Lysozyme and RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin

Human chorionic gonadotropin (hCG) preparations contain activity against HI T: type 1 (HIV-1). However, there has been controversy about whether some b iological activities of hCG beta-subunit (hCG beta) preparations are caused by the beta-subunit itself or other proteins present in the preparations, We report here the purification, characterization, and identification of th ree enzymes with anti-HIV activity present in the beta-core fraction of hCG beta prepared from the urine of pregnant women. The N-terminal amino acid sequence of one protein is identical to human urinary lysozyme C, and those of the other two are identical to human RNase A and urinary RNase U. We th us refer to these proteins as AVL (antiviral lysozyme) and AVR (antiviral R Nases). In addition to HIV-1 inhibition, AVL is capable of lysing Micrococc us lysodeikticus. AVR digests a variety of RNA substrates, including RNA fr om HIV-1-infected cells. We also find that lysozyme from chicken egg white, human milk and human neutrophils and RNase A from bovine pancreas possess activity against HIV-I. These findings may offer additional strategies for the treatment of HIV-1 infection.