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Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development

Title: Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development
Authors: Boyd, M R; Gustafson, K R; McMahon, J B; Shoemaker, R H; O'Keefe, B R; Mori, T; Gulakowski, R J; Wu, L; Rivera, M I; Laurencot, C M; Currens, M J; Cardellina, J H; Buckheit, R W; Nara, P L; Pannell, L K; Sowder, R C; Henderson, L E
Source: Antimicrobial Agents and Chemotherapy ; volume 41, issue 7, page 1521-1530 ; ISSN 0066-4804 1098-6596
Publisher Information: American Society for Microbiology
Publication Year: 1997
Description: We have isolated and sequenced a novel 11-kDa virucidal protein, named cyanovirin-N (CV-N), from cultures of the cyanobacterium (blue-green alga) Nostoc ellipsosporum. We also have produced CV-N recombinantly by expression of a corresponding DNA sequence in Escherichia coli. Low nanomolar concentrations of either natural or recombinant CV-N irreversibly inactivate diverse laboratory strains and primary isolates of human immunodeficiency virus (HIV) type 1 as well as strains of HIV type 2 and simian immunodeficiency virus. In addition, CV-N aborts cell-to-cell fusion and transmission of HIV-1 infection. Continuous, 2-day exposures of uninfected CEM-SS cells or peripheral blood lymphocytes to high concentrations (e.g., 9,000 nM) of CV-N were not lethal to these representative host cell types. The antiviral activity of CV-N is due, at least in part, to unique, high-affinity interactions of CV-N with the viral surface envelope glycoprotein gp120. The biological activity of CV-N is highly resistant to physicochemical denaturation, further enhancing its potential as an anti-HIV microbicide.
Document Type: article in journal/newspaper
Language: English
DOI: 10.1128/aac.41.7.1521
DOI: 10.1128/AAC.41.7.1521
Availability: https://doi.org/10.1128/aac.41.7.1521; https://journals.asm.org/doi/pdf/10.1128/AAC.41.7.1521
Rights: https://journals.asm.org/non-commercial-tdm-license
Accession Number: edsbas.84E7D0DC
Database: BASE