Cyphocarax gilbert (Szidat, L., 1948) is a fish commonly found in coastal drainage of eastern Brazil. This fish is sometimes caught with signs of infection by the crustacean Riggia paranensis, a haematophagous parasite. A remarkable feature of infected fish is that they lack gonads. In this paper we have analysed the frequency of parasitism, the gonadal development of non-infected fish and the profile of plasma proteins in both infected and non-infected specimens. Two reproductive periods/year were observed, beginning in February and August. On average, 40% of fish were infected, in the Itabapoana River (Brazil). Sex-specific proteins were identified by electrophoresis. SDS-PAGE analysis demonstrated that a 143 kDa female-specific glycolipoprotein (FSP) is a calcium-binding phosphoprotein. FSP was isolated through ultracentrifugation and SDS-PAGE analysis showed that the native protein is composed of three polypeptides of 143, 100 and 70 kDa. Both FSP and a 33 kDa male-specific protein (MSP) are absent from infected fish plasma. FSP levels in female plasma changes with the developmental stage of gonads. Altogether these data suggest that the FSP corresponds to fish vitellogenin. Furthermore, the absence of the above-mentioned proteins in infected fish suggests that R. paranensis might interfere with the regular hormonal process of fish vitellogenesis.

Anti-Bacillus megaterium activity was measured in unfractionated plasma withdrawn from three common US East Coast bivalve molluscs: an oyster Crassostrea virginica and the mussels Geukensia demissa and Mytilus edulis. The activities of the plasma samples from these bivalves were also measured against a C. virginica pathogen Perkinsus marinus. Strong anti-B. megaterium activity was measured in plasma from C. virginica and M. edulis, but was not detected in G. demissa. Bactericidal activity was found in hemocyte extracts from all bivalves in this study, suggesting a cellular origin of cytotoxic humoral factors. Peptides (< 10 kDa) were separated from the plasma samples by ultrafiltration; weak antibacterial peptide activity was quantified in C. virginica peptides, but not in peptides from the mussels. In the case of P. marinus, plasma from M. edulis or G. demissa was boldly cidal as compared to plasma from C. virginica. This difference in activity probably reflects the low pathogenicity of this oyster parasite for the mussel species tested. In summary, the bactericidal activity of plasma proteins from these bivalves showed considerable interspecies variation and did not necessarily correlate directly with antiprotistan activity. When present, antibacterial and antiprotistan activities seemed to be associated with plasma proteins rather than < 10-kDa plasma peptides, with the possible exception of C. virginica anti-B. megaterium activity and the occasionally expressed anti-P. marinus activity of M. edulis peptides. The precise identity of the plasma protein(s) responsible for the antimicrobial activities measured have yet to be determined, but it is likely that agents other than, or in addition to, lysozyme play significant roles in the process.