Cyanovirin-N (CV-N)

Cyanovirin-N is a small (11 kDa), two-domain lectin originally isolated from the cyanobacterium Nostoc ellipsosporum[6][2]. It specifically binds to α(1-2)-linked oligomannose structures on viral surface glycoproteins, most notably the envelope glycoprotein gp120 of human immunodeficiency virus (HIV), and can also bind oligosaccharides on other viral glycoproteins (e.g., influenza hemagglutinin)[5][8]. By binding these carbohydrates, cyanovirin-N blocks the interaction between the virus and target cell receptor(s), thereby potently inhibiting viral entry and cell-to-cell fusion[2][5][4]. CV-N is highly stable and resistant to denaturation, and its antiviral activity is observed at low nanomolar concentrations. Structurally, it comprises two quasi-symmetric domains, each containing distinct carbohydrate binding sites with different sugar affinities[6][1]. Cyanovirin-N and its homologs (CVNH family) are of interest as potential antiviral therapeutics, particularly for topical or microbicidal applications against HIV and other enveloped viruses[5][6][8]. It is not a classic receptor, enzyme, or transporter, but a non-mammalian, carbohydrate-binding protein with therapeutic potential in infectious disease[2][4][6]. Caveats: Cyanovirin-N is not a human protein, but a protein derived from cyanobacteria[2][5]. It is not currently a marketed drug target; most data is preclinical or experimental[2][5][4]. Interacting drugs are only experimental carbohydrate analogs used as molecular probes[2].

Other names

CV-N

Binds to high-mannose glycans on viral envelope glycoproteins (e.g., HIV gp120), blocking essential interactions between the virus and host cell receptors, preventing viral entry[2][5][6][4].