- 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
- Characterization of a novel phage depolymerase specific to Escherichia coli O157:H7 and biofilm control on abiotic surfaces
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Do-Won Park , Jong-Hyun Park
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J. Microbiol. 2021;59(11):1002-1009. Published online October 6, 2021
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DOI: https://doi.org/10.1007/s12275-021-1413-0
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Abstract
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The increasing prevalence of foodborne diseases caused by
Escherichia coli O157:H7 as well as its ability to form biofilms
poses major threats to public health worldwide. With increasing
concerns about the limitations of current disinfectant treatments,
phage-derived depolymerases may be used as promising
biocontrol agents. Therefore, in this study, the characterization,
purification, and application of a novel phage depolymerase,
Dpo10, specifically targeting the lipopolysaccharides
of E. coli O157, was performed. Dpo10, with a molecular
mass of 98 kDa, was predicted to possess pectate lyase
activity via genome analysis and considered to act as a receptor-
binding protein of the phage. We confirmed that the
purified Dpo10 showed O-polysaccharide degrading activity
only for the E. coli O157 strains by observing its opaque halo.
Dpo10 maintained stable enzymatic activities across a wide
range of temperature conditions under 55°C and mild basic
pH. Notably, Dpo10 did not inhibit bacterial growth but significantly
increased the complement-mediated serum lysis
of E. coli O157 by degrading its O-polysaccharides. Moreover,
Dpo10 inhibited the biofilm formation against E. coli O157
on abiotic polystyrene by 8-fold and stainless steel by 2.56 log
CFU/coupon. This inhibition was visually confirmed via fieldemission
scanning electron microscopy. Therefore, the novel
depolymerase from E. coli siphophage exhibits specific binding
and lytic activities on the lipopolysaccharide of E. coli O157
and may be used as a promising anti-biofilm agent against
the E. coli O157:H7 strain.
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Citations
Citations to this article as recorded by - Identify and characterize a carbapenem-resistant Salmonella enteritidis phage depolymerase Dpo52
Wei Li, Mengyao Yuan, Jiaxin Che, Shangyang Wei, Yanzhi Chen, Jiayi Ren, Runxin Song, Hao Zhao, Jing Huang, Zhimin Guo
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Frontiers in Cellular and Infection Microbiology.2026;[Epub] CrossRef - Rapid and Specific Detection of Escherichia coli O157:H7 Using Engineered Phage Tailspike Protein-Based Magnetic Assisted Luminescence Assay
Jin Seo, Dahee Choi, Seongshin Jo, Minsuk Kong
Analytical Chemistry.2026; 98(27): 20092. CrossRef - Targeting Foodborne Pathogens with Bacteriophages: Mechanisms, Applications, and Resistance
Lekshmi K. Edison, Subhashinie Kariyawasam
Pathogens.2026; 15(7): 711. CrossRef - Phage vB_KpnS_MK54: lPS-associated factors involved in phage adsorption and depolymerase-driven anti-biofilm effects
Yan Zeng, Zhaomin Wu, Zhuangkan Yan, Yin Wang, Zexiao Yang, Yixin Huang, Suizhong Cao, Xueping Yao
Frontiers in Microbiology.2026;[Epub] CrossRef - Escherichia coli bacteriophage vB_EcoS_MS2 effectively prevents biofilm formation but shows limited activity against mature biofilms
Nur Isz Aishah Ismail, Liat Hung Cheah, Mohd Termizi Yusof, Hasliza Abu Hassim, Zulkifli Idrus, Roseliza Roslee, Mohd Asrore Mohd Shaufi
Brazilian Journal of Microbiology.2026;[Epub] CrossRef -
Staphylococcus aureus
Biofilms: Challenges and Advances in Bacteriophage Therapy
Kokkarambath Vannadil Suchithra, Nisha K. Rai, A. Veena Shetty
PHAGE: Therapy, Applications, and Research.2026;[Epub] CrossRef - Application of phage-derived enzymes for enhancing food safety
Junhwan Kim, Xinyu Liao, Song Zhang, Tian Ding, Juhee Ahn
Food Research International.2025; 209: 116318. CrossRef - Novel polygalacturonase PG-BG31 prevents biofilm formation and increases antibiotic efficacy against catheter-associated Escherichia coli
Marija Atanaskovic, Andjela Dilparic, Mario Zlatović, Lidija Senerovic
Journal of Biotechnology.2025; 406: 179. CrossRef - Isolation and identification of bacteriophage against Escherichia coli ATCC 25922 and their biofilm Inhibition studies
Lakshminarayanan Sivakumar, Jeya Vignesh John Durai Kumar, Subadarshini Madhavan, K U Mina Parvesh, Santhosh Kumar Arunagiri, Suriyaprakash Rajadesingu, Shobana Sugumar, Narenkumar Jayaraman, Kagithakara Vajravelu Leela, A. Karthik, Tabarak Malik, Parthip
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Nimisha Tehri, Dharun Vijay Puniya, Anil Kumar Puniya
Current Food Science and Technology Reports.2025;[Epub] CrossRef - Lytic bacteriophages as alternative to overcoming antibiotic-resistant biofilms formed by clinically significant bacteria
Abdul-Halim Osman, Samuel Darkwah, Fleischer C. N. Kotey, Adwoa Asante-Poku, Eric S. Donkor
