title: Disulfide-linked protein associated with Mycoplasma pneumoniae cytadherence phase variation.
abstract: Wild-type Mycoplasma pneumoniae possessed a protein with a very high molecular weight under nonreducing conditions (greater than 340,000; designated HMW5); this protein was absent from a noncytadhering phase variant lacking HMW1, 2, 3, and 4. When examined by two-dimensional nonreducing-reducing gel electrophoresis, HMW5 dissociated to yield a single polypeptide spot of molecular weight 190,000 that comigrated with cytadherence phase-variable protein HMW2. Extraction of wild-type mycoplasmas with Triton X-100 revealed the exclusive partitioning of HMW5 with the detergent-insoluble cytoskeletonlike triton shell.
authors.affiliation: Department of Microbiology, University of Georgia, Athens 30602.
authors.forename: M K
authors.initials: MK
authors.lastname: Stevens
authors.forename: D C
authors.initials: DC
authors.lastname: Krause
mesh_terms: D000942:Antigens, Bacterial / Q000032:analysis*; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000032:analysis*; D004220:Disulfides; D015180:Electrophoresis, Gel, Two-Dimensional; D008970:Molecular Weight; D009177:Mycoplasma pneumoniae / Q000032:analysis*; D013045:Species Specificity
chemical_list: D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D004220:Disulfides