A single VH domain intrabody to RAS stops transformation in vitro.

2003 NOV 5 - (NewsRx.com & NewsRx.net) -- A new way of generating intrabodies yields an intrabody to RAS that could inhibit related oncogenic transformation in vitro.

According to recent research from England, "There is a major need in target validation and therapeutic applications for molecules that can interfere with protein function inside cells. Intracellular antibodies (intrabodies) can bind to specific targets in cells, but isolation of intrabodies is currently difficult.

"Intrabodies are normally single chain Fv fragments comprising variable domains of the immunoglobulin heavy (VH) and light chains (VL). We now demonstrate that single VH domains have excellent intracellular properties of solubility, stability, and expression within the cells of higher organisms; and can exhibit specific antigen recognition in vivo.

"We have used this intracellular single variable domain (IDab) format, based on a previously characterized intrabody consensus scaffold, to generate diverse intrabody libraries for direct in vivo screening. IDabs were isolated using 2 distinct antigens and affinities of isolated IDabs ranged between 20 nM and 200 nM," wrote T. Tanaka and colleagues.

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