Therapeutic Advances in Infectious Disease.2025;[Epub] CrossRef - Synergistic Disruption of Foodborne Pathogen Biofilms by Oregano Essential Oil and Bacteriophage phiLLS: Atomic Force Microscopy Insights
Ana Karina Kao Godínez, Carlos Regalado-González, Claudia Villicaña, José Basilio Heredia, José Benigno Valdez-Torres, María Muy-Rangel, Monserrat Escamilla-García, Josefina León-Félix
Molecules.2025; 30(17): 3552. CrossRef - Phage-encoded depolymerases and endolysins as prospective strategies to combat multidrug-resistant Klebsiella pneumoniae
Yunhan Zhang, Weiqing Lan, Xiaohong Sun
International Journal of Biological Macromolecules.2025; 321: 146159. CrossRef -
Isolation and characterization of a novel K3-type capsule-targeting phage for the treatment of carbapenem-resistant
Acinetobacter baumannii
Hewen Deng, Ziqiang Liu, Siyun Wang, Shitong Lu, Ruopeng Cai, Linwan Feng, Kun Shi, Xin Tan, Rui Du, Hui Wang
Microbiology Spectrum.2025;[Epub] CrossRef - Penetrating the biofilm barrier: characterization of Escherichia phage vB_EcoS-TPF103dw and harnessing depolymerase to combat Shiga toxin-producing Escherichia coli O103 biofilm
David L. Campos, Yen-Te Liao, Leslie A. Harden, Yujie Zhang, Vivian C. H. Wu
Frontiers in Microbiology.2025;[Epub] CrossRef - Effect of Bacteriophages against Biofilms of Escherichia coli on Food Processing Surfaces
Ana Brás, Márcia Braz, Inês Martinho, João Duarte, Carla Pereira, Adelaide Almeida
Microorganisms.2024; 12(2): 366. CrossRef - Bacteriophage–Host Interactions and the Therapeutic Potential of Bacteriophages
Leon M. T. Dicks, Wian Vermeulen
Viruses.2024; 16(3): 478. CrossRef - Current Strategies for Combating Biofilm-Forming Pathogens in Clinical Healthcare-Associated Infections
Rashmita Biswas, Bhawana Jangra, Ganapathy Ashok, Velayutham Ravichandiran, Utpal Mohan
Indian Journal of Microbiology.2024; 64(3): 781. CrossRef - Phage Adsorption to Gram-Positive Bacteria
Audrey Leprince, Jacques Mahillon
Viruses.2023; 15(1): 196. CrossRef - Prevalence of Indigenous Antibiotic-Resistant Salmonella Isolates and Their Application to Explore a Lytic Phage vB_SalS_KFSSM with an Intra-Broad Specificity
Jaein Choe, Su-Hyeon Kim, Ji Min Han, Jong-Hoon Kim, Mi-Sun Kwak, Do-Won Jeong, Mi-Kyung Park
Journal of Microbiology.2023; 61(12): 1063. CrossRef - Phages against Pathogenic Bacterial Biofilms and Biofilm-Based Infections: A Review
Siyu Liu, Hongyun Lu, Shengliang Zhang, Ying Shi, Qihe Chen
Pharmaceutics.2022; 14(2): 427. CrossRef
- Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition
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Jun-Hyeok Yu , Do-Won Park , Jeong-A Lim , Jong-Hyun Park
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J. Microbiol. 2021;59(9):840-847. Published online August 12, 2021
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DOI: https://doi.org/10.1007/s12275-021-1242-1
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892
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9
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Abstract
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Endolysin, a peptidoglycan hydrolase derived from bacteriophage,
has been suggested as an alternative antimicrobial
agent. Many endolysins on staphylococcal phages have been
identified and applied extensively against Staphylococcus spp.
Among them, LysK-like endolysin, a well-studied staphylococcal
endolysin, accounts for most of the identified endolysins.
However, relatively little interest has been paid to LysKunlike
endolysin and a few of them has been characterized.
An endolysin LysSAP33 encoded on bacteriophage SAP33
shared low homology with LysK-like endolysin in sequence
by 41% and domain composition (CHAP-unknown CBD).
A green fluorescence assay using a fusion protein for Lys-
SAP33_CBD indicated that the CBD domain (157-251 aa)
was bound to the peptidoglycan of S. aureus. The deletion of
LysSAP33_CBD at the C-terminal region resulted in a significant
decrease in lytic activity and efficacy. Compared to
LysK-like endolysin, LysSAP33 retained its lytic activity in a
broader range of temperature, pH, and NaCl concentrations.
In addition, it showed a higher activity against biofilms than
LysK-like endolysin. This study could be a helpful tool to develop
our understanding of staphylococcal endolysins not
belonging to LysK-like endolysins and a potential biocontrol
agent against biofilms.
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Citations
Citations to this article as recorded by - Bacteriophage lysins: a promising strategy for combating foodborne pathogens in food safety
Jiaxin Wei, Yuying Zhang, Yubao Li, Lei Wang
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Mina Golban, Javad Charostad, Hossein Kazemian, Hamid Heidari
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Players Orchestrating Bacteriophage-Induced Cell Lysis and their
Therapeutic Applications
Safia Samir
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