Microbial evasion of the immune system: structural modifications of enterobactin impair siderocalin recognition.
The mammalian protein siderocalin binds and inactivates the ferric complex of the bacterial siderophore enterobactin with a Kd value similar to that of the bacterial receptor FepA. However, microorganisms can evade this immune response by structural modifications of the siderophore. The binding of siderophores by siderocalin relies in part on electrostatic interactions and does not depend greatly on what metal is in the complex. It is also sterically limited by the rigid conformation of the protein calyx; methylation of the three catecholate rings of enterobactin hinders siderocalin recognition. The siderocalin binding has been probed for a series of enterobactin analogues in order to investigate in detail the specificity of siderocalin recognition.
Abergel
Rebecca J
RJ
Department of Chemistry, University of California, Berkeley, California 94720-1460, USA.
Moore
Evan G
EG
Strong
Roland K
RK
Raymond
Kenneth N
KN
D004758:Enterobactin / Q000737:chemistry*; D004926:Escherichia coli / Q000276:immunology*; D007447:Invertebrate Hormones / Q000737:chemistry*; D011487:Protein Conformation; D012471:Salivary Proteins and Peptides / Q000737:chemistry*; D019779:Salmonella enterica / Q000276:immunology*; D012486:Salmonella typhimurium / Q000276:immunology*; D013050:Spectrometry, Fluorescence
D007447:Invertebrate Hormones; D012471:Salivary Proteins and Peptides; C072490:calin; D004758:Enterobactin