The HIV-inactivating protein, cyanovirin-N, does not block gp120-mediated virus-to-cell binding.

Mariner, J.M., McMahon, J.B., O'Keefe, B.R., Nagashima, K., Boyd, M.R.: Biochem.Biophys.Res.Comm. 248: 841-845, 1998.

Abstract:

Concentrations of the potent, HIV(human immunodeficiency virus) inactivating protein, cyanovirin-N (CV-N), which completely inhibit HIV-1 infectivity, do not block the binding of soluble CD4-receptor (sCD4) to HIV-1 lysates nor the attachment of intact HIV-1 virions to several target T-cell lines. Furthermore, in contrast to the known disassociative effects of sCD4 on viral enveleope glycoproteins, treatment of HIVRF with high concentrations of CV-N results in complete viral inactivation but without apparent shedding of gp120 or other ultrastructural changes. These results are consistent with the view that the virucidal effects of CV-N result from interference with step(s) in the fusion process subsequent to the initial binding of the virus to target cells.

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