   3.4.17.13 | physiological function |
a LD-carboxypeptidase isoform Pgp2 mutant shows an increase in tetrapeptide-containing muropeptides and a complete absence of tripeptides in the peptidoglycan structure, consistent with LD-carboxypeptidase activity. An isoform Pgp1Pgp2 double mutant demonstrates that Pgp2 activity is required to generate the tripeptide substrate for Pgp1. Loss of Pgp2 affects several pathogenic properties, the deletion strain is defective for motility in semisolid agar, biofilm formation, and fluorescence on calcofluor white. Isoform Pgp2 peptidoglucan also causes decreased stimulation of the human nucleotide-binding oligomerization domain 1 (Nod1) proinflammatory mediator in comparison with wild type, these changes do not alter the ability of the Pgp2 mutant strain to survive within human epithelial cells or to elicit secretion of IL-8 from epithelial cells after infection. The Pgp2 mutant also shows significantly reduced fitness in a chick colonization model |
732172 |
