<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Tellis, Meenakshi B.</style></author><author><style face="normal" font="default" size="100%">Chaudhari, Bhagyashri Y.</style></author><author><style face="normal" font="default" size="100%">Deshpande, Shweta V.</style></author><author><style face="normal" font="default" size="100%">Nikam, Sanika V.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Kotkar, Hemlata M.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Trehalose transporter-like gene diversity and dynamics enhances stress response and recovery in Helicoverpa armigera</style></title><secondary-title><style face="normal" font="default" size="100%">Gene</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Gene expression</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Stress</style></keyword><keyword><style  face="normal" font="default" size="100%">Transporter-like</style></keyword><keyword><style  face="normal" font="default" size="100%">trehalose</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">862</style></volume><pages><style face="normal" font="default" size="100%">147259</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.913&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kallure, Gopal S.</style></author><author><style face="normal" font="default" size="100%">Sahoo, Shubhranshu Shekhar</style></author><author><style face="normal" font="default" size="100%">Kale, Rutuja S.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Kontham, Ravindar</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Aminoacylase efficiently hydrolyses fatty acid amino acid conjugates of Helicoverpa armigera potentially to increase the pool of glutamine</style></title><secondary-title><style face="normal" font="default" size="100%">Insect Biochemistry and Molecular Biology </style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aminoacylase</style></keyword><keyword><style  face="normal" font="default" size="100%">Fatty acid amino acid conjugates</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutamine</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Oral secretion</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">165</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.8&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Patil, Yogita P.</style></author><author><style face="normal" font="default" size="100%">Wagh, Deepti S.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Gawari, Shyam K.</style></author><author><style face="normal" font="default" size="100%">Pisalwar, Priyanka D.</style></author><author><style face="normal" font="default" size="100%">Ahmed, Shadab</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Altered Octopamine synthesis impairs tyrosine metabolism affecting Helicoverpa armigera vitality</style></title><secondary-title><style face="normal" font="default" size="100%">Pesticide Biochemistry and Physiology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Octopamine biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Tomatidine</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyramine (1-hydroxylase (HaT(1H)</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine metabolic pathway</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">208</style></volume><pages><style face="normal" font="default" size="100%">106323</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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'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.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	4.2&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Joshi, Kaumudi S.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Hadapad, Ashok B.</style></author><author><style face="normal" font="default" size="100%">Hire, Ramesh S.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">LDH-dsRNA nanocarrier-mediated spray-induced silencing of juvenile hormone degradation pathway genes for targeted control of Helicoverpa armigera</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Development</style></keyword><keyword><style  face="normal" font="default" size="100%">dsRNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Juvenile hormone</style></keyword><keyword><style  face="normal" font="default" size="100%">Layered double hydroxide</style></keyword><keyword><style  face="normal" font="default" size="100%">Nanocarrier</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">332</style></volume><pages><style face="normal" font="default" size="100%">148673</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Helicoverpa armigera, a devastating agricultural pest, poses significant threats to global crop productivity. Targeting the Juvenile Hormone (JH) degradation pathway may offer a promising approach for pest management, given its pivotal role in insect development and reproduction. In this study, we developed a nanoclay-based formulation of double-stranded RNA (dsRNA) targeting three key JH degradation pathway genes: Juvenile Hormone Esterase (HaJHE), Juvenile Hormone Epoxy Hydrolase (HaJHEH), and Juvenile Hormone Diol Kinase (HaJHDK). Expression analysis revealed tissue and stage-specific patterns of these genes, with qRT-PCR confirming high expression levels of specific isoforms in key developmental transition: the pre-pupal stage. Treatment with bacterially expressed dsRNAs achieved &amp;gt;50 % silencing of target genes, resulting in delay in larval-to-pupal transitions. Bioassay demonstrated that treatment with LDH-based dsRNA nanocarrier resulted in downregulation of target genes, causing developmental delays, including prolonged larval and pupal stages. Metabolomic analysis further indicated reduced accumulation of JH degradation pathway metabolites, highlighting the pathway-specific action of dsRNAs. Furthermore, combinatorial application of dsRNAs resulted in higher mortalities compared to individual dsRNA application. These results suggest that the application of the LDH-based dsRNA nanocarrier formulation against H. armigera JH degradation pathway for spray-induced gene silencing could serve as a potential insect management strategy.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	5.2&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chaudhari, Bhagyashri Y.</style></author><author><style face="normal" font="default" size="100%">Nichit, Vikram J.</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mechanistic insights in the role of trehalose transporter in metabolic homeostasis in response to dietary trehalose</style></title><secondary-title><style face="normal" font="default" size="100%">G3-Genes Genomes Genetics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">gut</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">sugar uptake</style></keyword><keyword><style  face="normal" font="default" size="100%">transporters</style></keyword><keyword><style  face="normal" font="default" size="100%">trehalose</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">16</style></volume><pages><style face="normal" font="default" size="100%">jkaf303</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Trehalose is the major sugar in insect hemolymph and plays a diverse role. Its level is regulated by the dynamics of biosynthesis and distribution by sugar transporters. The metabolic balance between trehalose synthesis and uptake remains poorly understood, despite its critical role in homeostasis. Here, we examined the role of the putative gut-specific sugar transporter, HaST46, in regulating trehalose levels in Helicoverpa armigera, a model Lepidopteran pest. Analysis of publicly available transcriptomics, proteomics data, and qRT-PCR study suggests that HaST46 showed localization in the posterior midgut and its expression alters in response to dietary contents. The liquid chromatography-mass spectrometry (LC-MS) analysis of HaST46 overexpressing Sf9 cells indicated that trehalose transport is preferred over glucose. HaST46 expression was found to be modulated tissue-specific manner in response to dietary trehalose availability. Furthermore, trehalose synthesis genes were found to be downregulated in the case of a 50 mM trehalose diet. This suggests that a potential increase in exogenous trehalose uptake may attenuate its endogenous synthesis. HaST46 overexpression and silencing lead to altered trehalose levels in the insect, while also having impact on trehalose metabolizing enzymes. Overall, our findings reveal the role of gut predominant sugar transporter, HaST46, in metabolic fine-tuning between exogenous trehalose uptake and endogenous synthesis.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	4.3&lt;/p&gt;
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