Search

The supercritical carbon dioxide foaming characteristics of the biodegradable polymer poly(3-hydroxybutyrate-co-4-hydroxybutyrate) (P(3HB-co-4HB)) are studied for environmentally friendly packaging materials. The effect of the 4HB composition of the P(3HB-co-4HB) copolymers on the foaming conditions such as pressure and temperature is studied and the density and the expansion ratio of the resulting P(3HB-co-4HB) foam are together evaluated. The increase in the 4HB content reduces the crystallinity and tan δ value of P(3HB-co-4HB) required for the growth of the foam cells. Therefore, the foaming temperature needs to be lower to retain a suitable tan δ value of P(3HB-co-4HB) for foaming. It was found that P(3HB-co-4HB) with less crystallinity showed better formability and cell uniformity. However, foaming is not possible regardless of the foaming temperature when the 4HB content of P(3HB-co-4HB) is over 50%, due to the high tan δ value. A lower foam density and higher expansion ratio can be obtained with crystalline P(3HB-co-4HB) of low 4HB content, compared with non-crystalline P(3HB-co-4HB) of high 4HB content. The expansion ratio of P(3HB-co-4HB) foams can be increased slightly by using a chain extender, due to the lowing of crystallinity and tan δ. This is most effective in the case of P(3HB-co-4HB), whose 4HB content is 16%. [ABSTRACT FROM AUTHOR]

Results demonstrate that carbon storage regulator A positively regulates acetyl or phosphotransacetylase in Escherichia coli. Data also point out that a metabolic stress is created by the interplay of carbon flux imbalance, inhibition of amino acid uptake, and a deficient acetate metabolism.

A trans factor for osmoregulation, OmpR, appears responsible for negatively regulating flagellar expression after phosphorylation with acetyl phosphate as a regulatory effector. The internal level of acetyl phosphate modulates flagellar expression at the flhDC master operon's transcription through the direct interaction of the promoter region of flhDC and OmpR. External addition of acetate also modulates flhDC transcription.

Binding of meningitis-causing Escherichia coli K1 to human brain microvascular endothelial cells (HBMEC) contributes to traversal of the blood-brain barrier, which occurs in part by the mannose-sensitive binding of FimH. In this study, we showed that FimH also binds to HBMEC, independent of mannose, and identified ATP synthase beta-subunit and actin proteins from the surface biotinylated HBMEC as the mannose-insensitive binding targets for FimH. Co-immunoprecipitation experiments in the presence of alpha-methyl mannose verified the binding of FimH to ATP synthase beta-subunit of HBMEC. ATP synthase beta-subunit antibody decreased E. coli K1 binding to HBMEC in the presence of alpha-methyl mannose. Taken together, these findings demonstrate that FimH of E. coli K1 binds to HBMEC in both mannose-sensitive and -insensitive manner.

Escherichia coli K1 invasion of brain microvascular endothelial cells (BMEC) is a prerequisite for penetration into the central nervous system. We previously have shown that outer membrane protein A (OmpA) and cytotoxic necrotizing factor-1 (CNF1) contribute to E. coli K1 invasion of BMEC. In this study we constructed a double-knockout mutant by deleting ompA and cnf1. We demonstrated that the double-knockout mutant was significantly less invasive in human BMEC as compared with its individual Delta ompA and Delta cnf1 mutants, suggesting that the contributions of OmpA and CNF1 to BMEC invasion are independent of each other. In addition, we showed that OmpA treatment of human BMEC resulted in phosphatidylinositol 3-kinase (PI3K) activation with no effect on RhoA, while CNF1 treatment resulted in RhoA activation with no effect on PI3K, supporting the concept that OmpA and CNF1 contribute to E. coli K1 invasion of BMEC using different mechanisms. This concept was further confirmed by using both PI3K inhibitor (LY294002) and Rho kinase inhibitor (Y27632), which exhibited additive effects on inhibiting E. coli K1 invasion of BMEC. We isolated a 96KD OmpA interacting human BMEC protein by affinity chromatography using purified OmpA, which was identified as gp96 protein, a member of the HSP90 family. This receptor differed from the CNF1 receptor (37LRP) identified from human BMEC. Taken together, these data indicate that OmpA and CNF1 contribute to E. coli K1 invasion of BMEC in an additive manner by interacting with different BMEC receptors and using diverse host cell signaling mechanisms.