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Structural studies of algal lectins with anti-HIV activity

100%

Ziółkowska N. E., Wlodawer A.

2006

vol. 53

issue 4

617-626

A number of antiviral lectins, small proteins that bind carbohydrates found on viral envelopes, are currently in pre-clinical trials as potential drugs for prevention of transmission of human immunodeficiency virus (HIV) and other enveloped viruses, such as the Ebola virus and the coronavirus responsible for severe acute respiratory syndrome (SARS). Lectins of algal origin whose antiviral properties make them candidate agents for prevention of viral transmission through topical applications include cyanovirin-N, Microcystis viridis lectin, scytovirin, and griffithsin. Although all these proteins exhibit significant antiviral activity, their structures are unrelated and their mode of binding of carbohydrates differs significantly. This review summarizes the current state of knowledge of the structures of algal lectins, their mode of binding of carbohydrates, and their potential medical applications.

A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa

100%

Zhang G. Q., Sun J., Wang H. X., Ng T. B.

issue 3

415-421

Little was known about biological activities of compounds from the medicinal mushroom of the genus Pholiota. A lectin from the Pholiota adiposa has now been isolated and its properties tested. The isolation procedure included ion exchange chromatography on DEAE-cellulose and CM-cellulose, and fast protein liquid chromatography-gel filtration (FPLC) on Superdex 75. The lectin was composed of two identical subunits, each with a molecular mass of 16 kDa. Its N-terminal amino-acid sequence showed little similarity to sequences of other Agaricales lectins. The hemagglutinating activity of the lectin was stable at temperatures up to 50°C, and in NaOH and HCl solutions with concentrations less than 25 mM. It was inhibited by inulin (12.5-200 mM), but enhanced by Cu2+ (6.25-25 mM), Fe2+ (12.5-25 mM), and Al3+ (6.25-25 mM) ions. The lectin showed antiproliferative activity toward hepatoma Hep G2 cells and breast cancer MCF7 cells with an IC50 of 2.1 µM and approximately 3.2 µM, respectively. It exhibited HIV-1 reverse transcriptase inhibitory activity with an IC50 of 1.9 µM. When compared with P. aurivella lectin, the only Pholiota lectin published to date, P. adiposa lectin differs in chromatographic behavior, molecular mass, N-terminal sequence, and effect of cations on hemagglutinating activity. In the case of the lectin from P. aurivella, its antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities have not been determined.

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2 Acta Biochimica Polonica

1 2009

1 2006

1 Ng T. B.

1 Sun J.

1 Wang H. X.

1 Wlodawer A.

1 Zhang G. Q.

1 Ziółkowska N. E.

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Structural studies of algal lectins with anti-HIV activity

A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa