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Keywords = Pleurotus salmoneostramineus

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22 pages, 2518 KiB  
Article
Anticancer Effects of Pleurotus salmoneostramineus Protein Hydrolysate on HepG2 Cells and In Silico Characterization of Structural Effects of Chromoprotein-Derived Peptides on the Mitochondrial Uncoupling Protein 2 (UCP2)
by Erica K. Ventura-García, Mónica A. Valdez-Solana, Claudia Avitia-Domínguez, Guadalupe García-Arenas, Alfredo Téllez-Valencia, Nagamani Balagurusamy and Erick Sierra-Campos
BioMedInformatics 2025, 5(2), 29; https://doi.org/10.3390/biomedinformatics5020029 - 26 May 2025
Viewed by 1598
Abstract
Background: Pleurotus salmoneostramineus is acknowledged as a reliable source of high-quality protein, with its protein concentrates, hydrolysates, and peptides potentially offering health benefits to humans. However, studies validating the medicinal effects of P. salmoneostramineus proteins, particularly the pink chromoprotein, are currently absent. [...] Read more.
Background: Pleurotus salmoneostramineus is acknowledged as a reliable source of high-quality protein, with its protein concentrates, hydrolysates, and peptides potentially offering health benefits to humans. However, studies validating the medicinal effects of P. salmoneostramineus proteins, particularly the pink chromoprotein, are currently absent. Methods: This study explores anticancer peptides from the chromoprotein of P. salmoneostramineus, evaluating their ability to bind UCP2 via in silico analysis. Additionally, it assesses the protein hydrolysate from P. salmoneostramineus (PSPs) effect on HepG2 cell proliferation and mitochondrial metabolism, focusing on uncoupling protein activity. Results: Eight peptides were identified as potential UCP2 inhibitors. According to mACPpred2.0 and CSM-peptides servers, the peptides TSMQSSL, QEGQKL, SEDSGEA, and GRNSL exhibit promising anticancer properties. These anticancer peptides yielded the following docking scores (kcal/mol) when tested against UCP2: TSMQSSL (−166.75), QEGQKL (−126.06), SEDSGEA (−99.93), and GRNSL (−137.93). Molecular dynamics simulations have shown that the peptides establish stable interactions with UCP2 through salt bridges, hydrophobic interactions, and hydrogen bonds, implying that hydrogen bonding with RRR88 and FVW92 causes conformational changes in UCP2. Moreover, the outcomes of this study indicated that PSPs possess an antiproliferative effect on HepG2 cells and lower mitochondrial bioenergetics, especially UCP2 activity. Conclusions: These findings suggest that peptides from P.salmoneostramineus can inhibit UCP2, offering a promising approach for cancer prevention, playing therapeutic roles in treatment, and providing a basis for designing peptide-based cancer therapies. Full article
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11 pages, 2173 KiB  
Article
Oyster Mushroom Spherical Virus Crosses the Species Barrier and Is Pathogenic to a New Host Pleurotus pulmonarius
by Xiaoyan Zhang, Haijing Hu, Yanxiang Zhao, Yifan Wang, Wenjing Zhang, Lunhe You, Jianrui Wang, Yu Liu and Xianhao Cheng
Int. J. Mol. Sci. 2023, 24(13), 10584; https://doi.org/10.3390/ijms241310584 - 24 Jun 2023
Cited by 3 | Viewed by 2329
Abstract
Oyster mushroom spherical virus (OMSV) is a mycovirus with a positive-sense single-stranded RNA genome that infects the edible mushroom Pleurotus ostreatus. OMSV is horizontally transferred from an infected strain to a cured strain via mycelia. The infection results in significant inhibition of [...] Read more.
Oyster mushroom spherical virus (OMSV) is a mycovirus with a positive-sense single-stranded RNA genome that infects the edible mushroom Pleurotus ostreatus. OMSV is horizontally transferred from an infected strain to a cured strain via mycelia. The infection results in significant inhibition of mycelial growth, malformation of fruiting bodies, and yield loss in oyster mushrooms. This study successfully transferred OMSV from P. ostreatus to Pleurotus pulmonarius. However, transmission was not successful in other Pleurotus species including P. citrinopileatus, P. eryngii, P. nebrodensis, and P. salmoneostramineus. The successful OMSV infection in P. pulmonarius was further verified with Western blot analysis using a newly prepared polyclonal antiserum against the OMSV coat protein. Furthermore, OMSV infection reduced the mycelial growth rate of P. pulmonarius. The OMSV-infected strain demonstrated abnormal performance including twisted mushrooms or irregular edge of the cap as well as reduced yield of fruiting bodies in P. pulmonarius, compared to the OMSV-free strain. This study is the first report on the infection and pathogenicity of OMSV to the new host P. pulmonarius. The data from this study therefore suggest that OMSV is a potential threat to P. pulmonarius. Full article
(This article belongs to the Collection Microbial Virulence Factors)
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