Currently, I'm doing western blots using a phage displayed pool of scFv's
as the primary antibody. I test against the protein, that the phage were
selected against in the first place and to check specificity, also against
a bacterial cytosolic extract from the E.coli strain, TG-1.
What I see after development is a pattern of 11 proteins in the extract
recognized by the phage added. They are from 14 kDa to 40 kDa in size.
They are not a result of crossreactivity from the scFv's as they also appear
when I use helper phage as a negative control. It must then be a specific
interaction between the phage-body and some bacterial proteins.
I know that thioredoxin is known to interact with the phage particle during
the assembly process, but I was wondering if anyone could help me with
other possible candidates for such interactions.
References would be appreciated