Disease relevance of kpsE

• The nucleotide and predicted amino acid sequences of cpxDCBA contained a high degree of homology to the capsule export genes of H. influenzae type b bexDCBA, Neisseria meningitidis group B ctrABCD, and, to a lesser extent, Escherichia coli K1 and K5 kpsE and kpsMT [1].
• The transport of group 2 capsular polysaccharides across the periplasmic space in Escherichia coli. Roles for the KpsE and KpsD proteins [2].

High impact information on kpsE

• In addition, we demonstrate that KpsD is present not only within the periplasm but is also in both the cytoplasmic and outer membrane fractions and that the correct membrane association of KpsD was dependent on KpsE, Lpp, and the secreted polysaccharide molecule [2].
• Collectively the data suggest that the trans-periplasmic export involves KpsD acting as the link between the cytoplasmic membrane transporter and the outer membrane with KpsE acting to facilitate this transport process [2].
• The transport process is independent of the repeat structure of the polysaccharide, and translocation across the periplasm requires the cytoplasmic membrane-anchored protein KpsE and the periplasmic protein KpsD [2].
• By chemical cross-linking we show that KpsE is likely to exist as a dimer and that dimerization is independent of the other Kps proteins or the synthesis of capsular polysaccharide [2].
• Complementation of mutations in the kpsE, kpsD, and kpsC genes in region 1 of the K5 capsule gene cluster by subclones of the K10 and K54 capsule gene clusters indicated that certain stages in the export of group II and I/II capsules may be conserved [3].

Chemical compound and disease context of kpsE

• Characterization and localization of the KpsE protein of Escherichia coli K5, which is involved in polysaccharide export [4].

Biological context of kpsE

• Chromosomal mutagenesis with MudJ and subsequent complementation analysis, maxicell and in vitro protein expression studies, and nucleotide sequencing identified the region 1 gene, kpsE, which encodes a 39-kDa polypeptide [5].

Anatomical context of kpsE

• Intact KpsE was extracted from the membranes of a KpsE-overexpressing recombinant strain with octyl-beta-glucoside [4].

Analytical, diagnostic and therapeutic context of kpsE

• We have also used FTIR spectroscopy and lipid phase transition temperature analysis to investigate the interaction of a peptide homologue of KpsE C-terminal region with membrane lipid [6].

References