Surface chemical composition and fibrinogen adsorption-retention properties of plasma-deposited fluoropolymer films deposited from an RF Glow Discharge

Fluoropolymer films have been deposited in the glow and afterglow regions of radio frequency glow discharges fed with C2F6−H2 mixtures. Structure, growth rate, composition, and wettability of the films have been investigated by means of atomic force microscopy, electron spectroscopy for chemical analysis, secondary ion mass spectrometry, and water contact angle measurements.125I labeled baboon fibrinogen in baboon plasma has been used to study the adsorption of the protein onto the films. Protein retention, i.e., the binding affinity of the adsorbed protein, has been examined by elution with a sodium dodecyl sulfate solution. Adsorption and retention of fibrinogen were correlated using multivariate statistical methods with the wettability, the degree of film fluorination, and the CF x (1≤x≤3) group distribution of the coatings. This correlation identified the influence of each variable on the adsorption and retention of fibrinogen onto these substrates. These variables or surface properties can be easily balanced by properly tuning the experimental conditions of the glow discharge deposition process

The role of the influenza virus RNA polymerase in host shut-off

Viruses induce an antiviral host response by activating the expression of antiviral host genes. However, viruses have evolved a wide range of strategies to counteract antiviral host responses. One of the strategies used by many viruses is the general inhibition of host gene expression, also referred to as a host shut-off mechanism. Here we discuss our recent findings that influenza virus infection results in the inhibition and degradation of host RNA polymerase II (Pol II) and that the viral RNA polymerase plays a critical role in this process. In particular, we found that Pol II is ubiquitylated in influenza virus infected cells and ubiquitylation can be induced by the expression of the RNA polymerase. Moreover, the expression of an antiviral host gene could be inhibited by the overexpression of the RNA polymerase. Both ubiquitylation and the inhibition of the host gene were dependent on the ability of the RNA polymerase to bind to Pol II. Further studies will be required to understand the interplay between the host and viral transcriptional machineries and to elucidate the exact molecular mechanisms that lead to the inhibition and degradation of Pol II as a result of viral RNA polymerase binding. These findings extend our understanding of how influenza virus counteracts antiviral host responses and underpin studies into the mechanisms by which the RNA polymerase determines virulence