<?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%">Pathak, Gauri M.</style></author><author><style face="normal" font="default" size="100%">Gurjar, Gayatri S.</style></author><author><style face="normal" font="default" size="100%">Kadoo, Narendra Y.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Insights of Bipolaris sorokinianasecretome-anin silicoapproach</style></title><secondary-title><style face="normal" font="default" size="100%">Biologia</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cochliobolus sativus</style></keyword><keyword><style  face="normal" font="default" size="100%">pathogenesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Phytopathogenic fungi</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretory proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</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%">75</style></volume><pages><style face="normal" font="default" size="100%">2367-2381</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The plant pathogen,Bipolaris sorokiniana(teleomorph:Cochliobolus sativus), is of global concern as it attacks many economically important cereals and grasses. During the infection process, phytopathogenic fungi are known to secrete a variety of proteins collectively known as the secretome, analyzing which can help in deciphering the mechanism of fungal pathogenesis. In this study, we performedin silicosecretome analysis ofC. sativusstrain ND90Pr using established secretome prediction pipeline involving software tools such as SignalP, TargetP, TMHMM, big-PI Fungal Predictor, ProtComp, and WoLF PSORT. Using these software and other prediction criteria, we identified 196 probable secretory proteins from theB. sorokinianaproteome. Characterization of the predicted secretome revealed proteins that may have probable functions in degradation of the plant cell wall, lipids, proteins, and nucleic acids, as well as in pathogenesis and metabolism. Further, the PHI-base analysis identified 38 proteins having a possible role in pathogenicity and virulence. This study helped to predict the composition of the secretome ofB. sorokinianaand extrapolate its role in plant infection and pathogen survival. It may provide clues for developing new control strategies targeting the vital fungal secretory proteins.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">12</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;0.811&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%">Gupta, Lovely</style></author><author><style face="normal" font="default" size="100%">Sen, Pooja</style></author><author><style face="normal" font="default" size="100%">Bhattacharya, Asish K.</style></author><author><style face="normal" font="default" size="100%">Vijayaraghavan, Pooja</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Isoeugenol affects expression pattern of conidial hydrophobin gene RodA and transcriptional regulators MedA and SomA responsible for adherence and biofilm formation in Aspergillus fumigatus</style></title><secondary-title><style face="normal" font="default" size="100%">Archives of Microbiology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aspergillus fumigatus</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrophobicity</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoeugenol</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription regulators</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</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%">204</style></volume><pages><style face="normal" font="default" size="100%">214</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Aspergillus fumigatus is one of the major pathogenic fungal species, causing life-threatening infections. Due to a limited spectrum of available antifungals, exploration of new drug targets as well as potential antifungal molecules has become pertinent. Rodlet layer plays an important role in adherence of fungal conidia to hydrophobic cell surfaces in host, which also leads to A. fumigatus biofilm formation, contributing factor to fungal pathogenicity. From decades, natural sources have been known for the development of new active molecules. The present study investigates effect of isoeugenol on genes responsible for hydrophobins (RodA), adhesion as well as biofilm formation (MedA and SomA) of A. fumigatus. Minimum inhibitory concentrations (MIC and IC50) of isoeugenol against A. fumigatus were determined using broth microdilution assay. The IC50 results showed reduced hydrophobicity and biofilm formation as well as eradication after treatment with the compound and electron micrograph data corroborated these findings. The qRT-PCR showed a significant downregulation of genes RodA, MedA, SomA and pksP involved in hydrophobicity and biofilm formation. SwissADME studies potentiated drug-like propensity for isoeugenol which formed four hydrogen bonds with low binding energy (- 4.54 kcal/mol) at the catalytic site of RodA protein studied via AutoDock4. Hence, the findings conclude that isoeugenol inhibits conidial hydrophobicity and biofilm formation of A. fumigatus and further investigations are warranted in this direction.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</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;
