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NilB is a surface-exposed outer membrane protein. Expression of NilB is suppressed by NilR and growth in nutrient-rich medium. Members of this family exist in diverse bacteria and are common in the genomes of mucosal pathogens. Bioinformatic analyses reported that NilB is the only characterized member of a family of proteins distinguished by a conserved C-terminal domain of unknown function (DUF560) and N-terminal region tetratricopeptide repeats (TPR). Insertion and deletion mutational analyses revealed that NilB forms a beta barrel with 14 transmembrane strands and seven extracellular surface loops, and an N-terminal globular domain. The globular domain and surface loop 6 have a crucial role in the nematode colonization. Epifluorescence microscopy of these mutants revealed that NilB is necessary at early stages of colonization.
Mutational analyses reveal overall topology and functional regions of NilB, a bacterial outer membrane protein required for host association in a model of animal-microbe mutualism
J Bacteriol. 2012 Apr;194(7):1763-76. doi: 10.1128/JB.06711-11. Epub 2012 Jan 27.
Substrate specificity within a family of outer membrane carboxylate channels
PLoS Biol. 2012 Jan;10(1):e1001242. doi: 10.1371/journal.pbio.1001242. Epub 2012 Jan 17.