Recombinant antibodies and their fragments currently represent over 30% of
all biological proteins undergoing clinical trials for diagnosis and therap
y. These reagents dominate the cancer-targeting field, as highlighted by th
e recent approval of the first engineered therapeutic antibodies by the Foo
d and Drugs Administration (FDA). Last year, important advances have been m
ade in the design, selection and production of recombinant antibodies. The
natural immune repertoire and somatic cell affinity maturation has been sup
erseded by large antibody display libraries and rapid molecular evolution s
trategies. These novel libraries and selection methods have enabled the rap
id isolation of high-affinity cancer targeting and antiviral antibodies, th
e latter capable of redirecting viruses for gene therapy applications. In a
lternative strategies for cancer diagnosis and therapy, recombinant antibod
y fragments have been fused to radioisotopes, drugs, toxins, enzymes and bi
osensor surfaces. Antibody-directed cancer pre-targeting followed by prodru
g activation (ADEPT) has proved a most promising therapeutic strategy. Mult
i-specific antibodies have been effective for cytotoxic T-cell recruitment
and antibody-fusion proteins have delivered enhanced immunotherapeutic and
vaccination strategies. The new millennium is indeed an exciting time for t
he design, selection and formulation of a range of new antibody-based produ
cts for cancer diagnosis and therapy.