title: Neutrophil serine proteases in antibacterial defense.
abstract: Neutrophil serine proteases (NSPs) are critical for the effective functioning of neutrophils and greatly contribute to immune protection against bacterial infections. Thanks to their broad substrate specificity, these chymotrypsin-like proteases trigger multiple reactions that are detrimental to bacterial survival such as direct bacterial killing, generation of antimicrobial peptides, inactivation of bacterial virulence factors and formation of neutrophil extracellular traps. Recently, the importance of NSPs in antibacterial defenses has been further underscored by discoveries of unique bacterial evasion strategies to combat these proteases. Bacteria can indirectly disarm NSPs by protecting bacterial substrates against NSP cleavage, but also produce inhibitory molecules that potently block NSPs. Here we review recent insights in the functional contribution of NSPs in host protection against bacterial infections and the elegant strategies that bacteria use to counteract these responses.
authors.affiliation: Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands.
authors.forename: Daphne A C
authors.initials: DA
authors.lastname: Stapels
authors.affiliation: Department of Biochemistry & Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.
authors.forename: Brian V
authors.initials: BV
authors.lastname: Geisbrecht
authors.affiliation: Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. Electronic address: s.h.m.rooijakkers@umcutrecht.nl.
authors.forename: Suzan H M
authors.initials: SH
authors.lastname: Rooijakkers
mesh_terms: D000486:Allergy and Immunology / Q000639:trends; D000818:Animals; D001419:Bacteria / Q000276:immunology*; D001424:Bacterial Infections / Q000276:immunology*; D035843:Biomedical Research / Q000639:trends; D054884:Host-Pathogen Interactions; D006801:Humans; D057131:Immune Evasion; D008829:Microbiology / Q000639:trends; D009504:Neutrophils / Q000201:enzymology* / Q000276:immunology* / Q000382:microbiology; D057057:Serine Proteases / Q000378:metabolism*
chemical_list: D057057:Serine Proteases