Search bioRxiv⌕ Search

Biology subjects

Andrade, C. M.

Publications and source records attributed to Andrade, C. M..

4 recordsLinked to original sources

Repeated shrimp allergen exposure drives 5-lipoxygenase-dependent avoidance and selective gut-brain activation

Peripheral immune processes can shape animal behavior, yet how noninfectious inflammatory reactions affect neural activity and behavioral outputs remains poorly understood. We developed an optimized murine model of shrimp allergy using whole shrimp extract to examine how a complex dietary allergen elicits integrated immune, neural, and behavioral responses. Sensitized mice received repeated oral shrimp challenges and were assessed for allergic pathology, food preference, affective-like behaviors, and neuronal activation in the brain. Repeated exposure increased total IgE and shrimp-specific IgG1, induced mast cell activation, accelerated gastrointestinal transit, caused mild hypothermia consistent with oral anaphylaxis, and increased intestinal length. Shrimp-sensitized mice did not avoid shrimp solution after sensitization alone. Instead, avoidance emerged only after repeated oral challenges and strengthened over time. This delayed aversion occurred without detectable changes in locomotor activity or measures of anxiety-like or depressive-like behavior at the time points tested. Repeated shrimp exposure increased cFOS expression in the area postrema, nucleus of the tractus solitarius, central amygdala, and paraventricular nucleus of the thalamus, implicating brainstem and limbic-thalamic pathways involved in visceral sensing and aversion. Pharmacological inhibition of 5-lipoxygenase partially reversed avoidance and reduced circulating mast cell protease-1 in allergic mice. These findings establish a robust whole-shrimp allergy model and show that a complex food allergen engages gut-brain pathways to promote 5-lipoxygenase-dependent avoidance. The delayed, selective nature of this response supports immune-mediated food aversion as a shared output of food allergy, while suggesting that its kinetics and neural recruitment vary with allergen identity and inflammatory context.

immunology↗

Controlled human infection with Plasmodium falciparum-infected mosquito bites elicits antibodies against mosquito salivary protein SG1L3

Human malaria infections begin with the injection of Plasmodium sporozoites via mosquito saliva. Whole sporozoite immunizations have been used as a model to study immune responses to malaria parasites, having culminated in circumsporozoite protein (CSP)-targeting vaccines and monoclonal antibodies (mAbs). However, antibody responses targeting non-CSP antigens on the sporozoite surface remain poorly characterized. Here, we isolated single B cells from a human volunteer immunized by Plasmodium falciparum-infected mosquito bites, who had acquired non-CSP-specific antibodies that recognize sporozoites. We identified two mAbs that recognize the surface of P. falciparum sporozoites, but do not bind to CSP. Using immunoprecipitation followed by mass-spectrometry, we found that the target of these mAbs is not a P. falciparum protein but the mosquito salivary protein SG1L3. We observed that recombinant SG1L3 binds to P. falciparum sporozoites. However, the SG1L3-specific mAbs and SG1L3-specific polyclonal antibodies from this volunteer, as well as polyclonal antibodies raised against recombinant SG1L3 in rabbits, fail to block liver stage infection in vitro, making this an unlikely target for functional antibodies. We observed that inhabitants from an area with intense Anopheles exposure in Burkina Faso can have antibodies against SG1L3, and that antibody titers increase with age. In conclusion, we identified the first human mAbs against a mosquito saliva protein that binds to the surface of sporozoites. Future work should assess whether naturally acquired antibodies against this protein may be used as a serological marker of mosquito exposure.

microbiology↗

Uncovering the genetic diversity of the malaria parasite antigen MSP2 across Sub-Saharan Africa

Genetic diversity in Plasmodium falciparum poses a significant challenge to malaria control and elimination. This is particularly important for developing fully efficacious vaccines, which should include valuable blood stage antigens. Several antigen candidates are highly diverse and require further understanding. We surveyed the genetic diversity of the highly polymorphic merozoite surface protein 2 (MSP2) in 2761 P. falciparum isolates collected across Sub-Saharan Africa. Using PCR-based genotyping and long-read sequencing, we identified extensive diversity among msp2 size variants and sequences. Some size variants were more prevalent than others across different geographical regions, transmission intensities, and time points. These variants comprised multiple unique sequences, of which several were geographically and temporally widespread. Our study reveals greater msp2 sequence diversity than previously known, while also identifying interesting similarities in sequence and gene length across Sub-Saharan Africa. These findings support the further exploration of common msp2 variants in relation to parasite virulence and vaccine development.

microbiology↗

Structure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies

The Pfs230:Pfs48/45 complex forms the basis for leading malaria transmission-blocking vaccine candidates, yet li]le is known about its molecular assembly. Here, we used cryogenic electron microscopy to elucidate the structure of the endogenous Pfs230:Pfs48/45 complex bound to six potent transmission-blocking antibodies. Pfs230 consists of multiple domain clusters rigidified by interactions mediated through insertion domains. Membrane-anchored Pfs48/45 forms a disc-like structure and interacts with a short C-terminal peptide on Pfs230 that is critical for Pfs230 membrane-retention in vivo. Interestingly, membrane retention through this interaction is not essential for transmission to mosquitoes, suggesting that complex disruption is not a mode of action for transmission-blocking antibodies. Analyses of Pfs48/45-and Pfs230-targeted antibodies identify conserved epitopes on the Pfs230:Pfs48/45 complex and provides a structural paradigm for complement-dependent activity of Pfs230-targeting antibodies. Altogether, the antibody-bound Pfs230:Pfs48/45 structure presented improves our molecular understanding of this biological complex, informing the development of next-generation Plasmodium falciparum transmission-blocking interventions.

molecular biology↗