Rheumatoid arthritis (RA) is characterised by persistent joint inflammation and concomitant joint destruction, and in severe cases with extra-articular manifestations, multiple joint involvement, and a significant reduction in life expectancy. In addition, functional decline and disability inevitably accompanies joint destruction. The extent to which most standard medical approaches have a positive impact on the course of rheumatoid disease is the subject of debate.1 Intense research effort has focused on understanding cellular inflammatory mechanisms that may serve as therapeutic targets.

Tumour necrosis factor α (TNFα) is a pleiotropic cytokine overproduced in rheumatoid joints primarily by macrophages.2 Although the causes of RA are not fully understood, TNFα seems to play a cardinal part in a variety of events in inflammatory synovitis and articular matrix degradation,3 and is therefore a prime target for directed immunotherapy in RA.4 ,5 Accordingly, antibodies and soluble TNF receptors that bind TNFα with high specificity neutralise its activity and have been developed for use as therapeutic agents. However, current anti-TNFα treatments for RA may be limited by their capacity to elicit immune responses to their non-human elements or artificially fused human sequences.6 The high specificity neutralisation potency of a previously perfected murine monoclonal antibody was transferred to a fully human IgG1 antibody format (D2E7).

D2E7, a high affinity, recombinant, fully human anti-TNFα …