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Background  The possibility that a sub domain of a C clade HIV-1 gp120 could act as an effective immunogen was investigated. To do this, the outer domain (OD) of gp120 CN54  was expressed and characterized in a construct marked by a re-introduced conformational epitope for MAb 2G12. The expressed sequence showed efficient epitope retention on the isolated OD CN54  suggesting authentic folding. To facilitate purification and subsequent immunogenicity OD CN54  was fused to the Fc domain of human IgG1. Mice were immunised with the resulting fusion proteins and also with gp120 CN54 -Fc and gp120 alone.    Results  Fusion to Fc was found to stimulate antibody titre and Fc tagged OD CN54  was substantially more immunogenic than non-tagged gp120. Immunogenicity appeared the result of Fc facilitated antigen processing as immunisation with an Fc domain mutant that reduced binding to the FcR lead to a reduction in antibody titre when compared to the parental sequence. The breadth of the antibody response was assessed by serum reaction with five overlapping fragments of gp120 CN54  expressed as GST fusion proteins in bacteria. A predominant anti-inner domain and anti-V3C3 response was observed following immunisation with gp120 CN54 -Fc and an anti-V3C3 response to the OD CN54 -Fc fusion.    Conclusion  The outer domain of gp120 CN54  is correctly folded following expression as a C terminal fusion protein. Immunogenicity is substantial when targeted to antigen presenting cells but shows V3 dominance in the polyvalent response. The gp120 outer domain has potential as a candidate vaccine component.

Immunogenicity of the outer domain of a HIV-1 clade C gp120