Identification of an aprotinin antiviral domain

Abstract

Digestion of the proteinase inhibitor aprotinin, by clostripain, a cysteine proteinase, yielded five oligopeptide fragments. Two fragments exhibited both antiviral and antibacterial activities, two fragments only antiviral activity, and one fragment showed no antimicrobial activity. One of the former oligopeptides showed antiviral activity against human herpes simplex virus type 1 and bovine parainfluenza virus type 3. It consisted of the hexapeptide Y-F-Y-N-A-K corresponding to amino acids 21-26 of intact aprotinin. An identical synthetic pcptide had the same antiviral spectrum as the natural hexapeptide, exhibited no antibacterial activity, and was also devoid of trypsin inhibiting activity. Intact aprotinin, in contrast, is ineffective against human herpes simplex virus 1 and bovine parainfluenza virus 3 but possesses antibacterial properties against several bacterial species [(1992) J. Appl. Bact. 72,[180][181][182][183][184][185][186][187].

Plasmid DNA nicking- a Novel Activity of Soybean Trypsin Inhibitor and Bovine Aprotinin

“…A recent report on structure-function relationship of ORB, a short inhibitor with AM activity isolated from skin secretions of Odorrana grahami, proposed AM activity was independent of TI activity 25 . Similar observation was made from structural studies with bovine aprotinin 26,27 . AM proteins were also thought to act through cell wall and/or membrane disruption but recent experiments have revealed a diversity of mechanisms 15 .…”

“…Following clostripain digestion, one antiviral and three antibacterial peptides were isolated by Pellegrini et al . 26,27 . All three peptides, P1–15 (includes PI site Lys15), P18–P39 and P40–58, showed AM activity with peptide P18–39 being the most active.…”

Different modes of inhibition of human adenovirus proteinase, probably a cysteine proteinase, by bovine pancreatic trypsin inhibitor

“…This was to be expected as one outstanding property of BPTI is its uncommon stability to proteolytic degradation by other proteinsase [22]. BPTI is known to have antimicrobial and antiviral activities [29]; the observations reported here may be relevent as to how BPTI may accomplish this.…”

A Protease Inhibitor of the Kunitz Family from Skin Secretions of the Tomato Frog, Dyscophus guineti (Microhylidae)

“…The broad spectrum antimicrobial activities of several proteinase inhibitors has been described. BPTI shows growth inhibitory activity against a range of Grampositive and Gram-negative strains (25) and antiviral activity against human herpes simplex virus and bovine parainfluenza virus (26). Similarly, antileukoprotease, a protein produced by keratinocytes that prevents degradation of extracellular matrix proteins by inhibiting neutrophil-derived serine proteases, is activity against several microorganisms associated with skin, such as Psuedomonas aeruginosa, Staphylococcus aureus, Staphylococcus epidermis, and Candida albicans (27).…”