Screening the receptors for <i>Mycoplasma penetrans</i> P35 lipoprotein and characterization of its functional binding domains.

ABSTRACT: Mycoplasma penetrans, a prokaryotic microorganism initially isolated from the urine of a patient infected with human immunodeficiency virus (HIV), possesses a distinctive elongated flask-like shape and a tip-like structure. This unique morphology has been shown to facilitate its ability to invade cells both in vitro and in vivo. The adhesion of M. penetrans to host cells relies on lipid-associated membrane proteins (LAMPs), especially P35 lipoprotein, which is exposed on the mycoplasmal surface. In this study, modified Virus Overlay Protein Binding Assay (VOPBA) was employed to identify P35-interacting proteins from membrane protein extracts of SV40-immortalized human uroepithelial (SV-HUC-1) cells. Through recombinant protein binding assays, siRNA-mediat

SUBMITTER: Li X 

PROVIDER: S-EPMC11955645 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature