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Worldwide, parenthood remains a major driver for the reduced participation of women in the job market, where discrimination stems from people's biases against mothers, based on stereotypes and misconceptions surrounding the vision of motherhood in our society. In academia, parenthood may be perceived as negatively affecting scientists' commitment and dedication, especially women's. We conducted a survey amongst Brazilian scientists and found that mothers self-reported a higher prevalence of negative bias in their workplace when compared to fathers. The perception of a negative bias was influenced by gender and career status, but not by race, scientific field or number of children. Regarding intersections, mothers with less than 15 years of hiring reported having suffered a higher rate of negative bias against themselves. We discuss implications of these results and suggest how this negative bias should be addressed in order to promote an equitable environment that does not harm women in science., Competing Interests: Competing interestsThe authors declare no competing interests., (© The Author(s) 2023.)

Despite the progress observed in recent years, women are still underrepresented in science worldwide, especially at top positions. Many factors contribute to women progressively leaving academia at different stages of their career, including motherhood, harassment and conscious and unconscious discrimination. Implicit bias plays a major negative role in recognition, promotions and career advancement of female scientists. Recently, a rank of the most influential scientists in the world was created based on several metrics, including the number of published papers and citations. Here, we analyzed the representation of Brazilian scientists in this rank, focusing on gender. Female Brazilian scientists are greatly underrepresented in the rank (11% in the Top 100,000; 18% in the Top 2%). Possible reasons for this observed scenario are related to the metrics used to rank scientists, which reproduce and amplify the well-known implicit bias in peer-review and citations. Male scientists have more self-citation than female scientists and positions in the rank varied when self-citations were included, suggesting that self-citation by male scientists increases their visibility. Discussions on the repercussions of such ranks are pivotal to avoid deepening the gender gap in science.

The coronavirus disease 2019 (COVID-19) pandemic is altering dynamics in academia, and people juggling remote work and domestic demands - including childcare - have felt impacts on their productivity. Female authors have faced a decrease in paper submission rates since the beginning of the pandemic period. The reasons for this decline in women's productivity need to be further investigated. Here, we analyzed the influence of gender, parenthood and race on academic productivity during the pandemic period based on a survey answered by 3,345 Brazilian academics from various knowledge areas and research institutions. Productivity was assessed by the ability to submit papers as planned and to meet deadlines during the initial period of social isolation in Brazil. The findings revealed that male academics - especially those without children - are the least affected group, whereas Black women and mothers are the most impacted groups. These impacts are likely a consequence of the well-known unequal division of domestic labor between men and women, which has been exacerbated during the pandemic. Additionally, our results highlight that racism strongly persists in academia, especially against Black women. The pandemic will have long-term effects on the career progression of the most affected groups. The results presented here are crucial for the development of actions and policies that aim to avoid further deepening the gender gap in academia., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2021 Staniscuaski, Kmetzsch, Soletti, Reichert, Zandonà, Ludwig, Lima, Neumann, Schwartz, Mello-Carpes, Tamajusuku, Werneck, Ricachenevsky, Infanger, Seixas, Staats and de Oliveira.)

Jaburetox is a recombinant peptide derived from one of the Canavalia ensiformis urease isoforms. This peptide induces several toxic effects on insects of different orders, including interference on muscle contractility in cockroaches, modulation of UDP-N-acetylglucosamine pyrophosphorylase (UAP) and nitric oxide synthase (NOS) activities in the central nervous system of triatomines, as well as activation of the immune system in Rhodnius prolixus. When injected, the peptide is lethal for R. prolixus and Triatoma infestans. Here, we evaluated Jaburetox toxicity to Nauphoeta cinerea cockroaches, exploring the effects on the central nervous system through the activities of UAP, NOS, acid phosphatases (ACP), and acetylcholinesterase (AChE). The results indicated that N. cinerea is not susceptible to the lethal effect of the peptide. Moreover, both in vivo and in vitro treatments with Jaburetox inhibited NOS activity, without modifying the protein levels. No alterations on ACP activity were observed. In addition, the enzyme activity of UAP only had its activity affected at 18 hr after injection. The peptide increased the AChE activity, suggesting a mechanism involved in overcoming the toxic effects. In conclusion, our findings indicate that Jaburetox affects the nitrinergic signaling as well as the AChE and UAP activities and establishes N. cinerea as a Jaburetox-resistant model for future comparative studies., (© 2020 Wiley Periodicals LLC.)

