Journal of Microbiology

Journal Article

Alpha‑Hemolysin from Staphylococcus aureus Obstructs Yeast‑Hyphae Switching and Diminishes Pathogenicity in Candida albicans: Xiaoyu Yu , Yinhe Mao , Guangbo Li , Xianwei Wu , Qiankun Xuan , Simin Yang , Xiaoqing Chen , Qi Cao , Jian Guo , Jinhu Guo , Wenjuan Wu; J. Microbiol. 2023;61(2):233-243. Published online February 9, 2023; DOI: https://doi.org/10.1007/s12275-022-00006-4

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The use of antibiotics can disrupt the body’s natural balance and increase the susteptibility of patients towards fungal infections. Candida albicans is a dimorphic opportunistic fungal pathogen with niches similar to those of bacteria. Our aim was to study the interaction between this pathogen and bacteria to facilitate the control of C. albicans infection. Alpha-hemolysin (Hla), a protein secreted from Staphylococcus aureus, causes cell wall damage and impedes the yeast–hyphae transition in C. albicans. Mechanistically, Hla stimulation triggered the formation of reactive oxygen species that damaged the cell wall and mitochondria of C. albicans. The cell cycle was arrested in the G0/G1 phase, CDC42 was downregulated, and Ywp1 was upregulated, disrupting yeast hyphae switching. Subsequently, hyphae development was inhibited. In mouse models, C. albicans pretreated with Hla reduced the C. albicans burden in skin and vaginal mucosal infections, suggesting that S. aureus Hla can inhibit hyphal development and reduce the pathogenicity of candidiasis in vivo.

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Candida albicans and Candida glabrata : global priority pathogens
Myrto Katsipoulaki, Mark H. T. Stappers, Dhara Malavia-Jones, Sascha Brunke, Bernhard Hube, Neil A. R. Gow, Joseph Heitman
Microbiology and Molecular Biology Reviews.2024;[Epub] CrossRef

Review

MINIREVIEW] Multilayered regulations of RIG-I in the anti-viral signaling pathway: Nari Kim , Hesung Now , Nhung T.H. Nguyen , Joo-Yeon Yoo; J. Microbiol. 2016;54(9):583-587. Published online August 31, 2016; DOI: https://doi.org/10.1007/s12275-016-6322-2

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Abstract

RIG-I is a cytosolic receptor recognizing virus-specific RNA structures and initiates an antiviral signaling that induces the production of interferons and proinflammatory cytokines. Because inappropriate RIG-I signaling affects either viral clearance or immune toxicity, multiple regulations of RIG-I have been investigated since its discovery as the viral RNA detector. In this review, we describe the recent progress in research on the regulation of RIG-I activity or abundance. Specifically, we focus on the mechanism that modulates RIGI- dependent antiviral response through post-translational modifications of or protein-protein interactions with RIG-I.

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Military Medical Research.2024;[Epub] CrossRef
ZNF205 positively regulates RLR antiviral signaling by targeting RIG-I
Ni Zhong, Chen Wang, Guangxiu Weng, Ting Ling, Liangguo Xu
Acta Biochimica et Biophysica Sinica.2023; 55(10): 1582. CrossRef
Identification of Vital Hub Genes and Potential Molecular Pathways of Dermatomyositis by Bioinformatics Analysis
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BioMed Research International.2021; 2021: 1. CrossRef
HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I
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Frontiers in Cellular and Infection Microbiology.2020;[Epub] CrossRef
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Discovery of Key Genes in Dermatomyositis Based on the Gene Expression Omnibus Database
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Change in the immune function of porcine iliac artery endothelial cells infected with porcine circovirus type 2 and its inhibition on monocyte derived dendritic cells maturation
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Identification of a cellular protein interacting with murine retrovirus Gag polyproteins: Choi , Won Ja; J. Microbiol. 1996;34(4):311-315.

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Abstract: The retroviral Gag polyprotein directs the assembly of virion particles and plays an important role in some events after entry into a host cell. The Gag polyprotein of a virus mixture is responsible for inducing murine acquired immunodeficiency syndrome (MAIDS) when injected into susceptible strains of mice. In order to identify the host cellular proteins which interact with the MAIDS virus Gag proteins and possibly mediate the function of the Gag proteins, mouse T-cell leukemic cDNA expression library was screened using the yeast GAL4 two hybrid system. Of 11 individual positive clones, the clone Y1 was selected for the study of protein-protein interaction. Its DNA sequence revealed that it was an exact match to the murine SH3 domain-containing protein SH3P8. It is expressed as 2.4 kbp transcripts in testis at higher levels and in various tissues tested at lower levels. Glutathione S-transferase-Y1 fusion protein binds tightly to Pr60^def-gag as well as Pr 65^eco-gag.

Regulation of Glycogen Concentration by the Histidine-Containing Phosphocarrier Protein HPr in Escherichia coli: Byoung-Mo Koo , Yeong-Jae Seok; J. Microbiol. 2001;39(1):24-30.

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Abstract: In addition to effecting the catalysis of sugar uptake, the bacterial phosphoenolpyruvate:sugar phosphotransferase system regulates a variety of physiological processes. In a previous paper [Seok et al., (1997) J. Biol. Chem. 272, 26511-26521], we reported the interaction with and allosteric regulation of Escherichia coli glycogen phosphorylase activity by the histidine-containing phosphocarrier protein HPr in vitro. Here, we show that the specific interaction between HPr and glycogen phosphorylase occurs in vivo. To address the physiological role of the HPr-glycogen phosphorylase complex, intracellular glycogen levels were measured in E. coli strains transformed with various plasmids. While glycogen accumulated during the transition between exponential and stationary growth phases in wildtype cells, it did not accumulate in cells overproducing HPr or its inactive mutant regardless of the growth stage. From these results, we conclude that HPr mediates crosstalk between sugar uptake through the phosphoenolpyruvate:sugar phosphotransferase system and glycogen breakdown. The evolutionary significance of the HPr-glycogen phosphorylase complex is suggested.

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