PubMed:12356469 JSONTXT

{"project":"GlycoGenes","denotations":[{"id":"PD-GlycoGenes-B_T1","span":{"begin":301,"end":306},"obj":"GGDB:LARGE"},{"id":"PD-GlycoGenes-B_T2","span":{"begin":567,"end":572},"obj":"GGDB:LARGE"},{"id":"PD-GlycoGenes-B_T3","span":{"begin":1082,"end":1087},"obj":"GGDB:LARGE"}],"namespaces":[{"prefix":"GGDB","uri":"http://acgg.asia/ggdb2/"}],"text":"Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts.\nCyanovirin-N (CV-N) is under development as a topical (vaginal or rectal) microbicide to prevent sexual transmission of human immunodeficiency virus (HIV), and an economically feasible means for very large-scale production of the protein is an urgent priority. We observed that N-glycosylation of CV-N in yeast eliminated the anti-HIV activity, and that dimeric forms and aggregates of CV-N occurred under certain conditions, potentially complicating the efficient, large-scale manufacture of pure monomeric CV-N. We therefore expressed and tested CV-N homologs in which the glycosylation-susceptible Asn residue at position 30 was replaced with Ala, Gln, or Val, and/or the Pro at position 51 was replaced by Gly to eliminate potential conformational heterogeneity. All homologs exhibited anti-HIV activity comparable to wild-type CV-N, and the Pro51Gly homologs were significantly more stable proteins. These glycosylation-resistant, functional cyanovirins should be amenable to large-scale production either in bacteria or in eukaryotic hosts."}

{"project":"Lectin_function","denotations":[{"id":"T1","span":{"begin":23,"end":35},"obj":"GL_000336"},{"id":"T2","span":{"begin":101,"end":113},"obj":"GL_000336"}],"text":"Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts.\nCyanovirin-N (CV-N) is under development as a topical (vaginal or rectal) microbicide to prevent sexual transmission of human immunodeficiency virus (HIV), and an economically feasible means for very large-scale production of the protein is an urgent priority. We observed that N-glycosylation of CV-N in yeast eliminated the anti-HIV activity, and that dimeric forms and aggregates of CV-N occurred under certain conditions, potentially complicating the efficient, large-scale manufacture of pure monomeric CV-N. We therefore expressed and tested CV-N homologs in which the glycosylation-susceptible Asn residue at position 30 was replaced with Ala, Gln, or Val, and/or the Pro at position 51 was replaced by Gly to eliminate potential conformational heterogeneity. All homologs exhibited anti-HIV activity comparable to wild-type CV-N, and the Pro51Gly homologs were significantly more stable proteins. These glycosylation-resistant, functional cyanovirins should be amenable to large-scale production either in bacteria or in eukaryotic hosts."}