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Background Agricultural workers face high heat stress risk due to environmental and working conditions. Migrant agricultural workers (MAW) are especially vulnerable due to additional structural factors including irregular migratory status and high economic needs. Our study explores the lived experiences of occupational heat stress among MAW and its impact on health. Methods An interpretive, qualitative design was employed. Through purposive sampling we selected MAW in Almeria, Lleida, and Huelva for semi-structured interviews. Interviews were audio-recorded, transcribed, and analyzed using reflexive thematic analysis. Results Thirty interviews were conducted with six female and 24 male MAW, predominantly from sub-Saharan and North-Africa. The findings were organized into five overarching themes: Working under the sun: exposure and embodiment; The dilemma of heat: work or wellbeing; Employer´s efforts to protect workers: a regime of discretion; Protecting oneself from the heat: navigating limited agency; and non-work-related factors: compounding vulnerabilities. Participants described discomfort and heat-related illness symptoms. Protective strategies included drinking water, wearing appropriate clothing, and taking breaks, but pressure from supervisors to maintain a fast work pace and limit breaks often compromised these protective efforts. Employer discretion largely determined access to heat-protective measures. Participants also reported limited ability to cool down after work due to high indoor temperatures in substandard housing. Conclusions Occupational heat risk for MAW extends beyond environmental factors and is amplified by socioeconomic inequities. Implementation of more specific and enforceable heat-protection measures and improved enforcement mechanisms, alongside mandated improvements to working and living conditions, are needed to reduce heat-related health risks.

In this work, the preparation and characterization of composites from cellulose acetate (CA)–poly(ethylene oxide) (PEO) nanofibers (NFs) with incorporated zinc oxide nanoparticles (ZnO-NPs) using solution blow spinning (SBS) is reported. CA–PEO nanofibers were produced by spinning solution that contained a higher CA-to-PEO ratio and lower (equal) CA-to-PEO ratio. Nanoparticles were added to comprise 2.5% and 5% of the solution, calculated on the weight of the polymers. To have better control of the SBS processing conditions, characterization of the spinning suspensions is carried out, which reveals a decrease in viscosity (two- to eightfold) upon the addition of NPs. It is observed that this variation of viscosity does not significantly affect the mean diameters of nanofibers, but does affect the mode of the nanofibers’ size distribution, whereby lower viscosity provides thinner fibers. FESEM–EDS confirms ZnO NP encapsulation into nanofibers, specifically into the CA component based on UV-vis studies, since the release of ZnO is not detected for up to 5 days in deionized water, despite the significant swelling of the material and accompanied dissolution of water-soluble PEO. Upon the dissolution of CA nanofibers into acetone, immediate release of ZnO is detected, both visually and by spectrometer. ATR–FTIR studies reveal interaction of ZnO with the CA component of composite nanofibers. As ZnO nanoparticles are known for their bioactivity, it can be concluded that these CA–PEO–ZnO composites are good candidates to be used in filtration membranes, with no loss of incorporated ZnO NPs or their release into an environment.

What can we do to stop the sabotage of the President's program? We are unknown, unimportant people--but there are a lot of us. We helped elect President Eisenhower because we believed in him and we still do.

By means of a differential screening technique, a 92-kDa antigen, designated Tp92, was identified from Treponema pallidum subspecies pallidum. This protein is similar in sequence to the protective surface antigens D15 from Haemophilus influenzae and Oma87 from Pasteurella multocida. Amino acid sequence analyses revealed a cleavable N-terminal signal sequence and predicted the outer membrane location for Tp92. In support of this, antiserum raised against recombinant Tp92 promotes opsonization and phagocytosis of T. pallidum by rabbit macrophages, and anti-Tp92 reactivity is absent from washed treponemal preparations presumed to be lacking outer membranes. The Tp92 amino acid sequence is 95.5%–100% conserved among 11 strains representing 4 pathogenic treponemes, and immunization with recombinant Tp92 partially protected rabbits from subsequent T. pallidum challenge. These results demonstrate that Tp92 is an invariant, immunoprotective antigen that may be present on the surface of T. pallidum and may represent a potential vaccine candidate for syphilis.

Abstract To identify potential opsonic targets of Treponema pallidum subsp. pallidum, a treponemal genomic expression library was constructed and differentially screened with opsonic and non-opsonic T. pallidum antisera. This method identified an immunoreactive clone containing an open reading frame encoding a 356 residue protein. Nucleotide sequence analysis demonstrated the translated protein to be a homologue of glycerophosphodiester phosphodiesterase, a glycerol metabolizing enzyme previously identified in Haemophilus influenzae, Escherichia coli, Bacillus subtilis and Borrelia hermsii. Sequence alignment analyses revealed the T. pallidum and H. influenzae enzymes share a high degree of amino acid sequence similarity (72%), suggesting that in T. pallidum this molecule may be surface exposed and involved in IgD binding as is the case with its counterpart in H. influenzae.

To identify potential opsonic targets of Treponema pallidum subsp. pallidum, a treponemal genomic expression library was constructed and differentially screened with opsonic and non-opsonic T. pallidum antisera. This method identified an immunoreactive clone containing an open reading frame encoding a 356 residue protein. Nucleotide sequence analysis demonstrated the translated protein to be a homologue of glycerophosphodiester phosphodiesterase, a glycerol metabolizing enzyme previously identified in Haemophilus influenzae, Escherichia coli, Bacillus subtilis and Borrelia hermsii. Sequence alignment analyses revealed the T. pallidum and H. influenzae enzymes share a high degree of amino acid sequence similarity (72%), suggesting that in T. pallidum this molecule may be surface exposed and involved in IgD binding as is the case with its counterpart in H. influenzae.