Larval stages of pentastomids were collected from different organs of small mammals from the Peruvian Amazon. These parasitized mammals included: a western Amazonian oryzomys (Hylaeamys perenensis), an elegant oryzomys (Euryoryzomys nitidus), a lowland paca (Cuniculus paca), two kinkajous (Potos flavus), two silvery woolly monkeys (Lagothrix poeppigii) and a brown-mantled tamarin (Leontocebus fuscicollis). Pentastomids were found in the mesentery and parenchyma of the liver and lungs of these animals. All pentastomids were morphologically identified as nymphs of Porocephalus spp. Only the nymphs collected from select animals (the western Amazonian oryzomys, the elegant oryzomys and the brown-mantled tamarin) were analysed molecularly. Molecular analysis was performed amplifying the mitochondrial cytochrome c oxidase subunit I gene from select nymphs collected from the western Amazonian oryzomys, the elegant oryzomys and the brown-mantled tamarin. The nucleotide sequences exhibited 95.8–97.7% similarity between them. Also, these sequences showed an identity of 95.8–97.9% to Porocephalus crotali (GenBank accession numbers MG559647–MG559655). Molecular analysis indicated the presence of at least two Porocephalus species. These findings represent the first record of Porocephalus in these mammals, thus adding new intermediate hosts for this pentastomid genus. This work represents the first molecular data of Porocephalus in a Neotropical climate.

Pentastomids are arthropod-like parasites which inhabit the respiratory tract of tetrapods and, despite being haematophagous, cause little or no visible pathology. Nymphs (or larvae), belonging to the advanced genus Porocephalus, encyst in the tissues of rodent intermediate hosts and migrate from this site to the lung following ingestion of the intermediate host. During migration, several moults occur and instars encounter a variety of tissue barriers and environmental cues. It was therefore relevant to define the proteins and proteinases released by the different instars during this migration as they are likely to be essential for tissue penetration, feeding and immune evasion. In vitro released proteins (IVRP), commonly termed ES, were defined on the basis of molecular size and immune recognition by naturally infected rodent intermediate hosts. In addition, proteinases present in IVRP were characterized using gelatin-substrate gels and protein degradation assays. These studies showed that the protein profile is subtly different when IVRP from different instars is compared. In addition, IVRP from each instar contained metallo-proteinases with proteolysis at 48 kDa dominating in all stages. However, other higher molecular weight activities were, to an extent, released in a stage-specific manner. These proteinases degraded haemoglobin and fibrinogen as well as structural proteins such as collagen and fibronectin, suggesting roles in bloodmeal digestion and tissue penetration. Immunoglobulin digestion was not demonstrated.