2,934 research outputs found

    Application of a Modified Brainstorming Technique

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    Our modified brainstorming technique is an assessment tool Extension professionals can use to generate new ideas. The modified brainstorming technique capitalizes on creativity at the individual level and helps maximize the contribution of the whole group. The technique leads to generation of useful ideas in a mutually supportive setting for a minimal time investment. This tool is effective for relatively small groups within Extension and may be applicable to other outreach and nonprofit organizations

    Comparison of Campylobacter coli strains isolated from pigs and humans - porcine strains a possible source of human infection?

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    The primary aim of this study was to detect and genotype Campylobacter strains from pigs and humans. AFLP (amplified fragment length polymorphism) analysis was used to compare different genotypes to identify the genetic diversity of Campylobacter coli (C. coli) strains. Heterogeneous patterns were detectable among the porcine and human C. coli pool. By using an optimized extraction method combined with a PCR it was possible to detect C. coli DNA in some samples of the investigated minced meat but it could not be distinguished between dead bacterial cells and viable but nonculturable cell (VBNC)-forms of C. coli strains

    Mutations in hepatitis C virus E2 located outside the CD81 binding sites lead to escape from broadly neutralizing antibodies but compromise virus infectivity.

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    Broadly neutralizing antibodies are commonly present in the sera of patients with chronic hepatitis C virus (HCV) infection. To elucidate possible mechanisms of virus escape from these antibodies, retrovirus particles pseudotyped with HCV glycoproteins (HCVpp) isolated from sequential samples collected over a 26-year period from a chronically infected patient, H, were used to characterize the neutralization potential and binding affinity of a panel of anti-HCV E2 human monoclonal antibodies (HMAbs). Moreover, AP33, a neutralizing murine monoclonal antibody (MAb) to a linear epitope in E2, was also tested against selected variants. The HMAbs used were previously shown to broadly neutralize HCV and to recognize a cluster of highly immunogenic overlapping epitopes, designated domain B, containing residues that are also critical for binding of viral E2 glycoprotein to CD81, a receptor essential for virus entry. Escape variants were observed at different time points with some of the HMAbs. Other HMAbs neutralized all variants except for the isolate 02.E10, obtained in 2002, which was also resistant to MAb AP33. The 02.E10 HCVpp that have reduced binding affinities for all antibodies and for CD81 also showed reduced infectivity. Comparison of the 02.E10 nucleotide sequence with that of the strain H-derived consensus variant, H77c, revealed the former to have two mutations in E2, S501N and V506A, located outside the known CD81 binding sites. Substitution A506V in 02.E10 HCVpp restored binding to CD81, but its antibody neutralization sensitivity was only partially restored. Double substitutions comprising N501S and A506V synergistically restored 02.E10 HCVpp infectivity. Other mutations that are not part of the antibody binding epitope in the context of N501S and A506V were able to completely restore neutralization sensitivity. These findings showed that some nonlinear overlapping epitopes are more essential than others for viral fitness and consequently are more invariant during earlier years of chronic infection. Further, the ability of the 02.E10 consensus variant to escape neutralization by the tested antibodies could be a new mechanism of virus escape from immune containment. Mutations that are outside receptor binding sites resulted in structural changes leading to complete escape from domain B neutralizing antibodies, while simultaneously compromising viral fitness by reducing binding to CD81

    Quantitative analysis of anti-hepatitis C virus anti body-secreting B cells in patients with chronic hepatitis C

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    Copyright © 2006 American Association for the Study of Liver DiseasesArticleHEPATOLOGY. 43(1): 91-99 (2006)journal articl
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