Antibody recognition of the glycoprotein g of viral haemorrhagic septicemia virus (VHSV) purified in large amounts from insect larvae

<p>Abstract</p> <p>Background</p> <p>There are currently no purification methods capable of producing the large amounts of fish rhabdoviral glycoprotein G (gpG) required for diagnosis and immunisation purposes or for studying structure and molecular mechanisms of action of this molecule (ie. pH-dependent membrane fusion). As a result of the unavailability of large amounts of the gpG from viral haemorrhagic septicaemia rhabdovirus (VHSV), one of the most dangerous viruses affecting cultured salmonid species, research interests in this field are severely hampered. Previous purification methods to obtain recombinant gpG from VHSV in <it>E. coli</it>, yeast and baculovirus grown in insect cells have not produced soluble conformations or acceptable yields. The development of large-scale purification methods for gpGs will also further research into other fish rhabdoviruses, such as infectious haematopoietic necrosis virus (IHNV), spring carp viremia virus (SVCV), hirame rhabdovirus (HIRRV) and snakehead rhabdovirus (SHRV).</p> <p>Findings</p> <p>Here we designed a method to produce milligram amounts of soluble VHSV gpG. Only the transmembrane and carboxy terminal-deleted (amino acid 21 to 465) gpG was efficiently expressed in insect larvae. Recognition of G21-465 by ß-mercaptoethanol-dependent neutralizing monoclonal antibodies (N-MAbs) and pH-dependent recognition by sera from VHSV-hyperimmunized or VHSV-infected rainbow trout (<it>Oncorhynchus mykiss</it>) was demonstrated.</p> <p>Conclusions</p> <p>Given that the purified G21-465 conserved some of its most important properties, this method might be suitable for the large-scale production of fish rhabdoviral gpGs for use in diagnosis, fusion and antigenicity studies.</p

Scaling laws for localized pattern formation in optical bistability

We study the kinetics of transverse pattern formation in a passive ring cavity containing two-level atoms. Parameters are chosen such that the Turing instabilities are on the upper and lower branches of a bistable domain and close to the limit points, so that the interaction between the long-wavelength modes includes the homogeneous mode. This leads to the formation of a localized structure which connects the two stable branches of the homogeneous bistable solution. The kinetics of this pattern formation is described by simple scaling laws.info:eu-repo/semantics/publishe

SEARCH: a phase III, randomized, double-blind, placebo-controlled trial of sorafenib plus erlotinib in patients with advanced hepatocellular carcinoma

Purpose To compare the clinical outcomes of sorafenib plus either erlotinib or placebo in patients with advanced hepatocellular carcinoma (HCC) in a multicenter, multinational, randomized, phase III trial.&lt;p&gt;&lt;/p&gt; Patients and Methods Patients with advanced HCC and underlying Child-Pugh class A cirrhosis, who were naive to systemic treatment (N = 720), were randomly assigned to sorafenib plus either erlotinib (n = 362) or placebo (n = 358). The primary end point was overall survival (OS).&lt;p&gt;&lt;/p&gt; Results Median OS was similar in the sorafenib plus erlotinib and sorafenib plus placebo groups (9.5 v 8.5 months, respectively; hazard ratio [HR], 0.929; P = .408), as was median time to progression (3.2 v 4.0 months, respectively; HR, 1.135; P = .18). In the sorafenib/erlotinib arm versus the sorafenib/placebo arm, the overall response rate trended higher (6.6% v 3.9%, respectively; P = .102), whereas the disease control rate was significantly lower (43.9% v 52.5%, respectively; P = .021). The median durations of treatment with sorafenib were 86 days in the sorafenib/erlotinib arm and 123 days in the sorafenib/placebo arm. In the sorafenib/erlotinib and sorafenib/placebo arms, the rates of treatment-emergent serious AEs (58.0% v 54.6%, respectively) and drug-related serious AEs (21.0% v 22.8%, respectively) were similar. AEs matched the known safety profiles of both agents, but rates of rash/desquamation, anorexia, and diarrhea were higher in the sorafenib/erlotinib arm, whereas rates of alopecia and hand-foot skin reaction were higher in the sorafenib/placebo arm. Withdrawal rates for AEs during cycles 1 to 3 were higher in the sorafenib/erlotinib arm.&lt;p&gt;&lt;/p&gt; Conclusion Adding erlotinib to sorafenib did not improve survival in patients with advanced HCC.&lt;p&gt;&lt;/p&gt

Une nouvelle plateforme d’an alyse moléculaire pour le diagnostic médical basée sur la nanolithographie douce et la biodétection optique sans marquage

International audienceIn this article, we show that by biopatterning probe molecules at the nanoscale using soft lithography, protein biochips can be produced at a significantly lower cost for their use as a systematic method of molecular analysis for medical diagnosis purposes. The combination of multiplexed nanoscale microcontact printing and label-free optical detection using the principle of light diffraction is implemented for generating engineered glass slides for analysis, and a dedicated diffractive scanner for reading the multiplexed results of an assay.Une nouvelle plateforme d'analyse molé culaire pour le diagnostic mé dical basé e sur la nanolithographie douce et la biodé tection optique sans marquage Ré sumé : Dans ce travail nous montrons que la structuration à l'é chelle nanomé trique de biomolé-cules sondes par lithographie douce permet de fabriquer des puces à proté ines à un coû t de production suffisamment ré duit pour entrevoir leur utilisation dans le domaine de l'analyse molé culaire mé dicale. La combinaison d'un procé dé d'impression molé culaire et d'une dé tection optique sans marquage fondé e sur le principe de la diffraction de la lumiè re est mise en oeuvre afin de produire des supports d'analyse en verre comportant des motifs nanomé tri-ques et un scanner de diffraction qui permet la lecture d'un test biolo-gique multiplexé. Abstract: In this article, we show that by biopatterning probe molecules at the nanoscale using soft lithography, protein biochips can be produced at a significantly lower cost for their use as a systematic method of molecular analysis for medical diagnosis purposes. The combination of multiplexed nano-scale microcontact printing and label-free optical detection using the principle of light diffraction is implemented for generating engineered glass slides for analysis, and a dedicated diffractive scanner for reading the multiplexed results of an assay