Autographiviridae phage HH109 uses capsular polysaccharide for infection of Vibrio alginolyticus

Abstract

Summary: Autographiviridae phage HH109 is a lytic Vibrio alginolyticus E110-specific phage, but the molecular mechanism underlying host recognition of this phage remains unknown. In this study, a transposon mutagenesis library of E110 was used to show that several capsular polysaccharide (CPS) synthesis-related genes were linked to the phage HH109 infection. Gene deletion combined with multiple functional assays demonstrated that CPS serves as the receptor for the phage HH109. Deletions of CPS genes caused reduction or loss of capsule and reduced adsorption. Comparative genome analysis revealed that phage-resistant mutants harbored loss-of-function mutations in the previously identified genes responsible for CPS biosynthesis. The tail protein gp02 of phage HH109 was identified as the receptor-binding protein (RBP) on CPS using antibody blocking assay, immunofluorescence staining, and CPS quantification. Additionally, we found that the phage HH109 could degrade approximately 88% of mature biofilms. Our research findings provide a theoretical basis against vibriosis.

Keywords

• Molecular biology
• Microbiology