- The novel antifungal agent AB-22 displays in vitro activity against hyphal growth and biofilm formation in Candida albicans and potency for treating systemic candidiasis
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Kyung-Tae Lee , Dong-Gi Lee , Ji Won Choi , Jong-Hyun Park , Ki Duk Park , Jong-Seung Lee , Yong-Sun Bahn
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J. Microbiol. 2022;60(4):438-443. Published online March 14, 2022
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DOI: https://doi.org/10.1007/s12275-022-2016-0
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Systemic candidiasis, which is mainly caused by Candida albicans,
is a serious acute fungal infection in the clinical setting.
In a previous study, we reported that compound 22h (designated
as AB-22 in this study), a vinyl sulfate compound, is a
fast-acting fungicidal agent against a broad spectrum of fungal
pathogens. In this study, we aimed to further analyze the
in vitro and in vivo efficacy of AB-22 against filamentation,
biofilm formation, and virulence of C. albicans. Under in vitro
hyphal growth-inducing condition, AB-22 effectively inhibited
germ tube formation and hyphal growth, which are required
for the initiation of biofilm formation. Indeed, AB-22
significantly suppressed C. albicans biofilm formation in a
dose-dependent manner. Moreover, AB-22 treatment inhibited
the normal induction of ALS3, HWP1, and ECE1, which
are all required for hyphal transition in C. albicans. Furthermore,
AB-22 treatment increased the survival of mice systemically
infected with C. albicans. In conclusion, in addition
to its fungicidal activity, AB-22 inhibits filamentation and
biofilm formation in C. albicans, which could collectively contribute
to its potent in vivo efficacy against systemic candidiasis.
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Citations
Citations to this article as recorded by  - Preparation and analysis of quinoa active protein (QAP) and its mechanism of inhibiting Candida albicans from a transcriptome perspective
Xufei Zhang, Chunmei Zheng, Wenxuan Ge, Xueying Li, Xiuzhang Wang, Yanxia Sun, Xiaoyong Wu
PeerJ.2025; 13: e18961. CrossRef - Inhibition of candidalysin production by methoxy-apo-enterobactin from Streptomyces ambofaciens CJD34 as a novel antifungal strategy against Candida albicans
Eui-Seong Kim, Hyeongju Jeong, Mustansir Abbas, Soohyun Um, Juntack Oh, Kyuho Moon, Kyung-Tae Lee
Journal of Microbiology.2025; 63(6): e2504019. CrossRef
- Directed analysis of cyanobacterial membrane phosphoproteome using stained phosphoproteins and titanium-enriched phosphopeptides§
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Dong-Gi Lee , Joseph Kwon , Chi-Yong Eom , Young-Moon Kang , Seong Woon Roh , Kyung-Bok Lee , Jong-Soon Choi
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J. Microbiol. 2015;53(4):279-287. Published online April 8, 2015
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DOI: https://doi.org/10.1007/s12275-015-5021-8
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Abstract
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Gel-free shotgun phosphoproteomics of unicellular cyanobacterium
Synechocystis sp. PCC 6803 has not been reported
up to now. The purpose of this study is to develop directed
membrane phosphoproteomic method in Synechocystis sp.
Total Synechocystis membrane proteins were separated by
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
and phosphoprotein-stained gel bands were selectively subjected
to in-gel trypsin digestion. The phosphorylation sites
of the resulting peptides were determined by assigning the
neutral loss of [M-H3PO4] to Ser, Thr, and Tyr residues using
nano-liquid chromatography 7 Tesla Fourier transform mass
spectrometry. As an initial application, 111 proteins and 33
phosphoproteins were identified containing 11 integral membrane
proteins. Identified four unknown phosphoproteins
with transmembrane helices were suggested to be involved in
membrane migration or transporters based on BLASTP search
annotations. The overall distribution of hydrophobic amino
acids in pTyr was lower in frequency than that of pSer or
pThr. Positively charged amino acids were abundantly revealed
in the surrounding amino acids centered on pTyr. A
directed shotgun membrane phosphoproteomic strategy provided
insight into understanding the fundamental regulatory
processes underlying Ser, Thr, and Tyr phosphorylation in
multi-layered membranous cyanobacteria.
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Citations
Citations to this article as recorded by - Global Profiling of Protein Phosphorylation, Acetylation, and β-Hydroxybutyrylation in Nannochloropsis oceanica
Lingyu Ouyang, Wuxin You, Ansgar Poetsch, Li Wei
Journal of Agricultural and Food Chemistry.2024; 72(47): 26248. CrossRef - Post-translational Modifications of Serine/Threonine and Histidine Kinases and Their Roles in Signal Transductions in Synechocystis Sp. PCC 6803
Wu Xu, Yingchun Wang
Applied Biochemistry and Biotechnology.2021; 193(3): 687. CrossRef - Comprehensive Phosphoproteomic Analysis of Nostoc flagelliforme in Response to Dehydration Provides Insights into Plant ROS Signaling Transduction
Wenyu Liang, Fengkun Yan, Meng Wang, Xiaoxu Li, Zheng Zhang, Xiaorong Ma, Jinhong Hu, Jun Wang, Lingxia Wang
ACS Omega.2021; 6(21): 13554. CrossRef - Metaproteomic analysis of harmful algal bloom in the Daechung reservoir, Korea
Jong-Soon Choi, Yun Hwan Park, Soo Hyeon Kim, Ju Seong Park, Yoon-E Choi
Environmental Biology Research.2020; 38(3): 424. CrossRef - Efficient profiling of detergent-assisted membrane proteome in cyanobacteria
Jong-Soon Choi, Yun Hwan Park, Jeong Hyun Oh, Sooyong Kim, Joseph Kwon, Yoon-E Choi
Journal of Applied Phycology.2020; 32(2): 1177. CrossRef - Assessment of Protein Content and Phosphorylation Level in Synechocystis sp. PCC 6803 under Various Growth Conditions Using Quantitative Phosphoproteomic Analysis
Masakazu Toyoshima, Yuma Tokumaru, Fumio Matsuda, Hiroshi Shimizu
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Piyoosh Kumar Babele, Jay Kumar, Venkatesh Chaturvedi
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Rachna Agarwal, Julian P. Whitelegge, Sanjay Saini, Amit Prakash Shrivastav
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Natalia Battchikova, Dorota Muth-Pawlak, Eva-Mari Aro
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Jiangqi Qu, Liping Shen, Meng Zhao, Wentong Li, Chengxia Jia, Hua Zhu, Qingjing Zhang
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Mengliang Shi, Xiaoqing Zhang, Guangsheng Pei, Lei Chen, Weiwen Zhang
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Qian Xiong, Zhuo Chen, Feng Ge
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Yunpeng Wang, Lei Chen, Weiwen Zhang
Biotechnology for Biofuels.2016;[Epub] CrossRef
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