Journal Articles
- Role of melatonin in murine “restraint stress”-induced dysfunction of colonic microbiota
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Rutao Lin , Zixu Wang , Jing Cao , Ting Gao , Yulan Dong , Yaoxing Chen
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J. Microbiol. 2021;59(5):500-512. Published online February 25, 2021
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DOI: https://doi.org/10.1007/s12275-021-0305-7
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Abstract
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Intestinal diseases caused by physiological stress have become
a severe public health threat worldwide. Disturbances in the
gut microbiota-host relationship have been associated with
irritable bowel disease (IBD), while melatonin (MT) has antiinflammatory
and antioxidant effects. The objective of this
study was to investigate the mechanisms by which MT-mediated
protection mitigated stress-induced intestinal microbiota
dysbiosis and inflammation. We successfully established a
murine restraint stress model with and without MT supplementation.
Mice subjected to restraint stress had significantly
elevated corticosterone (CORT) levels, decreased MT levels
in their plasma, elevated colonic ROS levels and increased bacterial
abundance, including Bacteroides and Tyzzerella, in
their colon tract, which led to elevated expression of Toll-like
receptor (TLR) 2/4, p-P65 and p-IκB. In contrast, supplementation
with 20 mg/kg MT reversed the elevation of the plasma
CORT levels, downregulated the colon ROS levels and inhibited
the changes in the intestinal microbiota induced by
restraint stress. These effects, in turn, inhibited the activities
of TLR2 and TLR4, p-P65 and p-IκB, and decreased the inflammatory
reaction induced by restraint stress. Our results
suggested that MT may mitigate “restraint stress”-induced
colonic microbiota dysbiosis and intestinal inflammation by
inhibiting the activation of the NF-κB pathway.
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Citations
Citations to this article as recorded by

- Microbial melatonin metabolism in the human intestine as a therapeutic target for dysbiosis and rhythm disorders
Petra Zimmermann, Salome Kurth, Benoit Pugin, Nicholas A. Bokulich
npj Biofilms and Microbiomes.2024;[Epub] CrossRef - Toll-like receptor 4 plays a vital role in irritable bowel syndrome: a scoping review
Xuemeng Wan, Liyuan Wang, Zhiling Wang, Chaomin Wan
Frontiers in Immunology.2024;[Epub] CrossRef - Christensenella minuta mitigates behavioral and cardiometabolic hallmarks of social defeat stress
A. Agusti, GV. Molina-Mendoza, M. Tamayo, V. Rossini, MC. Cenit, C. Frances-Cuesta, V. Tolosa-Enguis, EM. Gómez Del Pulgar, A. Flor-Duro, Y. Sanz
Biomedicine & Pharmacotherapy.2024; 180: 117377. CrossRef - The impact of acute and chronic stress on gastrointestinal physiology and function: a microbiota–gut–brain axis perspective
Sarah‐Jane Leigh, Friederike Uhlig, Lars Wilmes, Paula Sanchez‐Diaz, Cassandra E. Gheorghe, Michael S. Goodson, Nancy Kelley‐Loughnane, Niall P. Hyland, John F. Cryan, Gerard Clarke
The Journal of Physiology.2023; 601(20): 4491. CrossRef - Melatonin as a Mediator of the Gut Microbiota–Host Interaction: Implications for Health and Disease
María-Ángeles Bonmatí-Carrión, Maria-Angeles Rol
Antioxidants.2023; 13(1): 34. CrossRef - INVESTIGATION OF THE ROLE OF STRESS IN MALE INFERTILITY AND THE EFFECT OF CURRENT MELATONIN HORMONE TREATMENTS
İshak GÖKÇEK, Leyla AYDIN
Veteriner Farmakoloji ve Toksikoloji Derneği Bülteni.2023; 14(1): 36. CrossRef - The double burden of malnutrition and environmental enteric dysfunction as potential factors affecting gut-derived melatonin in children under adverse environments
Alane N. Bezerra, Caroline L. Peixoto, Synara C. Lopes, Veralice M. S. Bruin, Pedro Felipe C. Bruin, Reinaldo B. Oriá
