pre-incubated with 5xIC50 of N. kaouthia venom. The remaining free NK3 were incubated with nAChR before adding to the NK3 coated plates. The in vitro and in vivo median effective ratio, ER50s of 12 batches of antisera showed correlation (R 2) of 0.9809 (p < 0.0001). This in vitro assay should be applicable to antisera against other elapid venoms and should reduce the use of live animals and accelerate development of life-saving antivenoms.

show abstract

“…A good correlation, r = 0.65, was found between the in vitro hyaluronidase neutralization values and the ELISA titers of anti-CcHaseII against the corresponding venom at 1st, 4th and 7th weeks, suggesting that the antiserum in these periods more avid because more antigenic epitopes were involved. A set of high correlations was reported for the neutralization of specific venom activities with ELISA titers [1,42]. The success of toxin neutralization by antivenom depends on the abundance of specific antibody against the principle lethal toxin of the venom also on its binding affinity for the toxin [19,45].…”

Section: Detection Of Antibodies and Immunoreactivity Of Anticchaseiimentioning

confidence: 99%

Role of hyaluronidase inhibitors in the neutralization of toxicity of Egyptian horned viper Cerastes cerastes venom

Wahby

Mahdy

El-mezayen

et al. 2012

Journal of Genetic Engineering and Biotechnology

View full text Add to dashboard Cite

Hyaluronidase ''venom spreading factor'' is a common component of snake venoms and indirectly potentiates venom toxicity. It may cause permanent local tissue destruction at the bite site/systemic collapse of the envenomated victim. The present study was performed to assess the benefits of inhibiting the hyaluronidase activity of Egyptian horned viper, Cerastes cerastes (Cc). The aqueous extracts of some medicinal plants were screened for their inhibitory effect on hyaluronidase activity of Cc venom. The results revealed that the Rosmarinus officinalis (Ro) extract is the most potent hyaluronidase inhibitor among the tested extracts. The Ro extract is more potent inhibitory effect on the hyaluronidase activity than the prepared rabbit monoclonal antiserum of previously purified hyaluronidase enzyme from Cc venom (anti-CcHaseII). In addition, the Ro extract is efficiently inhibited the activity of hemorrhagic toxin previously purified from Cc venom, and it also neutralized the edema inducing activity of the Cc venom in vivo. Furthermore, the Ro extract markedly increased the survival time of experimental mice injected with lethal dose of Cc venom up to 7 h in compared to mice injected with venom alone or with venom/anti-CcHaseII (15 ± 5, 75 ± 4 min), respectively. Our findings imply the significance of plant-derived hyaluronidase inhibitor in the neutralization of local effects of Cc venom and retardation of death time. Therefore, it may use as a therapeutic value in complementary snakebite therapy.

show abstract

A comparison of in vitro methods for assessing the potency of therapeutic antisera against the venom of the coral snake Micrurus nigrocinctus

Cited by 24 publications

References 21 publications

Important B-cell epitopes for neutralization of human immunodeficiency virus type 1 Tat in serum samples of humans and different animal species immunized with Tat protein or peptides

Important B-cell epitopes for neutralization of human immunodeficiency virus type 1 Tat in serum samples of humans and different animal species immunized with Tat protein or peptides

A novel in vitro potency assay of antisera against Thai Naja kaouthia based on nicotinic acetylcholine receptor binding

Role of hyaluronidase inhibitors in the neutralization of toxicity of Egyptian horned viper Cerastes cerastes venom

Contact Info

Product

Resources

About