Structural Receptors and Host Adaptations Affecting the Bacteriophage Targeting of Vibrio Pathogens
Year: 2026
Type: article
Abstract: The widespread exposure of multidrug-resistant bacterial strains due to excessive use of antibiotics has accelerated the bacteriophage applications as highly specific antibacterial agents competent to target resistant pathogenic Vibrio through receptor-mediated adsorption and lytic infection. Vibrio pathogens are responsible for substantial economic losses, environmental instability, and foodborne infections in humans through contaminated seafood and water. However, the molecular determinants remain incompletely understood, commanding the Vibrio-phage host specificity, host range, and resistance evolution. This review highlights the comprehensive overview of structural, and functional framework of Vibrio surface receptors responsible for phage recognition, including outer membrane vesicles (OMVs), porins, lipopolysaccharides (LPS), capsular polysaccharides (CPS), flagella, and pili along with specialized bacteriophage tail spike proteins known as receptor-binding proteins (RBPs). We also explored the mechanisms against phage-mediated lysis, including receptor modification, intracellular defense systems, physiological remodeling, and structural adaptations that regulate burst size, lysis timing, and resistance evolution with emphasis on significant progress in phage biology and therapeutic development. It is critical to grasp the molecular-level interaction mechanisms due to limited marine phage ecological data, lack of standardized resistance databases, and regulatory constraints. Future perspectives emphasize the engineered phages, multi-omics integration, and artificial intelligence-driven phage design for the sustainable management of Vibriosis and improved aquaculture biosecurity.
Source: Microorganisms
Language: English
Subfield: Ecology
Field: Environmental Science
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $3,258
Awards: G4024419096, G657376064, G6875972670
OpenAlex ID: W7204883822
