The phage display is becoming a very powerful technology. Filamentous
phages can present on their surface either peptides, proteins or antib
ody fragments. Peptide libraries are selected on antibodies to rapidly
map epitopes, or on purified target to identify interaction sites. Se
lection on receptors identifies new therapeutic ligands while selectio
n on enzymes identifies new substrates. New protocols are leading to s
election on more complex targets as cells, patient serums or tissues.
Combinatorial antibody libraries represent a performant alternative to
hybridoma technology. Libraries constructed from immunised. repertoir
es allow rapid selection of high affinity binders. Libraries construct
ed from naive repertoires allow isolation of low affinity antibodies a
gainst a large range of antigens without the need of immunisation. Nai
ve libraries are particularly interesting to isolate human or anti-sel
f antibodies. A large number of biologically active proteins have been
expressed on phage and submitted to several rounds of modification/se
lection on target. This << in vitro evolution >> represents an excelle
nt tool for structure-function analysis. This review summarises severa
l applications which are developped in an increasing number of laborat
ories.