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Updated: May 30, 2026

Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins
Published on: June 11, 2015
Lytic myophage Abp53 encodes several proteins similar to those encoded by host Acinetobacter baumannii and phage
Chia-Ni Lee1, Tsai-Tien Tseng, Juey-Wen Lin
1Institute of Molecular Biology, National Chung Hsing University, Taichung 402, Taiwan.
Abstract:
Acinetobacter baumannii is an important Gram-negative opportunistic pathogen causing nosocomial infections. The emergence of multiple-drug-resistant A. baumannii isolates has increased in recent years. Directed toward phage therapy, a lytic phage of A. baumannii, designated Abp53, was isolated from a sputum sample in this study. Abp53 has an isometric head and a contractile tail with tail fibers (belonging to Myoviridae), a latent period of about 10 min, and a burst size of approximately 150 PFU per infected cell. Abp53 could completely lyse 27% of the A. baumannii isolates tested, which were all multiple drug resistant, but not other bacteria. Mg(2+) enhanced the adsorption and productivity of, and host lysis by, Abp53. Twenty Abp53 virion proteins were visualized in SDS-polyacrylamide gel electrophoresis, with a 47-kDa protein being the predicted major capsid protein. Abp53 has a double-stranded DNA genome of 95 kb. Sequence analyses of a 10-kb region revealed 8 open reading frames. Five of the encoded proteins, including 3 tail components and 2 hypothetical proteins, were similar to proteins encoded by A. baumannii strain ACICU. ORF1176 (one of the tail components, 1,176 amino acids [aa]), which is also similar to tail protein gp21 of Klebsiella phage phiKO2, contained repeated domains similar to those within the ACICU_02717 protein of A. baumannii ACICU and gp21. These findings suggest a common ancestry and horizontal gene transfer during evolution. As phages can expand the host range by domain duplication in tail fiber proteins, repeated domains in ORF1176 might have a similar significance in Abp53.
Insights
A novel lytic bacteriophage, Abp53, effectively lyses multidrug-resistant Acinetobacter baumannii strains. This phage therapy candidate shows potential for combating challenging nosocomial infections caused by this pathogen.
Area of Science:
- Microbiology
- Virology
- Infectious Diseases
Background:
- Acinetobacter baumannii is a significant Gram-negative opportunistic pathogen responsible for hospital-acquired infections.
- The increasing prevalence of multidrug-resistant (MDR) A. baumannii poses a critical threat to public health.
Purpose of the Study:
- To isolate and characterize a lytic bacteriophage targeting multidrug-resistant Acinetobacter baumannii.
- To evaluate the potential of the isolated phage for phage therapy applications.
Main Methods:
- Isolation and characterization of a lytic Acinetobacter baumannii phage (Abp53).
- Determination of phage morphology, latent period, burst size, and host lysis spectrum.
- Analysis of phage genome and virion proteins using SDS-PAGE and sequence analysis.
- Assessment of magnesium ion (Mg2+) effect on phage activity.
Main Results:
- Phage Abp53, belonging to the Myoviridae family, was isolated and characterized.
- Abp53 demonstrated effective lysis against 27% of tested multidrug-resistant A. baumannii isolates.
- Magnesium ions significantly enhanced Abp53's adsorption, productivity, and host lysis.
- Genomic and proteomic analyses revealed insights into Abp53's structure and potential evolutionary relationships.
Conclusions:
- Phage Abp53 is a promising candidate for phage therapy against multidrug-resistant Acinetobacter baumannii.
- The characterization provides a foundation for further development and application of Abp53.
- Evidence suggests potential horizontal gene transfer and common ancestry among related phages.
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