Abstract
Many bacterial species produce a paracrystalline layer, the surface layer, which completely surrounds the exterior of the cell. In some bacteria, the surface layer is implicated in pathogenesis. Two proteins present in cell wall extracts from Clostridium tetani have been investigated and identified one of these has been unambiguously as the surface-layer protein (SLP). The gene, slpA, has been located in the genome of C. tetani E88 that encodes the SLP. The molecular mass of the protein as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis is considerably larger than that predicted from the gene; however the protein does not appear to be glycosylated. Furthermore, analysis of five C. tetani strains, including three recent clinical isolates, shows considerable variation in the sizes of the SLP.
Original language | English |
---|---|
Pages (from-to) | 126-31 |
Number of pages | 6 |
Journal | Fems Microbiology Letters |
Volume | 274 |
Issue number | 1 |
DOIs | |
Publication status | Published - Sept 2007 |
Keywords
- Mass Spectrometry
- Genetic Variation
- Genome, Bacterial
- Amino Acid Motifs
- Electrophoresis, Polyacrylamide Gel
- Glycosylation
- Bacterial Outer Membrane Proteins
- Clostridium tetani