Isolation and characterization of Myrianthus holstii lectin, a potent HIV-1 inhibitory protein from the plant Myrianthus holstii

Romila D. Charan, Murray H. G. Munro, Barry R. O'Keefe, Raymond C. Sowder II, Tawnya C. McKee, Michael J. Currens, Lewis K. Pannell, and Michael R. Boyd: J.Nat.Prod. 63: 1170-1174, 2000.

Abstract:

Aqueous extracts from the African plant Myrianthus holstii potently inhibited the infection of the T-lymphoblastoid cell line, CEM-SS, by human immunodeficiency virus-1RF (HIV-1RF). The active constituent, M. holstii lectin (MHL), was purified by LH-20 column chromatography and reversed phase HPLC. MHL, a 9284-Da cysteine-rich protein, was characterized by amino acid analysis, N-terminal sequencing, ESIMS, and matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry. Pure MHL had anti-HIV activity, with an EC50 value of 150 nM. Delaying the addition of MHL for up to 8 h after initial exposure of CEM-SS cells to virus did not result in loss of the antiviral activity; however, if addition of the compound was delayed for 16 h or more, there was a marked decrease in the antiviral activity. MHL bound to a virus-free, soluble form of the viral envelope protein gp120 but did not inhibit the subsequent binding to a cell-free, soluble form of the cellular receptor CD4.

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