6533b85ffe1ef96bd12c0f81
RESEARCH PRODUCT
The Galactose-Specific Lectin from the Sponge Chondrilla Nucula Displays Anti-Human Immunodeficiency Virus Activity in vitro via Stimulation of the (2′-5′)Oligoadenylate Metabolism
B. KurelecW. E. G. MüllerZoran KljajićBarbara E. WeilerM. J. GasicGerhard UhlenbruckH. C. Schrödersubject
0301 basic medicinebiology2'-5'-Oligoadenylate030106 microbiologyLectinGeneral MedicineGlutamic acidbiology.organism_classification01 natural sciencesIn vitro0104 chemical sciences010404 medicinal & biomolecular chemistry03 medical and health sciencesIsoelectric pointBiochemistryConcanavalin ACell culturebiology.proteinChondrilla nuculadescription
A new lectin has been isolated from the sponge Chondrilla nucula. The purified CN lectin is a protein composed of four polypeptide chains with a molecular weight (MW) of 15600. The isoelectric point is 4.5 and the amino acid composition is rich in aspartic and glutamic acid. The lectin precipitates erythrocytes from humans (A, B, O) with a titre between 25 and 210. The CN lectin is d-galactose-specific and displays a moderate mitogenic effect on spleen lymphocytes from mice and on CD4-positive human H9 cells. An interesting feature of this lectin is its ability to stimulate the (2′-5′)oligoriboadenylate [(2′-5′)A] metabolic pathway in non-infected and human immunodeficiency virus (HIV-1)-infected H9 cells. Moreover, HIV-1-infected H9 cells show an increase in the time period of HIV-1 release in response to CN lectin treatment. These data suggest that CN lectin causes a retardation of HIV-1 release due to further increase of the elevated intracellular level of (2′-5′)A.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1990-04-01 | Antiviral Chemistry and Chemotherapy |