The sex-pheromone system of Enterococcus faecalis can be viewed as a unique and highly efficient plasmid-collection mechanism. The contact needed for transfer of the conjugative sexpheromone plasmids is mediated by an adhesin, called aggregation substance, which is encoded by these plasmids. We show here that for 17 of the 18 sex-pheromone plasmids (pAM373 being the exception) described to date, their adhesins are immunologically related to each other. In each case, we observed the presence of an N-terminal fragment of about 78 kDa in addition to the 137-kDa form of mature aggregation substance. The cross-reactions were different for the various plasmids. In the case of pPDl the 78-kDa fragment reacted only weakly. The aggregation substance encoded by sex-pheromone plasmid PAD1 (Asal) was characterized in detail. The conditions used for SDSI PAGE had a drastic influence on the migration behavior of mature aggregation substance and differently migrating, interconvertible forms were identified. Preliminary data indicate that Asal might be a glycoprotein. Antibodies were isolated which are directed against the N-and C-terminal parts of aggregation substance. They showed about the same reactivity on Western blots; however, only antibodies directed against the N-terminal part of the aggregation substance could inhibit the bacterial cell/cell contact. The reactions of the two antibody preparations with induced cells of E. faecalis was analyzed by transmission electron microscopy. The results indicated that especially the N-terminal part of aggregation substance is exposed on the cell surface of E. faecalis; the C-terminal part seems to be much less exposed.The sex-pheromone system of Enterococcus faecalis was discovered by the group of D. B. Clewell (Dunny et al., 1978). A first model to its function was given in 1979 (Dunny et al., 1979); it is, with slight modifications, still valid today (see Clewell and Weaver, 1989;Dunny, 1990, for recent reviews). According to this model, the sex-pheromone system can be viewed as a highly efficient plasmid-collection mechanism which is triggered by so-called sex pheromones (small linear peptides) excreted by plasmid-free recipient strains. Donors do not excrete sex peromone(s) corresponding to their plasmid(s) ; plasmid-free recipients are expected to excrete all existing sex pheromones. As a response to sex pheromones, the donor strains synthesize an adhesin (called aggregation substance) which is of proteinaceous nature and appears as hair-like structures (Galli Correspondence to R. Wirth, Lehrstuhl fur Mikrobiologie, Ludiwg-Maximilians-Universitat Miinchen,