Bovine lactoferrin (BLf) prevents the infection of some enveloped and naked viruses. To identify BLf sequences responsible for the antiviral activity, we tested 31 HPLC fractions, derived from tryptic digestion of BLf, toward herpes simplex virus type 1 (HSV-1). Only a few HPLC purified fragments were active against HSV-1, even if at lower extent than the native undigested BLf. Two large fragments, one corresponding to the C-lobe (amino acid sequence 345-689) and the other corresponding to a large portion of the N-lobe (1-280), were inhibitors of HSV-1 infection, while a smaller part of the N-lobe (86-258) was ineffective. Among the low-molecular-weight fragments, only two small peptides, which coeluted in a single chromatographic peak, were effective towards HSV-1. These peptides, both present in the N-lobe, were identified as peptides 222-230 (ADRDQYELL) and 264-269 (EDLIWK). The same peptides, chemically synthesised, were able to inhibit HSV-1 infection only when they were assayed in association.
Copyright 1999 Academic Press.