Polymeric collagen isolated from squid (Loligo peallii) connective tissue

Résumé On a isolé du collagène naturel et polymère du tissu du manteau du calmarLoligo peallii par la méthode de Nishihara, les fibres présentant au microscope électronique une périodicité de 680 Å. Le collagène a une composition typique d'amino acides et contient l'hydrate de carbone dans une proportion restreinte; principalement sous forme de glucose et de galactose.     

Conversion of psoralen DNA monoadducts in E. coli to interstrand DNA cross links by near UV light (320–360 nm): Inability of angelicin to form cross links,in vivo

Summary Both angelicin and psoralen monoadducts formed in vivo in E. coli by near UV light produce lethal and mutagenic effects. However psoralen monoadducts are converted to cross links by higher doses of UV; angelicin monoadducts are not. The relevance of these results to psoralen photosensitization is discussed.Supported by the National Research Council of Canada.     

Isoguvacine,isonipecotic acid,muscimol and N-methyl isoguvacine on the GABA receptor in rat sympathetic ganglia

Summary The GABA-mimetic activities of 4 analogues muscimol, isonipecotic acid, isoguvacine and N-methyl isoguvacine have been examined at the GABA receptor in the rat isolated superior cervical ganglion. The depolarizing action of all 4 analogues could be selectively antagonized by bicuculline methochloride and isopropyl bicyclophosphate. Muscimol was the only analogue more potent than GABA (molar potency ratio=5.08±0.707). The potency of isoguvacine was 0.23±0.026 and isonipecotic acid 0.011±0.0028. N.-methyl isoguvacine was <0.001 GABA.     

Structural basis of West Nile virus neutralization by a therapeutic antibody

West Nile virus is a mosquito-borne flavivirus closely related to the human epidemic-causing dengue, yellow fever and Japanese encephalitis viruses. In establishing infection these icosahedral viruses undergo endosomal membrane fusion catalysed by envelope glycoprotein rearrangement of the putative receptor-binding domain III (DIII) and exposure of the hydrophobic fusion loop. Humoral immunity has an essential protective function early in the course of West Nile virus infection. Here, we investigate the mechanism of neutralization by the E16 monoclonal antibody that specifically binds DIII. Structurally, the E16 antibody Fab fragment engages 16 residues positioned on four loops of DIII, a consensus neutralizing epitope sequence conserved in West Nile virus and distinct in other flaviviruses. The E16 epitope protrudes from the surface of mature virions in three distinct environments, and docking studies predict Fab binding will leave five-fold clustered epitopes exposed. We also show that E16 inhibits infection primarily at a step after viral attachment, potentially by blocking envelope glycoprotein conformational changes. Collectively, our results suggest that a vaccine strategy targeting the dominant DIII epitope may elicit safe and effective immune responses against flaviviral diseases.