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	2.667&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%">Kumaravel, Nalayeni</style></author><author><style face="normal" font="default" size="100%">Ebinezer, Leonard Barnabas</style></author><author><style face="normal" font="default" size="100%">Ashwin, N. M. R.</style></author><author><style face="normal" font="default" size="100%">Franchin, Cinzia</style></author><author><style face="normal" font="default" size="100%">Battisti, Ilaria</style></author><author><style face="normal" font="default" size="100%">Carletti, Paolo</style></author><author><style face="normal" font="default" size="100%">Sundar, Amalraj Ramesh</style></author><author><style face="normal" font="default" size="100%">Masi, Antonio</style></author><author><style face="normal" font="default" size="100%">Malathi, Palaniyandi</style></author><author><style face="normal" font="default" size="100%">Viswanathan, Rasappa</style></author><author><style face="normal" font="default" size="100%">Arrigoni, Giorgio</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparative proteomics of sugarcane smut fungus- Sporisorium scitamineum unravels dynamic proteomic alterations during the dimorphic transition</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Proteomics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">fungi</style></keyword><keyword><style  face="normal" font="default" size="100%">iTRAQ</style></keyword><keyword><style  face="normal" font="default" size="100%">Smut</style></keyword><keyword><style  face="normal" font="default" size="100%">Sugarcane</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</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%">JUL </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">304</style></volume><pages><style face="normal" font="default" size="100%">105230</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Life cycle of the dimorphic sugarcane smut fungi, Sporisorium scitamineum , involves recognition and mating of compatible saprophytic yeast -like haploid sporidia (MAT -1 and MAT -2) that upon fusion, develop into infective dikaryotic mycelia. Although the dimorphic transition is intrinsically linked with the pathogenicity and virulence of S. scitamineum , it has never been studied using a proteomic approach. In the present study, an iTRAQ-based comparative proteomic analysis of three distinct stages was carried out. The stages were: the dimorphic transition period - haploid sporidial stage (MAT -1 and MAT -2); the transition phase (24 h post co -culturing (hpc)) and the dikaryotic mycelial stage (48 hpc). Functional categorization of differentially abundant proteins showed that the most altered biological processes were energy production, primary metabolism, especially, carbohydrate, amino acid, fatty acid, followed by translation, post -translation and protein turnover. Several differentially abundant proteins (DAPs), especially in the dikaryotic mycelial stage were predicted as effectors. Taken together, key molecular mechanisms underpinning the dimorphic transition in S. scitamineum at the proteome level were highlighted. The catalogue of stage -specific and dimorphic transition -associated -proteins and potential effectors identified herein represents a list of potential candidates for defective mutant screening to elucidate their functional role in the dimorphic transition and pathogenicity in S. scitamineum . Biological significance: Being the first comparative proteomics analysis of S. scitamineum , this study comprehensively examined three pivotal life cycle stages of the pathogen: the non-pathogenic haploid phase, the transition phase, and the pathogenic dikaryotic mycelial stage. While previous studies have reported the sugarcane and S. scitamineum interactions, this study endeavored to specifically identify the proteins responsible for pathogenicity. By analyzing the proteomic alterations between the haploid and dikaryotic mycelial phases, the study revealed significant changes in metabolic pathway -associated proteins linked to energy production, notably oxidative phosphorylation, and the citrate cycle. Furthermore, this study successfully identified key metabolic pathways that undergo reprogramming during the transition from the non-pathogenic to the pathogenic stage. The study also deciphered the underlying mechanisms driving the morphological and physiological alterations crucial for the S. scitamineum virulence. By studying its life cycle stages, identifying the key metabolic pathways and stage -specific proteins, it provides unprecedented insights into the pathogenicity and potential avenues for intervention. As proteomics continues to advance, such studies pave the way for a deeper understanding of plantpathogen interactions and the development of innovative strategies to mitigate the impact of devastating pathogens like S. scitamineum.&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;
	2.8&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%">Gupta, Lovely</style></author><author><style face="normal" font="default" size="100%">Verma, Shalini</style></author><author><style face="normal" font="default" size="100%">Goswami, Lakshmi</style></author><author><style face="normal" font="default" size="100%">Kamboj, Himanshu</style></author><author><style face="normal" font="default" size="100%">Sen, Pooja</style></author><author><style face="normal" font="default" size="100%">Bhattacharya, Asish K.