title: Defensive remodeling: How bacterial surface properties and biofilm formation promote resistance to antimicrobial peptides.
abstract: Multidrug resistance bacteria are a major concern worldwide. These pathogens cannot be treated with conventional antibiotics and thus alternative therapeutic agents are needed. Antimicrobial peptides (AMPs) are considered to be good candidates for this purpose. Most AMPs are short and positively charged amphipathic peptides, which are found in all known forms of life. AMPs are known to kill bacteria by binding to the negatively charged bacterial surface, and in most cases cause membrane disruption. Resistance toward AMPs can be developed, by modification of bacterial surface molecules, secretion of protective material and up-regulation or elimination of specific proteins. Because of the general mechanisms of attachment and action of AMPs, bacterial resistance to AMPs often involves biophysical and biochemical changes such as surface rigidity, cell wall thickness, surface charge, as well as membrane and cell wall modification. Here we focus on the biophysical, surface and surrounding changes that bacteria undergo in acquiring resistance to AMPs. In addition we discuss the question of whether bacterial resistance to administered AMPs might compromise our innate immunity to endogenous AMPs. This article is part of a Special Issue entitled: Bacterial Resistance to Antimicrobial Peptides.
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Reut
authors.initials: R
authors.lastname: Nuri
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Tal
authors.initials: T
authors.lastname: Shprung
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: Yechiel.Shai@weizmann.ac.il.
authors.forename: Yechiel
authors.initials: Y
authors.lastname: Shai
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000627:therapeutic use; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000276:immunology / Q000378:metabolism* / Q000627:therapeutic use; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D018441:Biofilms / Q000187:drug effects / Q000254:growth & development*; D024901:Drug Resistance, Multiple, Bacterial; D006090:Gram-Negative Bacteria / Q000187:drug effects / Q000254:growth & development / Q000276:immunology / Q000378:metabolism* / Q000472:pathogenicity; D016905:Gram-Negative Bacterial Infections / Q000276:immunology / Q000378:metabolism* / Q000382:microbiology / Q000517:prevention & control; D006094:Gram-Positive Bacteria / Q000187:drug effects / Q000254:growth & development / Q000276:immunology / Q000378:metabolism* / Q000472:pathogenicity; D016908:Gram-Positive Bacterial Infections / Q000276:immunology / Q000378:metabolism* / Q000382:microbiology / Q000517:prevention & control; D054884:Host-Pathogen Interactions; D006801:Humans; D057131:Immune Evasion; D007113:Immunity, Innate; D050296:Microbial Viability; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D013329:Structure-Activity Relationship; D013499:Surface Properties
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins
keywords: Antimicrobial peptides; Biochemical properties; Biofilm; Biophysical properties; Cross resistance; Resistance; Surface