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Red snapper fishing (Lutjanus purpureus) is an important fishing activity for the Brazilian economy due to its export. The scarcity of up-to-date information on this system's ecology, economy, and social characteristics contributes to inefficient management. We analyze whether the commercial snapper fishery on the Amazon continental shelf is socioecologically sustainable. For this, an assessment tool was used that can be applied to fishing systems with little data, the Fisheries Performance Indicators (FPI). The results showed that the critical points of this activity are mainly related to the Ecological indicator (2.3) and the Economic indicator (2.8). The best indicator was the Community (3.8). The problems that put at risk the permanence of the activity and its maintenance are: (i) fishing for juveniles; (ii) illegal vessels; (iii) lack of collaboration of the fishing sector with science, and (iv) unreliability of data supplied. All the points mentioned make the snapper fishery on the north coast of Brazil socio-ecologically unsustainable in the long term., Competing Interests: All authors listed have made a substantial, direct, and intellectual contribution to the work, and approved it for publication. This does not alter our adherence to PLOS ONE policies on sharing data and materials., (Copyright: © 2024 Mescouto et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)

Background: The proteins responsible for the key molecular events leading to the structural changes between the developmental stages of Echinococcus granulosus remain unknown. In this work, azidohomoalanine (AHA)-specific labeling was used to identify proteins expressed by E. granulosus protoscoleces (PSCs) upon the induction of strobilar development., Methodology/principal Findings: The in vitro incorporation of AHA with different tags into newly synthesized proteins (NSPs) by PSCs was analyzed using SDS-PAGE and confocal microscopy. The LC-MS/MS analysis of AHA-labeled NSPs by PSCs undergoing strobilation allowed for the identification of 365 proteins, of which 75 were differentially expressed in comparison between the presence or absence of strobilation stimuli and 51 were expressed exclusively in either condition. These proteins were mainly involved in metabolic, regulatory and signaling processes., Conclusions/significance: After the controlled-labeling of proteins during the induction of strobilar development, we identified modifications in protein expression. The changes in the metabolism and the activation of control and signaling pathways may be important for the correct parasite development and be target for further studies.

Botulinum neurotoxins (BoNTs) are extremely potent toxins that are capable of causing death or respiratory failure leading to long-term intensive care. Treatment includes serotype-specific antitoxins, which must be administered early in the course of the intoxication. Rapidly determining human exposure to BoNT is an important public health goal. In previous work, our laboratory focused on developing Endopep-MS, a mass spectrometry-based endopeptidase method for detecting and differentiating BoNT/A-G serotypes in buffer and BoNT/A, /B, /E, and /F in clinical samples. We have previously reported the effectiveness of antibody-capture to purify and concentrate BoNTs from complex matrices, such as clinical samples. Because some antibodies inhibit or neutralize the activity of BoNT, the choice of antibody with which to extract the toxin is critical. In this work, we evaluated a panel of 16 anti-BoNT/A monoclonal antibodies (mAbs) for their ability to inhibit the in vitro activity of BoNT/A1, /A2, and /A3 complex as well as the recombinant LC of A1. We also evaluated the same antibody panel for the ability to extract BoNT/A1, /A2, and /A3. Among the mAbs, there were significant differences in extraction efficiency, ability to extract BoNT/A subtypes, and inhibitory effect on BoNT catalytic activity. The mAbs binding the C-terminal portion of the BoNT/A heavy chain had optimal properties for use in the Endopep-MS assay.