OUP user menu

Crucial domains are conserved in Enterobacteriaceae porins

Valérie Simonet, Monique Malléa, Didier Fourel, Jean-Michel Bolla, Jean-Marie Pages
DOI: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08030.x 91-97 First published online: 1 February 1996


With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-peptide antibodies specific to exposed, transmembrane spanning, or pore-forming regions of Escherichia coli porins. Anti-peptide antibodies which recognized the exposed epitopes indicated a great variability among the bacterial porins analysed. Interestingly, an antigenic site located in the internal loop L3 constricting the pore diameter was present in the majority of the bacterial porins tested. Two epitopes located in domains involved in subunit interaction were also highly conserved. The presence of these common peptides suggested a conservation of specific regions involved in the functional organization of the enterobacterial porins.

  • Escherichia coli
  • Enterobacteriaceae
  • Bacterial porins
  • Anti-peptide antibodies
  • Epitopes
  • Antibiotic resistance