title: Role of Cathelicidin Peptides in Bovine Host Defense and Healing.
abstract: The in vitro antimicrobial activities and biological effects on host cells were compared for the bovine cathelicidins BMAP-28, an alpha-helical AMP, and Bac5 and Bac7, proline-rich AMPs. Our results confirm that the broad-spectrum activity of BMAP-28 correlates with a high capacity to interact with and permeabilize bacterial membranes, whereas the proline-rich AMPs selectively internalize into the cytoplasm of susceptible Gram-negative bacteria with a non-lytic mechanism. All peptides efficiently translocated into mammalian fibroblastic cells, but while Bac5 and Bac7(1-35) localized to nuclear structures and induced cellular proliferation, BMAP-28 associated with mitochondria and did not induce proliferation. Moreover, BMAP-28 was considerably more cytotoxic than the proline-rich peptides due to cytolytic and pro-apoptotic effects. Our results highlight important functional differences among the bovine cathelicidins and suggest that they contribute to an integrated response of the host to infection, with distinct but complementary activities.
authors.affiliation: Department of Biomedical Science and Biotechnology, University of Udine, Udine, Italy.
authors.forename: Linda
authors.initials: L
authors.lastname: Tomasinsig
authors.affiliation: Department of Life Sciences, University of Trieste, Trieste, Italy.
authors.forename: Monica
authors.initials: M
authors.lastname: Benincasa
authors.affiliation: Department of Life Sciences, University of Trieste, Trieste, Italy.
authors.forename: Marco
authors.initials: M
authors.lastname: Scocchi
authors.affiliation: Department of Biomedical Science and Biotechnology, University of Udine, Udine, Italy.
authors.forename: Barbara
authors.initials: B
authors.lastname: Skerlavaj
authors.affiliation: Department of Life Sciences, University of Trieste, Trieste, Italy. atossi@units.it.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Tossi
authors.affiliation: Department of Biomedical Science and Biotechnology, University of Udine, Udine, Italy.
authors.forename: Margherita
authors.initials: M
authors.lastname: Zanetti
authors.affiliation: Department of Life Sciences, University of Trieste, Trieste, Italy.
authors.forename: Renato
authors.initials: R
authors.lastname: Gennaro
keywords: Alpha-helical; Antimicrobial peptide; Cathelicidin; Membranolytic; Proline-rich