Journal of Microbiology

Journal Articles

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

A rule governing the FtsH-mediated proteolysis of the MgtC virulence protein from Salmonella enterica serovar Typhimurium: Jonghyun Baek , Eunna Choi , Eun-Jin Lee; J. Microbiol. 2018;56(8):565-570. Published online July 25, 2018; DOI: https://doi.org/10.1007/s12275-018-8245-6

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Abstract

A tightly controlled turnover of membrane proteins is required for lipid bilayer stability, cell metabolism, and cell viability. Among the energy-dependent AAA+ proteases in Salmonella, FtsH is the only membrane-bound protease that contributes to the quality control of membrane proteins. FtsH preferentially degrades the C-terminus or N-terminus of misfolded, misassembled, or damaged proteins to maintain physiological functions. We found that FtsH hydrolyzes the Salmonella MgtC virulence protein when we substitute the MgtC 226th Trp, which is well conserved in other intracellular pathogens and normally protects MgtC from the FtsH-mediated proteolysis. Here we investigate a rule determining the FtsHmediated proteolysis of the MgtC protein at Trp226 residue. Substitution of MgtC tryptophan 226th residue to alanine, glycine, or tyrosine leads to MgtC proteolysis in a manner dependent on the FtsH protease whereas substitution to phenylalanine, methionine, isoleucine, leucine, or valine resists MgtC degradation by FtsH. These data indicate that a large and hydrophobic side chain at 226th residue is required for protection from the FtsH-mediated MgtC proteolysis.

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Edwardsiella piscicida requires SecY homeostasis facilitated by FtsH and YccA for stress resistance and virulence
Qingjuan Wu, Aijun Tian, Jiarui Xu, Qingjian Fang, Huiqin Huang, Yonghua Hu
Aquaculture.2024; 582: 740528. CrossRef
For Someone, You Are the Whole World: Host-Specificity of Salmonella enterica
Anastasiya V. Merkushova, Anton E. Shikov, Anton A. Nizhnikov, Kirill S. Antonets
International Journal of Molecular Sciences.2023; 24(18): 13670. CrossRef
Edwardsiella piscicida YccA: A novel virulence factor essential to membrane integrity, mobility, host infection, and host immune response
Mengru Jin, Jiaojiao He, Jun Li, Yonghua Hu, Dongmei Sun, Hanjie Gu
Fish & Shellfish Immunology.2022; 126: 318. CrossRef
FtsH is required for protein secretion homeostasis and full bacterial virulence in Edwardsiella piscicida
Wei Wang, Jiatiao Jiang, Hao Chen, Yuanxing Zhang, Qin Liu
Microbial Pathogenesis.2021; 161: 105194. CrossRef
RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee
Journal of Microbiology.2019; 57(10): 910. CrossRef
The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee
Scientific Reports.2019;[Epub] CrossRef

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