Abstract
Successful in vivo infection following pathogen entry requires the evasion and subversion of multiple immunological barriers. Antimicrobial peptides (AMPs) are one of the first immune pathways upregulated during infection by multiple pathogens, in multiple organs in vivo. In humans, there are many classes of AMPs exhibiting broad antimicrobial activities, with defensins and the human cathelicidin LL-37 being the best studied examples. Whereas historically the efficacy and therapeutic potential of AMPs against bacterial infection has been the primary focus of research, recent studies have begun to elucidate the antiviral properties of AMPs as well as their role in regulation of inflammation and chemoattraction. AMPs as therapeutic tools seem especially promising against emerging infectious viral pathogens for which no approved vaccines or treatments are currently available, such as dengue virus (DENV) and Zika virus (ZIKV). In this review, we summarize recent studies elucidating the efficacy and diverse mechanisms of action of various classes of AMPs against multiple viral pathogens, as well as the potential use of human AMPs in novel antiviral therapeutic strategies.
Highlights
Found in virtually all organisms, antimicrobial peptides (AMPs) are short, positively-charged oligopeptides that exhibit a diversity of structures and functions
Cells incubated with defensins pre- or post-infection demonstrated minimal inhibitory activity against influenza A virus (IAV), whereas incubation of HNPs with virions prior to infection is necessary for the antiviral activity of these AMPs against IAV
The antiviral activity of LL-37 has been reported against a number of viruses including human immunodeficiency virus (HIV)-1, IAV, respiratory syncytial virus (RSV), rhinovirus (HRV), vaccinia virus (VACV), herpes simplex virus (HSV), Zika virus (ZIKV), and hepatitis C virus (HCV), mediated primarily by its interaction with the virus outer envelope (Table 1) [18,41,43,46]
Summary
Found in virtually all organisms, antimicrobial peptides (AMPs) are short, positively-charged oligopeptides that exhibit a diversity of structures and functions. The majority of AMPs are synthesized as large polyprotein precursors, the proteolytic processing of which releases active peptide segments which can be present alone or in multiple copies. Processed functional peptides have been characterized into many classes in mammals; in humans, they include defensins, cathelicidins, transferrins, hepcidin, human antimicrobial proteins, dermcidin, histones, AMPs derived from known proteins, chemokines, and AMPs from immune cells, antimicrobial neuropeptides, and. While all of the AMPs classes have been shown to possess antimicrobial activity, only a few classes have demonstrated antiviral properties. A defining feature of AMPs is their rapid response to infections of bacteria, viruses, fungi, or protozoa [1,4]. We report on the application of human AMPs in the treatment of viral infections
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