title: Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens.
abstract: Cationic antimicrobial peptides (CAMPs) are critical front line contributors to host defense against invasive bacterial infection. These immune factors have direct killing activity toward microbes, but many pathogens are able to resist their effects. Group A Streptococcus, group B Streptococcus and Streptococcus pneumoniae are among the most common pathogens of humans and display a variety of phenotypic adaptations to resist CAMPs. Common themes of CAMP resistance mechanisms among the pathogenic streptococci are repulsion, sequestration, export, and destruction. Each pathogen has a different array of CAMP-resistant mechanisms, with invasive disease potential reflecting the utilization of several mechanisms that may act in synergy. Here we discuss recent progress in identifying the sources of CAMP resistance in the medically important Streptococcus genus. Further study of these mechanisms can contribute to our understanding of streptococcal pathogenesis, and may provide new therapeutic targets for therapy and disease prevention. This article is part of a Special Issue entitled: Bacterial Resistance to Antimicrobial Peptides.
authors.affiliation: Department of Pediatrics, University of California, San Diego, La Jolla, CA, USA. Electronic address: clarock@ucsd.edu.
authors.forename: Christopher N
authors.initials: CN
authors.lastname: LaRock
authors.affiliation: Department of Pediatrics, University of California, San Diego, La Jolla, CA, USA; Skaggs School of Medicine and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA, USA; Rady Children's Hospital, San Diego, CA, USA. Electronic address: vnizet@ucsd.edu.
authors.forename: Victor
authors.initials: V
authors.lastname: Nizet
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000627:therapeutic use; D023181:Antimicrobial Cationic Peptides / Q000276:immunology / Q000378:metabolism* / Q000627:therapeutic use; D001426:Bacterial Proteins / Q000276:immunology / Q000378:metabolism*; D001692:Biological Transport; D024881:Drug Resistance, Bacterial; D054884:Host-Pathogen Interactions; D006801:Humans; D057131:Immune Evasion; D007113:Immunity, Innate; D026901:Membrane Transport Proteins / Q000378:metabolism; D050296:Microbial Viability; D059748:Proteolysis; D015398:Signal Transduction; D013290:Streptococcal Infections / Q000276:immunology / Q000378:metabolism* / Q000382:microbiology / Q000517:prevention & control; D013291:Streptococcus / Q000187:drug effects / Q000276:immunology / Q000378:metabolism* / Q000472:pathogenicity
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; D026901:Membrane Transport Proteins
keywords: Antimicrobial peptide; Cathelicidin; Defensin; LL-37; Streptococcus virulence factors, innate immunity