The 40- and 90-kDa membrane proteins (ORF6 gene product) of Mycoplasma pneumoniae are responsible for the tip structure formation and P1 (adhesin) association with the Triton shell

• Published in: FEMS microbiology letters 1999-05, Vol.174 (1), p.143-149
• Main Authors: Layh-Schmitt, Gerlinde, Harkenthal, Michael
• Format: Article
• Language: English
• Subjects: Adhesins, Bacterial - metabolism; Adhesins, Bacterial - ultrastructure; Adsorption; Bacterial Adhesion - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - ultrastructure; Bacteriology; Biogenesis of cell structures, supramolecular organization; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Hemadsorption; Membrane proteins; Membrane Proteins - metabolism; Membrane Proteins - ultrastructure; Membranes; Microbiology; Mutation; Mycoplasma pneumoniae; Mycoplasma pneumoniae - genetics; Mycoplasma pneumoniae - ultrastructure; Orf6 gene; ORF6 gene product; p1 Protein; Protein Binding; Proteins; Tip structure; Triton shell
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.1999.tb13561.x

Abstract After Triton X-100 treatment of Mycoplasma pneumoniae cells, a portion of the adhesin P1 (transmembrane protein) proved to remain tightly associated with the Triton insoluble material (Triton shell) as shown previously by several authors. However, the spontaneous loss of two cytadherence-associated membrane proteins of 90 and 40 kDa (gene product of the open reading frame 6 of the P1 operon) in a hemadsorption-negative mutant, designated M5, resulted in a 100% release of the P1 protein into the Triton phase and in the lack of the characteristic tip-like attachment organelle of M. pneumoniae indicating an essential role of the open reading frame 6 gene product in tip structure formation.