M13 phages engineered with chlamydia phage φCPG1 protein IN5 and arginine-glycine-aspartic acid inhibits Chlamydia trachomatis intracellular growth.

ABSTRACT: Chlamydia trachomatis (C. t) is the most common causative agent of sexually transmitted bacterial urogenital infections worldwide. C. t treatment failure is increasing because antibiotic resistance has developed in recent years. Therefore, the development of novel therapeutic strategies is necessary. Here, we constructed an M13 phage carrying two functional peptides, including the integrin binding peptide arginine-glycine-aspartic acid (RGD) on pⅧ and the IN5 protein from Chlamydia caviae phage φCPG1 on pIII to reduce C. t infection. We called these phages M13-RGD₈-IN5₃. The recombinant phages successfully expressed IN5 proteins. Confocal laser scanning microscopy confirmed that the recombinant phages were able to enter HeLa cells and C. t inclusion bodies. IN5 protei

SUBMITTER: You C 

PROVIDER: S-EPMC12593711 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature