Anti-Viral hemorrhagic septicemia virus [3F1H10]

Absolute Antibody

Anti-Viral hemorrhagic septicemia virus [3F1H10]

9

This antibody is specific for the transmembrane envelope glycoprotein (G protein) of viral hemorrhagic septicemia virus (VHSV). The G protein is the only protein known to be present on the surface of the virus particle, and it constitutes less than 10% of

The neutralizing activity of the original format of this antibody (mouse IgG1) was measured at the cell culture level in a plaque neutralization test (50% PNT). This antibody was administered to rainbow trout via intraperitoneal injection to evaluate its passive immunization protective effect and efficacy against Egtved virus infection. This antibody was used as the primary antibody in immunoblotting (IB) to detect the viral glycoprotein. This antibody, conjugated with fluorochromes like FITC or TRITC, was employed to visualize and detect Egtved virus-infected cells. This antibody, which was highly neutralizing in vitro, also provided the highest degree of protection in vivo of the antibodies tested (Lorenzen et al., 1990; PMID: 1690259). This antibodys neutralizing activity against different VHSV isolates was determined by 50% PNT; This antibodys original format neutralized type I isolates VHSV (I-F1 and I-92) well, but higher concentrations were needed to neutralize type II isolates and even higher concentrations were required to neutralize type III isolates. An ELISA was used to detect and quantify the antibodys binding efficiency to various VHSV strains. The antibodys binding kinetics were evaluated by surface plasmon resonance (SPR) analysis resulting in a KD of 3.8 nM for the immobilized G protein of VHSV strain I-F1 and a KD of 64 nM for the immobilized G protein of VHSV strain I-92 (Lorenzen et al., 2000; PMID: 10938729). Monovalent versions of this antibody, in the form of Fab and recombinant single-chain antibody fragments (scAbs), were able to neutralize VHSV, indicating that the Fc moiety and divalency of the antibody molecules are not necessary for neutralization. However, the neutralizing activity of Fab and scAb fragments was generally lower compared to the parent antibody due to the higher avidity of the divalent parent molecules; the Fab and scAb fragments exhibited a 10-100-fold increase in kd compared to the parent antibody, while the kas were similar. The increased kd was accompanied by decreased neutralizing activity. The KD measured against immobilized G protein of VHSV strain DK-F1 was 3.8 nM for the parent antibody and 124 and 241 nM for the daughter Fab and scAb, respectively (Cupit et al., 2001; PMID: 11682124).

ImmunoFluorescence, Western Blot, ELISA, Neutralisation/Blocking, Other Application

Research Use Only

Monoclonal

3F1H10

Rabbit

IgG

Spike glycoprotein

Virus

-20°C,2°C to 8°C

12352203