Journal of Antivirals & Antiretrovirals
Open Access
ISSN: 1948-5964
+44 1300 500008
ISSN: 1948-5964
+44 1300 500008
Lectin is a protein that specifically bound and cross-linked with carbohydrates and is involved in the activation of the lectin pathway which is considered a part of both innate and adaptive immunity. Lectin also has a role in plant defense system. In this study, lectin was isolated from Euphorbia and purified through aqueous extraction, ammonium sulfate precipitation, dialysis, filtration on superdex 75, ion exchange chromatography on SP-sepharose gel.
The study showed that lectin exhibits hemagglutination activity towards rabbit erythrocytes on concentration 50 μg/ml. This hemagglutination activity was retained by lectin till 60°C. Effect of pH, and denaturalizing agent on lectin was also studied, and found to have a low pH range (6-8). Molecular weight was determined for lectin using SDS gel-electrophoresis and found to be 30 KD, and determined by gel filtration to be 60 KD, indicating that lectin is homodimer in the plant.
Cytotoxicity assay of Euphorbia on the vero cell lines using MTT, was also studied and revealed that using a concentration till 100 μg/ml of Euphorbia was within the safe limit. Also the determination of antiviral activity of the Euphorbia lectin against HSV1 on vero cell lines was investigated using plaque reduction assay and MTT, showing 76% of virus inhibition. Mechanism of action of the effect of lectin on HSV1 was also investigated using MTT, and RT-PCR.
The study also showed that lectin affected the virus entry and attachment phase. This inhibition of the virus was totally diminished when the lectin was combined with EDTA before infection with HSV1.
Antiproliferative activity of Euphorbia was also studied against human cancer cell line by MTT assay.
The gene(s) encoding the lectin was isolated by PCR, which revealed that lectin is actually encoded by multi gene family.