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Contributo in rivista
Tipo: Articolo in rivista
Titolo: Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection.
Anno di pubblicazione: 2001
Autori: Superti F; Siciliano R; Rega B; Giansanti F; Valenti P; Antonini G.
Affiliazioni autori: Department of Ultrastructures, Istituto Superiore di SanitaŠ, I-00161 Rome, Italy Institute of Food Science and Technology, CNR, I-83100 Avellino, Italy Department of Basic and Applied Biology, University of L'Aquila, Coppito, I-67010 L'Aquila, Italy Institute of Microbiology, II University of Naples, I-80135 Naples, Italy
Abstract: Although the antiviral activity of lactoferrin is one of the major biological functions of this iron binding protein, the mechanism of action is still under debate. We have investigated the role of metal binding, of sialic acid and of tryptic fragments of bovine lactoferrin (bLf) in the activity towards rotavirus (intestinal pathogen naked virus) infecting enterocyte-like cells. The antiviral activity of bLf fully saturated with manganese or zinc was slightly decreased compared to that observed for apo- or iron-saturated bLf. The antiviral activity of differently metal-saturated bLf towards rotavirus was exerted during and after the virus attachment step. The removal of sialic acid enhanced the anti-rotavirus activity of bLf. Among all the peptidic fragments obtained by tryptic digestion of bLf and characterised by advanced mass spectrometric methodologies, a large fragment (86-258) and a small peptide (324-329: YLTTLK) were able to inhibit rotavirus even if at lower extent than undigested bLf.
Lingua abstract: inglese
Pagine da: 107
Pagine a: 115
Pagine totali: 9
Biochimica et biophysica acta. G, General subjects
Elsevier Scientific Publ. Co.
Numero volume: 1528
Referee: Sė: Internazionale
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