A soluble 1, kDa glycoprotein, namely gp17, was previously isolated from human semen and used to obtain mouse monoclonal or chicken polyclonal antibodies. This protein was shown to bind CD4+ T-cells and to soluble recombinant CD4 in vitro. Here, we report that the anti-gp17 monoclonal antibodies are captured by ejaculated spermatozoa and that gp17-like antigens are released by cell acid extraction. Immunoblotting experiments with monoclonal antibodies indicated that SDS-lysates from spermatozoa contain proteins with the same electrophoretic and antigenic properties of CD4 and gp17. Anti-CD4 mouse monoclonal antibodies were used to coprecipitate from NP40-lysate proteins reacting with chicken anti-gp17 antibodies. Analytical chromatography demonstrated that a number of gp17-like forms are present in the seminal plasma, put that only the 1 kDa species can be detected in the spermatozoa lysate. This protein was localised by immunofluorescence on the post-acrosomal region of the spermatozoon. The same surface domain was also reactive with anti-CD4 antibodies. After treatment to induce in vitro capacitation, gp17 was detected all over the spermatozoon head. Conversely, only a minor part of the treated spermatozoa exhibited CD4 immunostaining, which remained localised on the post-acrosomal region. The possible function of CD4 and gp17 on male germ cells is discussed.