Anti-Viral hemorrhagic septicemia virus [3F1A2 ]

Absolute Antibody

Anti-Viral hemorrhagic septicemia virus [3F1A2 ]

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) against different VHSV isolates was determined by 50% PNT; it neutralized type I isolates VHSV (I-F1 and I-92) and type II isolate VHSV (II-31) well, but higher concentrations were needed to neutralize type III isolates (III-51 and III-37). 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 2.4 nM for the immobilized G protein of VHSV strain I-F1 and a KD of 12.1 nM for the immobilized G protein of VHSV strain I-92 (Lorenzen et al., 2000; PMID: 10938729). The Fab and recombinant single-chain antibody fragments (scAbs) versions of this antibody neutralized VHSV, indicating that the Fc moiety and divalency of the antibody molecules are unnecessary 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 MAb, 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 2.4 nM for the parent MAb and 227 and 77 nM for the daughter Fab and scAb, respectively (Cupit et al., 2001; PMID: 11682124).

ELISA, Neutralisation/Blocking, Other Application

Research Use Only

Monoclonal

3F1A2

Rabbit

IgG

Spike glycoprotein

Virus

-20°C,2°C to 8°C

12352203