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Structure and Glycan Binding of a New Cyanovirin-N Homolog.

Structure and Glycan Binding of a New Cyanovirin-N Homolog.
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Matei E, Basu R, Furey W, Shi J, Calnan C, Aiken C, Gronenborn AM,


Matei E, Basu R, Furey W, Shi J, Calnan C, Aiken C, Gronenborn AM, (click to view)

Matei E, Basu R, Furey W, Shi J, Calnan C, Aiken C, Gronenborn AM,

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The Journal of biological chemistry 2016 07 07291(36) 18967-76 doi 10.1074/jbc.M116.740415

Abstract

The HIV-1 envelope glycoprotein gp120 is heavily glycosylated and bears numerous high mannose sugars. These sugars can serve as targets for HIV-inactivating compounds, such as antibodies and lectins, which bind to the glycans and interfere with viral entry into the target cell. We determined the 1.6 Å x-ray structure of Cyt-CVNH, a recently identified lectin from the cyanobacterium Cyanothece(7424), and elucidated its glycan specificity by NMR. The Cyt-CVNH structure and glycan recognition profile are similar to those of other CVNH proteins, with each domain specifically binding to Manα(1-2)Manα units on the D1 and D3 arms of high mannose glycans. However, in contrast to CV-N, no cross-linking and precipitation of the cross-linked species in solution was observed upon Man-9 binding, allowing, for the first time, investigation of the interaction of Man-9 with a member of the CVNH family by NMR. HIV assays showed that Cyt-CVNH is able to inhibit HIV-1 with ∼4-fold higher potency than CV-N(P51G), a stabilized version of wild type CV-N. Therefore, Cyt-CVNH may qualify as a valuable lectin for potential microbicidal use.

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