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Title: ANTIMICROBIAL ANIONIC PEPTIDE BINDS IN VIVO TO MANNHEIMIA (PASTEURELLA) HAEMOLYTICA ATTACHED TO OVINE ALVEOLAR EPITHELIUM

Author
item Heidari, Mohammad
item Hamir, Amirali
item Cutlip, Randall
item Brogden, Kim

Submitted to: International Journal of Antimicrobial Agents
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/23/2002
Publication Date: 3/20/2002
Citation: HEIDARI, M., HAMIR, A.N., CUTLIP, R.C., BROGDEN, K.A. ANTIMICROBIAL ANIONIC PEPTIDE BINDS IN VIVO TO MANNHEIMIA (PASTEURELLA) HAEMOLYTICA ATTACHED TO OVINE ALVEOLAR EPITHELIUM. INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS. 2002. v. 20. p. 69-72.

Interpretive Summary: Respiratory tract diseases are a leading cause of loss from disease in the cattle, sheep and goat industries. Annual loss in the United States is estimated to exceed one billion dollars. Losses are from mortality, reduced feed efficiency, and slaughter condemnations, as well as prevention and treatment measures. Currently, scientists and veterinarians are looking at novel ways to prevent or treat the disease. As part of our ongoing studies, we assessed the endogenous antimicrobial peptide activity in vivo of anionic peptide. To assess this, Mannheimia haemolytica was deposited into the lungs of adult sheep, which were killed at 0, 5, 10 and 20 min for necropsy. At 0 min, M. haemolytica appeared normal, and monoclonal antibody to antimicrobial anionic peptide (AP) and Protein A- colloidal gold identified AP already bound to the bacterial surface. At 5-20 min, many organisms were distorted with flocculated intracellular constituents characteristic of AP cellular damage. On the basis of our findings, it appears that AP can bind to and presumably help inactivate organisms in vivo.

Technical Abstract: Endogenous antimicrobial peptide activity in vivo has rarely been demonstrated. To assess this, Mannheimia haemolytica (Log10 10.20 CFU) was deposited into the lungs of adult sheep, which were killed at 0, 5, 10 and 20 min for necropsy. At 0 min, M. haemolytica appeared normal, and monoclonal antibody to antimicrobial anionic peptide (AP) and Protein A- colloidal gold identified AP already bound to the bacterial surface. At 5-20 min, many organisms were distorted with flocculated intracellular constituents characteristic of AP cellular damage, indicating that AP can bind to and presumably help inactivate organisms in vivo.