Jaburetox (JBTX) is an insecticidal and antifungal peptide derived from jack bean (Canavalia ensiformis) urease that has been considered a candidate for developing genetically modified crops. This study aimed to perform the risk assessment of the peptide JBTX following the general recommendations of the two-tiered, weight-of-evidence approach proposed by International Life Sciences Institute. The urease of C. ensiformis (JBU) and its isoform JBURE IIb (the JBTX parental protein) were assessed. The history of safe use revealed no hazard reports for the studied proteins. The available information shows that JBTX possesses selective activity against insects and fungi. JBTX and JBU primary amino acids sequences showed no relevant similarity to toxic, antinutritional or allergenic proteins. Additionally, JBTX and JBU were susceptible to in vitro digestibility, and JBU was also susceptible to heat treatment. The results did not identify potential risks of adverse effects and reactions associated to JBTX. However, further allergen (e.g. serum IgE binding test) and toxicity (e.g. rodent toxicity tests) experimentation can be done to gather additional safety information on JBTX, and to meet regulatory inquiries for commercial approval of transgenic cultivars expressing this peptide., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

Here we described two activities related to Women in Science: one main conference and one symposium, both developed during the Annual Congress of the Brazilian Physiological Society, which were held within the XXXIII Annual Meeting of the Federation of Brazilian Experimental Biology Societies, from September 3-6, 2018, in Campos do Jordão (SP/Brazil). This conference and the symposium were among the most popular activities of the congress. This is important because the activities addressed important issues, including the fact that only 29% of the worlds' researchers are women, and women have difficulty progressing in a scientific career. Our report discusses why and which strategies could change this reality. We believe this symposium has not only contributed to advance and bring insights to physiological sciences, but, more importantly, it inspired and motivated physiologists to think about gender balance and the contribution and participation of women in physiological science.

Gastric infection by Helicobacter pylori is considered a risk factor for gastric and duodenal cancer, and extragastric diseases. Previous data have shown that, in a non-enzymatic way, H. pylori urease (HPU) activates neutrophils to produce ROS and also induces platelet aggregation, requiring ADP secretion modulated by the 12-lipoxygenase pathway, a signaling cascade also triggered by the physiological agonist collagen. Here we investigated further the effects on platelets of recombinant versions of the holoenzyme HPU, and of its two subunits (HpUreA and HpUreB). Although HpUreA had no aggregating activity on platelets, it partially inhibited collagen-induced aggregation. HpUreB induced platelet aggregation in the nanomolar range, and also interfered dose-dependently on both collagen- and ADP-induced platelet aggregation. HPU-induced platelet aggregation was inhibited by antibodies against glycoprotein VI (GPVI), the main collagen receptor in platelets. Flow cytometry analysis revealed exposure of P-selectin in HPU-activated platelets. Anti-glycoprotein IIbIIIa (GPIIbIIIa) antibodies increased the binding of FITC-labeled HPU to activated platelets, whereas anti-GPVI did not. Evaluation of post-transcriptional events in HPU-activated platelets revealed modifications in the pre-mRNA processing of pro-inflammatory proteins, with increased levels of mRNAs encoding IL-1β and CD14. We concluded that HPU activates platelets probably through its HpUreB subunit. Activation of platelets by HPU turns these cells into a pro-inflammatory phenotype. Altogether, our data suggest that H. pylori urease, besides allowing bacterial survival within the gastric mucosa, may have an important, and so far overlooked, role in gastric inflammation mediated by urease-activated neutrophils and platelets.

