The P200 protein of Mycoplasma pneumoniae shows common features with the cytadherence-associated proteins HMW1 and HMW3

Gene. 1996 May 24;171(1):79-82. doi: 10.1016/0378-1119(96)00014-5.

Abstract

The gene coding for the P200 protein of the bacterium, Mycoplasma pneumoniae (Mp), was cloned and sequenced. The sequence-derived data and biochemical data indicated that P200 has several features in common with the well characterized cytadherence-associated proteins, HMW1 and HMW3. These features consist of abnormal migration in SDS-PAGE, a central acidic domain with a high Pro content, repeated peptide blocks within the Pro-rich domain and P200 partitioning similar to HMW1 and HMW3 in the insoluble fraction after extraction of Mp with the detergent Triton X-100.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Adhesion
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Cell Adhesion Molecules*
  • Cloning, Molecular
  • Genes, Bacterial / genetics*
  • Glutamic Acid / analysis
  • Isoelectric Point
  • Membrane Proteins / chemistry*
  • Molecular Sequence Data
  • Molecular Weight
  • Mycoplasma pneumoniae / chemistry
  • Mycoplasma pneumoniae / genetics*
  • Open Reading Frames / genetics
  • Proline / analysis

Substances

  • Bacterial Proteins
  • Cell Adhesion Molecules
  • HMW1 protein, Mycoplasma
  • HMW3 protein, Mycoplasma
  • Membrane Proteins
  • P200 protein, Mycoplasma pneumoniae
  • Glutamic Acid
  • Proline

Associated data

  • GENBANK/K25989