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Directed Evolution of gp120 Binding Mutants of the Lectin Cyanovirin-N

Abstract Cyanovirin-N (CV-N) is a naturally occurring lectin originally isolated from the cyanobacteria Nostoc ellipsosporum. This 11 kDa lectin is 101 amino acids long with two binding sites, one at each end of the protein. CV-N specifically binds to terminal Manα1-2Manα motifs on the branched, high mannose Man9 and Man8 glycosylations found on enveloped viruses including Ebola, Influenza, and HIV. wt-CVN has micromolar binding to soluble Manα1-2Manα and also inhibits HIV entry at low nanomolar concentrations. CV-N's high affinity and specificity for Manα1-2Manα makes it an excellent lectin to study for its glycan-specific properties. The long-term aim of this project is to make a vari... (more)
Created Date 2013
Contributor Ruben, Melissa (Author) / Ghirlanda, Giovanna (Advisor) / Allen, James (Committee member) / Wachter, Rebekka (Committee member) / Arizona State University (Publisher)
Subject Biochemistry / cyanovirin-N / phage display
Type Doctoral Dissertation
Extent 88 pages
Language English
Reuse Permissions All Rights Reserved
Note Ph.D. Biochemistry 2013
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS

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Description Dissertation/Thesis