title: Adherence, fibronectin binding, and induction of cytoskeleton reorganization in cultured human cells by Mycoplasma penetrans.
abstract: Mycoplasma penetrans adhered to cultured human cells, forming clusters that localized to specific areas of the host cell surface. Adherence and cluster formation were inhibited by anti-M. penetrans antibodies, suggesting the involvement of specific adhesin-receptor interactions. Ultrastructural studies showed that after 2 h of infection, mycoplasmas attach to and penetrate the host cell surface. M. penetrans bound selectively to immobilized fibronectin, an interaction which was not inhibited by a 70-kDa fragment containing a heparin-gelatin-binding domain of fibronectin, other matrix glycoproteins, or an RGD tripeptide, suggesting the recognition of other specific binding sites on the fibronectin molecule. A ca. 65-kDa fibronectin-binding protein of M. penetrans was eluted following Sepharose-fibronectin affinity chromatography. Confocal, light, and immunofluorescence microscopy demonstrated that the interaction of M. penetrans with target cells triggers a signal that causes recruitment of several cytoskeletal components, including tubulin and alpha-actinin, and aggregation of phosphorylated proteins. Detergent-soluble mycoplasma proteins with apparent molecular masses of 18, 28, 32, 36, 39, and 41 kDa selectively bound to glutaraldehyde-fixed HEp-2 cells. Our findings offer new insights into understanding the interaction of this human mycoplasma with host target cells.
authors.affiliation: Department of Microbiology, University of Texas Health Science Center at San Antonio 78284-7758, USA.
authors.forename: J A
authors.initials: JA
authors.lastname: Girón
authors.forename: M
authors.initials: M
authors.lastname: Lange
authors.forename: J B
authors.initials: JB
authors.lastname: Baseman
mesh_terms: D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial / Q000494:pharmacology; D001422:Bacterial Adhesion / Q000187:drug effects / Q000502:physiology*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000302:isolation & purification; D002352:Carrier Proteins; D002462:Cell Membrane / Q000382:microbiology; D002478:Cells, Cultured; D003599:Cytoskeleton / Q000648:ultrastructure*; D004847:Epithelial Cells; D004848:Epithelium / Q000382:microbiology; D005353:Fibronectins / Q000378:metabolism*; D019084:Fluorescent Antibody Technique, Indirect; D006801:Humans; D007700:Kinetics; D016253:Microscopy, Immunoelectron; D018661:Mycoplasma penetrans / Q000276:immunology / Q000502:physiology* / Q000648:ultrastructure; D011485:Protein Binding; D016707:Tissue Fixation
chemical_list: D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D005353:Fibronectins; C078635:fibronectin-binding proteins, bacterial