Journal article Open Access

Structures and functions of autotransporter proteins in microbial pathogens

Benz, Inga; Schmidt, M. Alexander


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{
  "DOI": "10.1016/j.ijmm.2011.03.003", 
  "author": [
    {
      "family": "Benz, Inga"
    }, 
    {
      "family": "Schmidt, M. Alexander"
    }
  ], 
  "issued": {
    "date-parts": [
      [
        2011, 
        8, 
        1
      ]
    ]
  }, 
  "abstract": "Since their discovery more than 20 years ago the autotransporter protein superfamily has been growing\ncontinuously and currently represents the largest protein family in (pathogenic) Gram-negative bacteria.\nAutotransporter proteins (AT) adhere to a common structural principle and are composed of a\nC-terminal -barrel-shaped 'translocator' domain and an N-terminal 'passenger' domain. The translocator\nis anchored in the outer membrane and is indispensable for the N-terminal passenger part to traverse\nthe outer membrane. Most if not all AT harbor a chaperone segment that increases protein stability and\nmay be located in the passenger or translocator domain. The passenger mediates the specific virulence\nfunction(s) of the particular AT. Accordingly, passenger domains of AT can be quite variable. Interestingly,\nAT have been identified as the first glycosylated proteins in Gram-negative bacteria. Despite the\nconsiderable efforts invested in the characterization of autotransporter biogenesis, various aspects such\nas the participation of accessory proteins, the fate of the translocator, or the translocation of glycosylated\nproteins still remain only poorly understood. In addition, recent evidence indicates that the prefix 'auto'\nmight be slightly exaggerated. Here, we will selectively discuss novel insights at various stages of AT\nbiogenesis.", 
  "title": "Structures and functions of autotransporter proteins in microbial pathogens", 
  "type": "article-journal", 
  "id": "895927"
}
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