@article {48306, title = {Trehalose transporter-like gene diversity and dynamics enhances stress response and recovery in Helicoverpa armigera}, journal = {Gene}, volume = {862}, year = {2023}, month = {APR}, pages = {147259}, type = {Article}, abstract = {

Trehalose is a primary sugar and its distribution across the insect body, regulated by trehalose transporters (TRETs), is essential for sugar metabolism and energy homeostasis. The large diversity of Tret-like sugar trans-porters (ST), belonging to SLC2A transporter family, in polyphagous insects probably contributes to their extremely adaptive nature. We aim to study spatio-temporal expression dynamics and functional relevance of ST transcript variants in the lepidopteran model organism, Helicoverpa armigera. Identification of 69 putative Tret-like HaST transcript variants from databases and their digital gene expression analysis indicated tissue and development-specific expression patterns. Phylogenetic and sequence similarity network analysis of HaSTs signify evolutionary divergence, while motif and structure analysis depicted conserved signatures. In vitro gene expression validation for selected genes depicts that HaST09 and 69 are fat body and haemolymph-specific. While, HaST06, 30, 36 and 57 are developmental stage or sex-specific. HaST69 has high expression in the haemolymph of fifth instar larvae. In the presence of trehalose metabolism inhibitors and abiotic stress, HaSTs expression show dysregulation, indicating their possible association with trehalose metabolism and stress re-covery. In vivo gene silencing of HaST69 resulted in reduced trehalose accumulation in the insect body, sug-gesting its plausible role in sugar metabolism. The overall understanding of HaST diversity and expression dynamics highlights their putative roles in sugar transport during adaptation and stress recovery of insects.

}, keywords = {Gene expression, Helicoverpa armigera, Stress, Transporter-like, trehalose}, issn = {0378-1119}, doi = {10.1016/j.gene.2023.147259}, author = {Tellis, Meenakshi B. and Chaudhari, Bhagyashri Y. and Deshpande, Shweta V. and Nikam, Sanika V. and Barvkar, Vitthal T. and Kotkar, Hemlata M. and Joshi, Rakesh S.} } @article {49076, title = {Aminoacylase efficiently hydrolyses fatty acid amino acid conjugates of Helicoverpa armigera potentially to increase the pool of glutamine}, journal = {Insect Biochemistry and Molecular Biology }, volume = {165}, year = {2024}, month = {FEB}, type = {Article}, abstract = {

One of the most prevalent bioactive molecules present in the oral secretion (OS) of lepidopteran insects is fatty acid amino acid conjugates (FACs). Insect dietary components have influence on the synthesis and retaining the pool of FACs in the OS. We noted differential and diet-specific accumulation of FACs in the OS of Helicoverpa armigera by using Liquid Chromatography-Quadrupole Time of Flight Mass Spectrometry. Interestingly, we identified FACs hydrolyzing enzyme aminoacylase (HaACY) in the OS of H. armigera through proteomic analysis. Next, we have cloned, expressed, and purified active recombinant HaACY in the bacterial system. Recombinant HaACY hydrolyzes all the six identified FACs in the OS of H. armigera larvae fed on host and non-host plants and releases respective fatty acid and glutamine. In these six FACs, fatty acid moieties vary while amino acid glutamine was common. Glutamine obtained upon hydrolysis of FACs by HaACY might serve as an amino acid pool for insect growth and development. To understand the substrate choices of HaACY, we chemically synthesized, purified, and characterized all the six FACs. Interestingly, rHaACY also shows hydrolysis of synthetic FACs into respective fatty acid and glutamine. Our results underline the importance of diet on accumulation of FACs and role of aminoacylase(s) in regulating the level of FACs and glutamine.

}, keywords = {Aminoacylase, Fatty acid amino acid conjugates, Glutamine, Helicoverpa armigera, Oral secretion}, issn = {0965-1748}, doi = {10.1016/j.ibmb.2024.104070}, author = {Kallure, Gopal S. and Sahoo, Shubhranshu Shekhar and Kale, Rutuja S. and Barvkar, Vitthal T. and Kontham, Ravindar and Giri, Ashok P.} } @article {49566, title = {Altered Octopamine synthesis impairs tyrosine metabolism affecting Helicoverpa armigera vitality}, journal = {Pesticide Biochemistry and Physiology}, volume = {208}, year = {2025}, month = {MAR}, pages = {106323}, type = {Article}, abstract = {

Tyramine (1-hydroxylase (T(1H) is a key enzyme in the biosynthesis of octopamine (OA), a vital neurohormone in invertebrates. This study explores the expression patterns and functional role of Helicoverpa armigera T(1H (HaT(1H) across various tissues and developmental stages. HaT(1H expression was highest in the head and adult male stages, reflecting tissue-specific and developmental regulation. HaT(1H silencing significantly increased locomotion and decreased feeding behavior. OA supplementation in silenced insects or HaT(1H overexpression showed a contrary effect on locomotory and feeding behavior. In silico screening and inhibitory assays identified tomatidine, a tomato-derived metabolite, as a potent HaT beta H inhibitor with strong binding affinity. In vivo bioassays confirmed tomatidine{\textquoteright}s inhibitory effects, reducing feeding and increasing mortality in H. armigera. Modulation in HaT(1H expression or activity disturbs the tyrosine metabolic pathway, with altered levels of tyramine, octopamine, and dopamine. These results highlight HaT(1H as a key regulator of OA biosynthesis, influencing insect feeding, locomotion, and overall survival. The present study also introduces tomatidine as a potential candidate for insect control, given its ability to disrupt HaT beta H function. This work provides new insights into the physiological roles of HaT beta H and offers promising avenues for developing targeted pest management strategies.

}, keywords = {Helicoverpa armigera, Octopamine biosynthesis, Tomatidine, Tyramine (1-hydroxylase (HaT(1H), Tyrosine metabolic pathway}, issn = {0048-3575}, doi = {10.1016/j.pestbp.2025.106323}, author = {Patil, Yogita P. and Wagh, Deepti S. and Barvkar, Vitthal T. and Gawari, Shyam K. and Pisalwar, Priyanka D. and Ahmed, Shadab and Joshi, Rakesh S.} }