Frontiers in Nutrition.2023;[Epub] CrossRef - Melatonin: Both a Messenger of Darkness and a Participant in the Cellular Actions of Non-Visible Solar Radiation of Near Infrared Light
Dun-Xian Tan, Russel J. Reiter, Scott Zimmerman, Ruediger Hardeland
Biology.2023; 12(1): 89. CrossRef - Glucocorticoids coordinate the bladder peripheral clock and diurnal micturition pattern in mice
Ichiro Chihara, Hiromitsu Negoro, Jin Kono, Yoshiyuki Nagumo, Haruki Tsuchiya, Kosuke Kojo, Masanobu Shiga, Ken Tanaka, Shuya Kandori, Bryan J. Mathis, Hiroyuki Nishiyama
Communications Biology.2023;[Epub] CrossRef - The Microbiota-Dependent Worsening Effects of Melatonin on Gut Inflammation
Jefferson Luiz da Silva, Lia Vezenfard Barbosa, Camila Figueiredo Pinzan, Viviani Nardini, Irislene Simões Brigo, Cássia Aparecida Sebastião, Jefferson Elias-Oliveira, Vânia Brazão, José Clóvis do Prado Júnior, Daniela Carlos, Cristina Ribeiro de Barros C
Microorganisms.2023; 11(2): 460. CrossRef - The Effects of Stress and Diet on the “Brain–Gut” and “Gut–Brain” Pathways in Animal Models of Stress and Depression
Mauritz F. Herselman, Sheree Bailey, Larisa Bobrovskaya
International Journal of Molecular Sciences.2022; 23(4): 2013. CrossRef - Intestinal microbiota and melatonin in the treatment of secondary injury and complications after spinal cord injury
Yiwen Zhang, Rui Lang, Shunyu Guo, Xiaoqin Luo, Huiting Li, Cencen Liu, Wei Dong, Changshun Bao, Yang Yu
Frontiers in Neuroscience.2022;[Epub] CrossRef - Protective Effects and Mechanisms of Melatonin on Stress Myocardial Injury in Rats
Jia-yao Chen, Ting Li, Jiao-ling Wang, Zhan-le Wang, Yun Zhang, Lin-quan Zang
Journal of Cardiovascular Pharmacology.2022; 80(3): 417. CrossRef - Rescue of social deficits by early-life melatonin supplementation through modulation of gut microbiota in a murine model of autism
Xia Liu, Yi Cui, Yuhan Zhang, Guo Xiang, Meng Yu, Xianshu Wang, Bin Qiu, Xin-gang Li, Wei Liu, Di Zhang
Biomedicine & Pharmacotherapy.2022; 156: 113949. CrossRef - Roles of PRR-Mediated Signaling Pathways in the Regulation of Oxidative Stress and Inflammatory Diseases
Pengwei Li, Mingxian Chang
International Journal of Molecular Sciences.2021; 22(14): 7688. CrossRef
- Phosphorylation of tegument protein pp28 contributes to trafficking to the assembly compartment in human cytomegalovirus infection
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Jun-Young Seo , Jin Ah Heo , William J. Britt
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J. Microbiol. 2020;58(7):624-631. Published online June 27, 2020
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DOI: https://doi.org/10.1007/s12275-020-0263-5
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Abstract
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Human cytomegalovirus (HCMV) UL99 encodes a late tegument
protein pp28 that is essential for envelopment and
production of infectious virus. This protein is localized to
the endoplasmic reticulum-Golgi intermediate compartment
(ERGIC) in transfected cells but it localizes to the cytoplasmic
assembly compartment (AC) in HCMV-infected cells. Trafficking
of pp28 to the AC is required for the assembly of infectious
virus. The N-terminal domain (aa 1-61) of pp28 is
sufficient for trafficking and function of the wild type protein
during viral infection. However, residues required for
authentic pp28 trafficking with the exception of the acidic
cluster in the N-terminal domain of pp28 remain undefined.
Monitoring protein migration on SDS-PAGE, we found that
pp28 is phosphorylated in the virus-infected cells and dephosphorylated
in the viral particles. By generating substitution
mutants of pp28, we showed that three serine residues
(aa 41–43) and a tyrosine residue (aa 34) account for its phosphorylation.
The mutant forms of pp28 were localized to the
plasma membrane as well as the ERGIC in transfected cells.