Jaburetox is a recombinant peptide derived from a Canavalia ensiformis urease that presents toxic effects upon several species of insects, phytopathogenic fungi and yeasts of medical importance. So far, no toxicity of Jaburetox to mammals has been shown. Previous reports have identified biochemical targets of this toxic peptide in insect models, although its mechanism of action is not completely understood. In this work, we aimed to characterize the effects of Jaburetox in hemolymphatic insect cells. For this purpose, the model insect and Chagas' disease vector Rhodnius prolixus was used. In vivo and in vitro experiments indicated that Jaburetox interacts with a subset of hemocytes and it can be found in various subcellular compartments. In insects injected with Jaburetox there was an increase in the gene expression of the enzymes UDP-N-acetylglucosamine pyrophosphorylase (UAP), chitin synthase and nitric oxide synthase (NOS). Nevertheless, the expression of NOS protein, the enzyme activities of UAP and acid phosphatase (a possible link between UAP and NOS) as well as the phosphorylation state of proteins remained unchanged upon the in vivo Jaburetox treatment. Nitric oxide (NO) imaging using fluorescent probes showed that Jaburetox augmented NO production in the hemocyte aggregates when compared to controls. Even though Jaburetox activated the hemocytes, as demonstrated by wheat germ agglutinin binding assays, the peptide did not lead to an increase of their phagocytic behavior. Taken together, these findings contribute to our understanding of toxic effects of Jaburetox, a peptide with biotechnological applications and a prospective tool for rational insect control., (Copyright © 2017 Elsevier Inc. All rights reserved.)

Aquaporins (AQPs) are water channels responsible for transport of water and, in some cases, transport of small solutes such as urea and glycerol across lipid bilayer membranes. Hematophagous insects, such as Rhodnius prolixus, ingest large volumes of fluid and must rapidly eliminate the excess of water and salts from the blood meal within the gut. In order to deal with this increase in body fluid volume, a hormone-controlled diuresis is activated, during which a high rate of water and salt absorption occurs across the anterior midgut, followed by secretion of water and salts by the Malpighian tubules (MTs). Previously, one member of the MIP family (major intrinsic protein that includes the AQP family) was identified in the MTs of R. prolixus, and named RpMIP. We have described here that the RpMIP gene has different variants, and is present in tissues other than MTs. In addition, we have characterized a new AQP (RhoprAQP1) found in different tissues of R. prolixus. The expression of these transcripts in unfed insects as well as blood fed insects was evaluated using real-time quantitative PCR. Molecular models of the predicted proteins were constructed and the characteristics of their pores evaluated. A yeast complementation assay was used to validate that the products of these transcripts were bona fide AQPs. Both RhoprAQP1 and RhoprMIP-A were capable of transporting water whereas RhoprMIP-A was also capable of transporting H2O2. Taken together, these analyses suggest that RhoprMIP is probably an aquaglyceroporin, while RhoprAQP1 appears to be a strict aquaporin that transports only water., (Copyright © 2013 Elsevier Ltd. All rights reserved.)

Urea is the nitrogen fertilizer most utilized in crop production worldwide. Understanding all factors involved in urea metabolism in plants is an essential step towards assessing and possibly improving the use of urea by plants. Urease, the enzyme responsible for urea hydrolysis, and its accessory proteins, necessary for nickel incorporation into the enzyme active site and concomitant activation, have been extensively characterized in bacteria. In contrast, little is known about their plant counterparts. This work reports a detailed characterization of Glycine max UreG (GmUreG), a urease accessory protein. Two forms of native GmUreG, purified from seeds, were separated by metal affinity chromatography, and their properties (GTPase activity in absence and presence of Ni(2+) or Zn(2+), secondary structure and metal content) were compared with the recombinant protein produced in Escherichia coli. The binding affinity of recombinant GmUreG (rGmUreG) for Ni(2+) and Zn(2+) was determined by isothermal titration calorimetry. rGmUreG binds Zn(2+) or Ni(2+) differently, presenting a very tight binding site for Zn(2+) (K (d) = 0.02 ± 0.01 μM) but not for Ni(2+), thus suggesting that Zn(2+) may play a role on the plant urease assembly process, as suggested for bacteria. Size exclusion chromatography showed that Zn(2+) stabilizes a dimeric form of the rGmUreG, while NMR measurements indicate that rGmUreG belongs to the class of intrinsically disordered proteins. A homology model for the fully folded GmUreG was built and compared to bacterial UreG models, and the possible sites of interaction with other accessory proteins were investigated.