</style></author><author><style face="normal" font="default" size="100%">Vijayaraghavan, Pooja</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Unveiling the cell wall-targeting mechanisms and multifaceted virulence modulation by a eugenol glycoconjugate against aspergillus fumigatus: insights from in vitro and in ovo studies</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Applied Macrobiology </style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aspergillus fumigatus</style></keyword><keyword><style  face="normal" font="default" size="100%">cell wall integrity</style></keyword><keyword><style  face="normal" font="default" size="100%">Eugenol</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoconjugate</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription regulators</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</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%">JAN </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">135</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Aim The primary objective of this study was to elucidate the putative cell wall-associated targets of compound 6i, a glycoconjugate of eugenol, in Aspergillus fumigatus, while also evaluating its toxicity and assessing histopathologic alterations in the liver, heart, and kidney of compound 6i-treated embryos using an in ovo model.Method To achieve this aim, compound 6i was synthesized, and a series of biochemical assays were performed to determine its impact on the fungal cell wall. Additionally, quantitative real time-PCR and liquid chromatography-mass spectrometry/mass spectrometry analyses were conducted to investigate changes in gene and protein expression profiles associated with melanin biosynthesis, conidiation, siderophore production, transcriptional regulation of beta-glucan biosynthesis, and calcineurin activity in A. fumigatus.Results The experimental findings revealed that compound 6i exhibited notable antifungal activity against A. fumigatus by perturbing cell wall integrity, hindering ergosterol, glucan, and chitin biosynthesis, and inhibiting catalase production. Moreover, relative gene expression and proteomic analyses demonstrated that compound 6i exerted both downregulatory and upregulatory effects on several crucial genes and proteins involved in the aforementioned fungal processes. Furthermore, increased expression of oxidative stress-related proteins was observed in the presence of compound 6i. Notably, the glycoconjugate of eugenol did not elicit cytotoxicity in the liver, heart, and kidney of chick embryos.Conclusion The current investigation elucidated the multifaceted mechanisms by which compound 6i exerts its antifungal effects against A. fumigatus, primarily through targeting cell wall components and signaling pathways. These findings underscore the potential of the eugenol glycoconjugate as a promising antifungal candidate, warranting further exploration and development for combating A. fumigatus infections.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</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&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%">Sen, Pooja</style></author><author><style face="normal" font="default" size="100%">Gupta, Lovely</style></author><author><style face="normal" font="default" size="100%">Chauhan, Aastha</style></author><author><style face="normal" font="default" size="100%">Goswami, Lakshmi</style></author><author><style face="normal" font="default" size="100%">Bhattacharya, Asish K.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Abhishek</style></author><author><style face="normal" font="default" size="100%">Vijayaraghavan, Pooja</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comprehensive in vitro and in silico assessment of eugenol glycoconjugates against azole and amphotericin B resistant Rhizopus spp.</style></title><secondary-title><style face="normal" font="default" size="100%">Molecular Biology Reports</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Antifungals</style></keyword><keyword><style  face="normal" font="default" size="100%">Eugenol</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoconjugates</style></keyword><keyword><style  face="normal" font="default" size="100%">Mucormycosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Resistance</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</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%">JUN </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">52</style></volume><pages><style face="normal" font="default" size="100%">589</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Background Rhizopus spp. is a major cause of mucormycosis, a severe infectious disease with high morbidity and mortality. Treatment is challenging due to rising antifungal resistance. Glycosylation is a crucial technique for enhancing the properties of phenolic compounds like eugenol. The present study aims to examine the antifungal efficacy of eugenol glycoconjugates against azole and amphotericin B-resistant Rhizopus isolates. Methods and results Out of 50 soil samples, 12 isolates belonging to Mucorales were obtained, of which 7 were identified as Rhizopus spp. via 18S ITS sequencing. Antifungal susceptibility testing (AST) revealed that all Rhizopus isolates were resistant to amphotericin B (MIC &amp;gt; 1 mu g/mL). Most isolates also showed resistance towards posaconazole (MIC &amp;gt; 1 mu g/mL) and itraconazole (MIC &amp;gt; 2 mu g/mL). AST of eugenol glycoconjugate (coded 6g) showed efficacy against resistant Rhizopus isolates, with MIC values ranging from 6.25 mu g/mL to 25 mu g/mL. Flow cytometry confirmed its fungicidal activity, correlating with MIC data. Compound 6g significantly reduced conidial germination within 24 h and exhibited no cytotoxicity on A549 lung cancer cells. In-silico analysis revealed a negative binding affinity of compound 6g for the spore coat protein CotH3, which could be a potential antifungal target. Conclusion Compound 6g could be an potential antifungal molecule against resistant Rhizopus spp, which requires further studies.&lt;/p&gt;
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	2.8&lt;/p&gt;
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