A Phage Endolysin-Derived Binding Protein Targeting the LysM Motif Enables Highly Specific Identification of

Shukho Kim1,2,3, Yoon-Jung Choi1,3, Md Shohel Rana2

  • 1Department of Microbiology, School of Medicine, Kyungpook National University, Daegu 41944, Republic of Korea.

Analytical Chemistry
|March 24, 2026
PubMed

Insights

A new diagnostic platform rapidly captures Acinetobacter baumannii using a phage endolysin

Area of Science:

  • Microbiology
  • Biotechnology
  • Infectious Diseases

Background:

  • Acinetobacter baumannii is a significant cause of hospital-acquired infections.
  • Distinguishing A. baumannii from related species is diagnostically challenging.
  • Current diagnostic methods can be time-consuming and complex.

Purpose of the Study:

  • To develop a novel, rapid, and specific diagnostic platform for Acinetobacter baumannii.
  • To utilize the cell wall-binding domain of an endolysin for bacterial capture.
  • To enable culture-independent detection of A. baumannii.

Main Methods:

  • Engineered a recombinant cell wall-binding domain (AbCD) from Acinetobacter baumannii phage Φ1656-2 endolysin.
  • Conjugated AbCD to epoxy magnetic beads (AbCD-eMB) for selective capture.
  • Validated specificity against various bacterial species and tested in clinical sputum specimens.

Main Results:

  • The AbCD-eMB complex rapidly captured Acinetobacter baumannii within 1 hour.
  • Achieved recovery rates of 72.5% in buffer and 55.7% in sputum specimens.
  • Demonstrated high specificity with no cross-reactivity against other common pathogens; detection limit ~3.4 × 10^3 CFU/mL.

Conclusions:

  • The AbCD-eMB platform offers a rapid, culture-independent, and highly specific method for Acinetobacter baumannii detection.
  • This approach has significant potential for clinical diagnostics and point-of-care testing.
  • Identified the LysM-containing peptidoglycan-binding domain as the key bacterial receptor for AbCD.