Biology subjects

Ghosh, E.

Publications and source records attributed to Ghosh, E..

5 recordsLinked to original sources

bioRxiv2024

'Disease-smart' assisted migration can enhance population fitness and increase resistance to pathogens via immune priming

O_LIWe studied the potential of combining insect immune priming to synergize with introduction of diverse migrant to safeguard small populations from disease outbreaks that might otherwise lead to extinction. C_LIO_LIImmune priming in insects refers to the stronger immune response insects have against pathogens after prior exposure. This enhanced immunity can be passed on to offspring and holds promise for insect conservation efforts against diseases. C_LIO_LIWe compared the fitness benefits to a small, inbred population of adding migrants that had not been primed to adding immune primed migrants. While both types of migrants enhanced reproduction, as in cases of genetic rescue, only primed migrants improved survival on exposure to a pathogen. C_LIO_LIBetter immunity led to a trade-off with reproduction in the migrants, but not upon outcrossing with the target population, revealing synergies between hybrid vigor and immune priming. C_LIO_LIGiven the demographic constraints and stochasticity that can exacerbate the effects of disease outbreaks in small populations, combining immune priming with assisted migration offers a proactive strategy to mitigate disease impacts. C_LI

ecology↗

bioRxiv2020

Performance of Bracon brevicornis (Wesmael) on two Spodoptera species and application as potential biocontrol agent against fall armyworm

Successful pest management using parasitoids requires careful evaluation of host-parasitoid interactions. Here, we report the performance of larval ecto-parasitoid wasp, Bracon brevicornis (Wesmael) on important agricultural pests, Spodoptera litura (Fabricius) and S. frugiperda (J.E. Smith). Biology of B. brevicornis was studied on different host instars under laboratory and cage setup. In no-choice assay, the parasitoid development was highest on fifth instar S. litura larvae as the wasp laid ∼253 eggs with 62% hatching, 76% pupae formation and 78% adult emergence. Similarly, these parameters were highest on fifth instar S. frugiperda larvae (293 eggs, 57% hatching, 80% pupae formation, 70% adult emergence). In two-choice assay, B. brevicornis preferred fourth or fifth over third instar larvae of both hosts. Successful parasitism depends on host paralysis and suppression of host immunity. B. brevicornis interaction downregulated cellular immunity of both hosts as shown by reduced hemocyte viability and spreading. The percent parasitism rate of B. brevicornis was unaltered in the presence of host plant, Zea mays in cage study. 76 and 84% parasitism was observed on fifth instar larvae of S. litura and S. frugiperda, respectively. We evaluated the performance of B. brevicornis as a biocontrol agent on S. frugiperda in maize field. Our results show 54% average reduction in infestation after release of B. brevicornis. Taken together, we report the performance of B. brevicornis on important insect pests for the first time in laboratory and field conditions. Our findings indicate that B. brevicornis is a promising candidate for integrated pest management.Key messagesWe have evaluated the instar preference and performance of B. brevicornis as a potential biocontrol agent for two serious pests, Spodoptera litura and S. frugiperda.Fifth instar larva was most suitable for B. brevicornis development irrespective of the host species. B. brevicornis attack induced permanent paralysis and down-regulated cellular immunity of both hosts.Our field experiment confirmed B. brevicornis as a promising parasitoid for controlling S. frugiperda, a highly invasive pest of growing concern.Competing Interest StatementThe authors have declared no competing interest.View Full Text

ecology↗

bioRxiv2019

Conformational sensors and domain-swapping reveal structural and functional differences between β-arrestin isoforms

Desensitization, signaling and trafficking of G protein-coupled receptors (GPCRs) are critically regulated by multifunctional adaptor proteins, {beta}-arrestins ({beta}arrs). The two isoforms of {beta}arrs ({beta}arr1 and 2) share a high degree of sequence and structural similarity, still however, they often mediate distinct functional outcomes in the context of GPCR signaling and regulation. A mechanistic basis for such a functional divergence of {beta}arr isoforms is still lacking. Using a set of complementary approaches including antibody fragment based conformational sensors, we discover structural differences between {beta}arr1 and 2 upon their interaction with activated and phosphorylated receptors. Interestingly, domain swapped chimeras of {beta}arrs display robust complementation in functional assays thereby, linking the structural differences between the receptor-bound {beta}arr1 and 2 with their divergent functional outcomes. Our findings reveal important insights into the ability of {beta}arr isoforms to drive distinct functional outcomes, and underscore the importance of integrating this aspect in the current framework of biased agonism.

biophysics↗

bioRxiv2019

Genetically encoded intrabody sensors illuminate structural and functional diversity in GPCR-β-arrestin complexes

Interaction of {beta}-arrestins ({beta}arrs) upon agonist-stimulation is a hallmark of G protein-coupled receptors (GPCRs) resulting in receptor desensitization, endocytosis and signaling. Although overall functional roles of {beta}arrs are typically believed to be conserved across different receptors, emerging data now clearly unveils receptor-specific functional contribution of {beta}arrs. The underlying mechanism however remains mostly speculative and represents a key missing link in our current understanding of GPCR signaling and regulatory paradigms. Here, we develop synthetic intrabody-based conformational sensors that help us visualize the assembly and trafficking of GPCR-{beta}arr1 complexes in cellular context for a broad set of receptors with spatio-temporal resolution. Surprisingly, these conformational sensors reveal a previously unappreciated level of diversity in GPCR-{beta}arr complexes that extends beyond the current framework of affinity-based classification and phosphorylation-code-based interaction patterns. More importantly, this conformational diversity arising from spatial signature of phosphorylation sites manifests directly in the form of distinct functional outcomes, including even opposite contribution of {beta}arrs in signal-transduction for different receptors. Taken together, these findings uncover that despite an overall similar interaction and trafficking patterns; critical structural and functional differences exist in {beta}arr complexes for different GPCRs that define and fine-tune receptor-specific downstream responses.

cell biology↗

bioRxiv2019

Partial ligand-receptor engagement yields functional bias at the human complement receptor, C5aR1

The human complement component, C5a, binds two different seven transmembrane receptors termed as C5aR1 and C5aR2. C5aR1 is a prototypical G protein-coupled receptor that couples to Gi sub-family of heterotrimeric G proteins and {beta}-arrestins ({beta}arr) following C5a stimulation. Peptide fragments derived from the carboxyl-terminus of C5a can still interact with the receptor, albeit with lower affinity, and can act as agonists or antagonists. However, whether such fragments might display ligand bias at C5aR1 remains unexplored. Here, we compare C5a and a modified C-terminal fragment of C5a, C5apep, in terms of G protein coupling, {beta}arr recruitment, endocytosis and ERK1/2 MAP kinase activation at the human C5aR1. We discover that C5apep acts as a full-agonist for G protein coupling, while only displaying partial agonism for {beta}arr recruitment. We also observe that whilst C5apep is significantly less efficient in inducing C5aR1 endocytosis compared to C5a, it exhibits robust activation of ERK1/2 phosphorylation at levels similar to C5a. Interestingly, C5apep displays full-agonist efficacy with respect to inhibiting LPS induced IL-6 secretion in human macrophages, but its ability to induce human neutrophil migration is substantially lower compared to C5a. Taken together, our findings reveal ligand-bias at C5aR1, not only with respect to transducer-coupling and receptor trafficking but also in terms of cellular responses. Our findings therefore establish a framework to explore additional levels of biased signaling and biased ligands at C5aR1 with therapeutic potential. More generally, our findings may be extended to discover biased ligands for the broad sub-family of chemokine GPCRs which also interact with chemokine ligands through a biphasic mechanism.

biochemistry↗