Xy. Ye et Tb. Ng, Isolation of unguilin, a cyclophilin-like protein with anti-mitogenic, antiviral, and antifungal activities, from black-eyed pea, J PROTEIN C, 20(5), 2001, pp. 353-359
A protein designated unguilin was isolated from seeds of the black-eyed pea
(Vigna unguiculata). It possesses a molecular weight of 18 kDa and an N-te
rminal sequence resembling that of cyclophilins and the cyclophilin-like an
tifungal protein from mung beans, and was adsorbed on Affi-gel blue gel and
CM-Sepharose. Unguilin exerted an antifungal effect toward fungi including
Coprinus comatus, Mycosphaerella arachidicola, and Botrytis cinerea. In ad
dition, unguilin was capable of inhibiting human immunodeficiency virus-1 r
everse transcriptase and the glycohydrolases alpha- and beta -glucosidases
which are involved in HIV infection. Unguilin was devoid of lectin and ribo
nuclease activities. It inhibited methyl-H-3-thymidine uptake by mouse sple
nocytes and it weakly inhibited translation in a rabbit reticulocyte lysate
system. Unguilin resembles mungin in some aspects, but differs from it in
others.