Effect of Qiguiyin Decoction(芪归银方) on Multidrug-Resistant Pseudomonas aeruginosa Infection in Rats

Objective： To investigate the effect of Qiguiyin Decoction （芪归银方, QGYD） on multidrug-resistant Pseudomonas aeruginosa infection in Sprague-Dawley （SD） rats. Methods： A pseudomonal infection model in SD rats was established by injecting multidrug-resistant P. aeruginosa intraperitoneally. Infected rats were randomized into four groups treated with Pure water, QGYD, ceftazidime, or combined QGYD and ceftazidime. Blood samples were obtained from the abdominal aorta. Serum was then collected and analyzed by peptide array for immune responsiveness to multidrug-resistant beta-lactamase proteins, including Verona integronencoded metailo-beta-lactamase 1 （VIM-l）, Sao Paulo metallo-beta-lactamase 1 （SPM-1）, and Temoniera （TEMs）. Blood levels of interleukin-113 （IL-113）, interleukin-4 （IL-4）, and interferon-γ （IFN-γ） were assessed by enzyme-linked immunosorbent assay. Results： QGYD enhanced antibody reactivity against VIM-1 [epitopes 7-11 and 36-40] and TEM-1 [epitopes 26-27, 52-55, and 66-70]. QGYD treatment restored the compromised antibody reactivity against VIM-1 [epitopes 53-54 and 56-58] and SPM-1 [epitopes 16-19 and 82-85] following pseudomonal infection. Serum levels of IL-113 and Thl/＇l-h2 in the rats were significantly elevated following pseudomonal infection （P〈0.05 or P〈0.01）. In contrast, QGYD and combination QGYD and ceftazidime treatment restored the elevated serum IL-1β and Thl/-rh2 levels to normal （P〉0.05）. Conclusions： QGYD improves the immune response to pseudomonal infection in rats by stimulating the production of protective antibodies against drug-resistant proteins VIM-1, SPM-1, and TEM-1. In addition, it protects the immune system and maintains immune responsiveness by restoring IL-1β and Thl/Th2 levels.

Proteomic composition of the acrostyle＂ Novel approaches to identify cuticular proteins involved in virus-insect interactions

The acrostyle is a distinct anatomical region present on the cuticle at the inner face of the common food/salivary canal at the tip of aphid maxillary stylets. This conserved structure is of particular interest as it harbors the protein receptors of at least l plant virus, Cauliflower mosaic virus＇, and presumably has other roles in plant-insect interactions. Previously we reported immunolabeling of a highly conserved motif of cuticular proteins from the CPR family （named for the presence of a Rebers and Riddiford consensus） within the acrostyle. Here we report the development of novel tools to further study the proteomic composition of this region and to identify proteins involved in insect- virus interactions. Using a series of antibodies against cuticular proteins from the RR-2 subfamily, we identified additional peptides present within the acrostyle. Our results demonstrated that the acrostyle is a complex structure containing multiple domains of cuticular proteins accessible for interaction. In addition, an array of overlapping peptides,which covers the diversity of the majority of the RR-2 subfamily, was ~tevelopect as a generic tool to characterize cuticular protein/pathogen interactions. Upon probing this array with Cucumber mosaic virus particles, consensus peptide sequences from hybridizing peptides were identified. Use of these novel tools has extended our knowledge of the proteomic composition of insect maxillary stylets and identified sequences that could be involved in virus binding, thus contributing to further elucidation of the various properties and functions of the acrostyle.