Project description:Specimens belonging to a new species of Perinereis Kinberg, 1865 were collected fromnatural oyster reefs in an estuarine environmenton Florida's southwest coast. The genus Perinereis includes more than 70 species, of which, Perinereis aibuhitensis (Grube, 1878), Perinereis brevicirrata (Treadwell, 1920), Perinereis camiguinoides (Augener, 1922), Perinereis jascooki Gibbs, 1972, Perinereis kuwaitensis Mohammad, 1970, Perinereis singaporiensis (Grube, 1878), Perinereis vancaurica (Ehlers, 1868) and the new species have two short bars on Area VI and notopodial dorsal ligules that are not greatly expanded. The most geographically close species is Perinereis brevicirrata. The new species can be distinguished from Perinereis brevicirrata by the absence of a notopodial prechaetal lobe, Area V with 3 cones in a triangle, and Area VII-VIII with two well-defined rows of 33 paragnaths, the basal row having longer paragnaths in relation to the distal ones. The new species resembles Perinereis singaporiensis based on the absence of notopodial prechaetal lobe; however, the two species differ in some morphological characteristics such as tentacular cirri length, shape of dorsal notopodial ligules, and falciger blades. A key to all American species of Perinereis is included.
Project description:Despite being one of the most common groups of polychaetes on intertidal shores, the genus Perinereis (Nereididae) is comparatively poorly known taxonomically, with confusion still existing due to the lack of comprehensive systematic studies. The systematics of Perinereis species from the intertidal Egyptian coasts of the Red Sea, Gulf of Suez and Suez Canal have been investigated using morphology and the mitochondrial barcoding marker cytochrome oxidase subunit I (COI). New sequence data was obtained for 102 Perinereis specimens and analysis included all publicly available COI data from other Perinereis species. The COI data indicate that monophyly of the P.nuntia species group is doubtful, as specimens identified in this species group from south-eastern Asia and Australia form a monophyletic group exclusive of the three new species described in this study from the Red Sea region. A morphometric character set (26 characters) was used to identify and characterize each specimen in the study. Three distinct morphospecies belonging to the P.nuntia species group were found, each differentiated by the number and type of paragnaths on pharyngeal areas V and VI, relative sizes of parapodial lobes, type of notochaetae and neurochaetae, and form of the neurochaetal falciger blades. The three morphospecies were well supported by COI data: two of the three new species, Perinereissuezensis sp. nov. and Perinereisfayedensis sp. nov., are closely similar to P.nuntia sensu stricto, while the other, Perinereisdamietta sp. nov., is similar to P.heterodonta. The new species are described and illustrated, and bring the number of species in Perinereis to 97. The new species are compared and contrasted to the closely similar P.heterodonta, P.nuntia and other congeners from the region.
Project description:Marine organisms are a rich source of enzymes that exhibit excellent biological activity and a wide range of applications. However, there has been limited research on the proteases found in marine mudflat organisms. Based on this background, the marine fibrinolytic enzyme FELP, which was isolated and purified from clamworm (Perinereis aibuhitensis), has exhibited excellent fibrinolytic activity. We demonstrated the FELP with a purification of 10.61-fold by precipitation with ammonium sulfate, ion-exchange chromatography, and gel-filtration chromatography. SDS-PAGE, fibrin plate method, and LC-MS/MS indicated that the molecular weight of FELP is 28.9 kDa and identified FELP as a fibrinolytic enzyme-like protease. FELP displayed the maximum fibrinolytic activity at pH 9 (407 ± 16 mm2) and 50 °C (724 ± 27 mm2) and had excellent stability at pH 7-11 (50%) or 30-60 °C (60%), respectively. The three-dimensional structure of some amino acid residues of FELP was predicted with the SWISS-MODEL. The fibrinolytic and fibrinogenolytic assays showed that the enzyme possessed direct fibrinolytic activity and indirect fibrinolysis via the activation of plasminogen; it could preferentially degrade Aα-chains of fibrinogen, followed by Bβ- and γ-chains. Overall, the fibrinolytic enzyme was successfully purified from Perinereis aibuhitensis, a marine Annelida (phylum), with favorable stability that has strong fibrinolysis activity in vitro. Therefore, FELP appears to be a potent fibrinolytic enzyme with an application that deserves further investigation.