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Microbiology 154 (2008), 1185-1192; DOI  10.1099/mic.0.2007/013342-0
© 2008 Society for General Microbiology

The acidic, glutamine-rich Mpn474 protein of Mycoplasma pneumoniae is surface exposed and covers the complete cell

Jan Hegermann1,{dagger}, Sven Halbedel1, Roger Dumke2, Jörg Regula3,{ddagger}, Razif R. Gabdoulline4, Frank Mayer1, Jörg Stülke1 and Richard Herrmann3

1 Abteilung für Allgemeine Mikrobiologie, Institut für Mikrobiologie und Genetik, Grisebachstr. 8, D-37077 Göttingen, Germany
2 Institut für Medizinische Mikrobiologie und Hygiene, Technische Universität, Medizinische Fakultät Carl Gustav Carus, Fetscherstr. 74, D-01307 Dresden, Germany
3 Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany
4 Molecular and Cellular Modeling Group, EML Research, Schloss-Wolfsbrunnenweg 33, D-69118 Heidelberg, Germany

Correspondence
Jan Hegermann
jhegerm1{at}gwdg.de

The protein Mpn474 encoded by the mpn474 gene of the human-pathogenic Mycoplasma pneumoniae contains 1033 amino acids and has an isoelectric point of 4.79, which is caused by the large excess of glutamic acid residues (11 %). Although the protein lacks recognizable export signals we showed by immuno-electron microscopy that Mpn474 is surface exposed, covering the cell completely. By combining cross-linking and careful treatment of the bacterial cells with Triton X-100, we found that this protein is weakly bound to the cell surface, while the true transmembrane protein Mpn141 (adhesin P1) is firmly attached under the same experimental conditions. A transposon mutant in the mpn474 gene, which has no obvious phenotype, served as negative control for the immunodetection.

{dagger}Present address: European Neuroscience Institute, Grisebachstr. 5, 37077 Göttingen, Germany.

{ddagger}Present address: Roche Diagnostics GmbH, Nonnenwald 2, 82377 Penzberg, Germany.

Supplementary material is available with the online version of this paper.






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