NDLI: Natural anti-infective pulmonary proteins: In vivo cooperative action of surfactant protein SP-A and the lung antimicrobial peptide $SP-B^{N}$

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Natural anti-infective pulmonary proteins: In vivo cooperative action of surfactant protein SP-A and the lung antimicrobial peptide $SP-B^{N}$

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Natural anti-infective pulmonary proteins: In vivo cooperative action of surfactant protein SP-A and the lung antimicrobial peptide $SP-B^{N}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Akinbi, Henry T. Yang, Li Sáenz, Alejandra Coya, Juan Manuel Weaver, Timothy E. Casals, Cristina
Description	Author Affiliation: Coya JM ( Department of Biochemistry and Molecular Biology I, Complutense University of Madrid, 28040 Madrid, Spain); Akinbi HT ( Division of Pulmonary Biology, Cincinnati Children's Hospital Medical Center and University of Cincinnati College of Medicine, Cincinnati, OH 45229.); Sáenz A ( Department of Biochemistry and Molecular Biology I, Complutense University of Madrid, 28040 Madrid, Spain); Yang L ( Division of Pulmonary Biology, Cincinnati Children's Hospital Medical Center and University of Cincinnati College of Medicine, Cincinnati, OH 45229.); Weaver TE ( Division of Pulmonary Biology, Cincinnati Children's Hospital Medical Center and University of Cincinnati College of Medicine, Cincinnati, OH 45229.); Casals C ( Department of Biochemistry and Molecular Biology I, Complutense University of Madrid, 28040 Madrid, Spain)
Abstract	The anionic antimicrobial peptide SP-B(N), derived from the N-terminal saposin-like domain of the surfactant protein (SP)-B proprotein, and SP-A are lung anti-infective proteins. SP-A-deficient mice are more susceptible than wild-type mice to lung infections, and bacterial killing is enhanced in transgenic mice overexpressing SP-B(N). Despite their potential anti-infective action, in vitro studies indicate that several microorganisms are resistant to SP-A and SP-B(N). In this study, we test the hypothesis that these proteins act synergistically or cooperatively to strengthen each other's microbicidal activity. The results indicate that the proteins acted synergistically in vitro against SP-A- and SP-B(N)-resistant capsulated Klebsiella pneumoniae (serotype K2) at neutral pH. SP-A and SP-B(N) were able to interact in solution (Kd = 0.4 µM), which enabled their binding to bacteria with which SP-A or SP-B(N) alone could not interact. In vivo, we found that treatment of K. pneumoniae-infected mice with SP-A and SP-B(N) conferred more protection against K. pneumoniae infection than each protein individually. SP-A/SP-B(N)-treated infected mice showed significant reduction of bacterial burden, enhanced neutrophil recruitment, and ameliorated lung histopathology with respect to untreated infected mice. In addition, the concentrations of inflammatory mediators in lung homogenates increased early in infection in contrast with the weak inflammatory response of untreated K. pneumoniae-infected mice. Finally, we found that therapeutic treatment with SP-A and SP-B(N) 6 or 24 h after bacterial challenge conferred significant protection against K. pneumoniae infection. These studies show novel anti-infective pathways that could drive development of new strategies against pulmonary infections.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1500778
Journal	The Journal of Immunology
Issue Number	4
Volume Number	195
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2015-08-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Pulmonary Surfactant-associated Proteins Metabolism Animals Anti-bacterial Agents Pharmacology Antimicrobial Cationic Peptides Cytokines Disease Models, Animal Drug Synergism Hydrogen-ion Concentration Klebsiella Infections Immunology Microbiology Klebsiella Pneumoniae Drug Effects Lung Pathology Macrophages Mice Mice, Knockout Neutrophil Infiltration Protein Binding Pulmonary Surfactant-associated Protein A Genetics Pulmonary Surfactant-associated Protein B Recombinant Proteins Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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