Likewise, these mutant proteins were localized to the plasma
membrane as well as the AC in virus-infected cells. These results
suggested that phosphorylation of pp28 contributes to
its intracellular trafficking and efficient viral assembly and
incorporation.
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Citations
Citations to this article as recorded by

- Exploring the genetic associations and causal relationships between antibody responses, immune cells, and various types of breast cancer
Yang Yang, Jiayi Chen, Fuhong Gong, Jingge Miao, Mengping Lin, Ruimin Liu, Chenxi Wang, Fei Ge, Wenlin Chen
Scientific Reports.2024;[Epub] CrossRef - Human cytomegalovirus induces significant structural and functional changes in terminally differentiated human cortical neurons
Jacob W. Adelman, Suzette Rosas-Rogers, Megan L. Schumacher, Rebekah L. Mokry, Scott S. Terhune, Allison D. Ebert, Thomas Shenk
mBio.2023;[Epub] CrossRef - Insights into the Transcriptome of Human Cytomegalovirus: A Comprehensive Review
Janine Zeng, Di Cao, Shaomin Yang, Dabbu Kumar Jaijyan, Xiaolian Liu, Songbin Wu, Ruth Cruz-Cosme, Qiyi Tang, Hua Zhu
Viruses.2023; 15(8): 1703. CrossRef - Features and Functions of the Conserved Herpesvirus Tegument Protein UL11 and Its Binding Partners
Linjiang Yang, Mingshu Wang, Anchun Cheng, Qiao Yang, Ying Wu, Juan Huang, Bin Tian, Renyong Jia, Mafeng Liu, Dekang Zhu, Shun Chen, Xinxin Zhao, Shaqiu Zhang, Xumin Ou, Sai Mao, Qun Gao, Di Sun
Frontiers in Microbiology.2022;[Epub] CrossRef - The human cytomegalovirus decathlon: Ten critical replication events provide opportunities for restriction
Declan L. Turner, Rommel A. Mathias
Frontiers in Cell and Developmental Biology.2022;[Epub] CrossRef
Research Support, Non-U.S. Gov't
- Rescue of a Cold-Sensitive Mutant at Low Temperatures by Cold Shock Proteins from Polaribacter irgensii KOPRI 22228
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Ji-hyun Uh , Youn Hong Jung , Yoo Kyung Lee , Hong Kum Lee , Hana Im
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J. Microbiol. 2010;48(6):798-802. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0402-5
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Abstract
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Exposure to low temperatures induces the biosynthesis of specific sets of proteins, including cold shock proteins (Csps). Since many of the specific functions of pychrophilic Csps are unknown, the roles of Csps from an Arctic bacterium, Polaribacter irgensii KOPRI 22228, were examined. The genes encoding CspA and
CspC of P. irgensii were cloned in this study. Sequence analysis showed that these proteins have cold shock domains containing two RNA-binding motifs, RNP1 and RNP2. Both proteins bound oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. When the P. irgensii Csps were overexpressed in Escherichia coli, the cold-resistance of the host was increased by more than five-fold. The P. irgensii Csps also rescued a cold-sensitive E. coli csp-quadruple deletion strain, BX04, at low temperatures. These results
suggest that Csps from P. irgensii play a role in survival in polar environments.
- Purification and Characterization of Cold Active Lipase from Psychrotrophic Aeromonas sp. LPB 4
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Han-Ki Lee , Min-Jung Ahn , Sung-Ho Kwak , Won-Ho Song , Byeong-Chul Jeong
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J. Microbiol. 2003;41(1):22-27.
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Abstract
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A lipase from Aeromonas sp. LPB 4, a psychrotophile isolated from a sea sediment was purified and characterized. The lipase was purified 53.5 fold to a homogeneous state by acetone precipitation and QAE sephadex column chromatography and its molecular weight was determined to be 50 kDa by SDS-PAGE. The enzyme exhibited maximum activity at 10oC and was stable at temperatures lower than 50℃. This lipase favored substrates containing medium carbon chain of acyl group, while too low and high carbon chain decreased its activity. The lipolytic activity of purified lipase was slightly increased by the addition of 0.1% detergent, but decreased by 1% of detergent. Butanol severely decreased the lipase activity while methanol increased the activity about 15%.