Recombinant Human IgG1 Enhances Complement-Mediated Bacteriolysis and Macrophage Phagocytosis of Pseudomonas aeruginosa via Targeting Cell Surface Polysaccharides

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Authors: Thae Thae Min, Audrey Guilbaud, Frédéric Pecorari, Pawana Panomket, Nitima Suttipanta, Dietmar Haltrich, Pattra Suntornthiticharoen, Montarop Yamabhai
Cited by: 1
References: 43

Abstract

High Resolution Image Download MS PowerPoint Slide The development of innovative therapeutics against WHO priority pathogens is an urgent global need. Here, we demonstrate the functionalities of a human antibody, previously isolated by whole cell biopanning of the phage display scFv library. The yPgi3G4 IgG1 could mediate antibody-dependent phagocytosis of Pseudomonas aeruginosa by human matured THP-1 monocytes, of which colocalization with caveolin was clearly observed at 24 h. Next, the antibacterial activity against live P. aeruginosa was demonstrated by an agglutination assay and complement-mediated killing of the bacteria. Lipopolysaccharide (LPS) extraction and Western blot (WB) analysis suggested that LPS was the target of the yPgi3G4 IgG1 antibody. A cross-reactivity assay to available isolates in Thailand and France showed that the antibody could detect 6 P. aeruginosa serotypes including several multidrug-resistant clinical isolates. This study proved the potential of using this strategy to identify a biotherapeutic for a certain quotient of multidrug-resistant P. aeruginosa and other bacterial infections.

Fields of Study & Subjects

Monoclonal and Polyclonal Antibodies Research Bacteriophages and microbial interactions Glycosylation and Glycoproteins Research

Publication details

Journal / source
ACS Infectious Diseases
Publisher
American Chemical Society (ACS)
Volume
12
Issue
2
Pages
841–853
Publication date
26 January 2026
Language
EN