References
- Collaborators GL. Estimates of the global, regional, and national morbidity, mortality, and aetiologies of lower respiratory tract infections in 195 countries: a systematic analysis for the global burden of disease study 2015. Lancet Infect Dis. 2017;17(11):1133–1161.
- Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat Rev Microbiol. 2005;3(3):238–250.
- Klotman ME, Chang TL. Defensins in innate antiviral immunity. Nat Rev Immunol. 2006;6(6):447–456.
- Aerts AM, Francois IE, Cammue BP, et al. The mode of antifungal action of plant, insect and human defensins. Cell Mol Life Sci. 2008;65(13):2069–2079.
- Fahy RJ, Wewers MD. Pulmonary defense and the human cathelicidin hCAP-18/LL-37. Immunol Res. 2005;31(2):75–89.
- Bastos P, Trindade F, da Costa J, et al. Human antimicrobial peptides in bodily fluids: current knowledge and therapeutic perspectives in the Postantibiotic Era. Med Res Rev. 2018;38(1):101–146.
- Bosso M, Standker L, Kirchhoff F, et al. Exploiting the human peptidome for novel antimicrobial and anticancer agents. Bioorg Med Chem. 2018;26(10):2719–2726.
- Munch J, Standker L, Forssmann WG, et al. Discovery of modulators of HIV-1 infection from the human peptidome. Nat Rev Microbiol. 2014;12(10):715–722.
- Detheux M, Standker L, Vakili J, et al. Natural proteolytic processing of hemofiltrate CC chemokine 1 generates a potent CC chemokine receptor (CCR)1 and CCR5 agonist with anti-HIV properties. J Exp Med. 2000;192(10):1501–1508.
- Munch J, Standker L, Pohlmann S, et al. Hemofiltrate CC chemokine 1[9-74] causes effective internalization of CCR5 and is a potent inhibitor of R5-tropic human immunodeficiency virus type 1 strains in primary T cells and macrophages. Antimicrob Agents Chemother. 2002;46(4):982–990.
- Zirafi O, Kim KA, Standker L, et al. Discovery and characterization of an endogenous CXCR4 antagonist. Cell Rep. 2015;11(5):737–747.
- Munch J, Standker L, Adermann K, et al. **Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. Cell. 2007;129(2):263–275.
- Munch J, Rucker E, Standker L, et al. Semen-derived amyloid fibrils drastically enhance HIV infection. Cell. 2007;131(6):1059–1071.
- Arnold F, Schnell J, Zirafi O, et al. Naturally occurring fragments from two distinct regions of the prostatic acid phosphatase form amyloidogenic enhancers of HIV infection. J Virol. 2012;86(2):1244–1249.
- Bensch KW, Raida M, Magert HJ, et al. hBD-1: a novel beta-defensin from human plasma. FEBS Lett. 1995;368(2):331–335.
- Liepke C, Zucht HD, Forssmann WG, et al. Purification of novel peptide antibiotics from human milk. J Chromatogr B Biomed Sci Appl. 2001;752(2):369–377.
- Kim JY, Park SC, Lee JK, et al. Novel antibacterial activity of beta(2)-microglobulin in human amniotic fluid. PLoS One. 2012;7(11):e47642.
- Bjorkman PJ, Saper MA, Samraoui B, et al. Structure of the human class I histocompatibility antigen, HLA-A2. Nature. 1987;329(6139):506–512.
- Wang G, Li X, Wang Z. APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res. 2016;44(D1):D1087–1093.
- Walters MT, Stevenson FK, Goswami R, et al. Comparison of serum and synovial fluid concentrations of beta 2-microglobulin and C reactive protein in relation to clinical disease activity and synovial inflammation in rheumatoid arthritis. Ann Rheum Dis. 1989;48(11):905–911.
- Fahey JL, Taylor JM, Detels R, et al. The prognostic value of cellular and serologic markers in infection with human immunodeficiency virus type 1. N Engl J Med. 1990;322(3):166–172.
- Danesh F, Ho LT. Dialysis-related amyloidosis: history and clinical manifestations. Semin Dial. 2001;14(2):80–85.
- Hirakura Y, Kagan BL. Pore formation by beta-2-microglobulin: a mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid. 2001;8(2):94–100.
- Chiou SJ, Wang CC, Tseng YS, et al. A novel role for beta2-microglobulin: a precursor of antibacterial chemokine in respiratory epithelial cells. Sci Rep. 2016;6:31035.
- Casimir GJ, Lefevre N, Corazza F, et al. The acid-base balance and gender in inflammation: a mini-review. Front Immunol. 2018;9:475.
- Mohr KB, Zirafi O, Hennies M, et al. Sandwich enzyme-linked immunosorbent assay for the quantification of human serum albumin fragment 408-423 in bodily fluids. Anal Biochem. 2015;476:29–35.
- Zhang J, Xin L, Shan B, et al. PEAKS DB: de novo sequencing assisted database search for sensitive and accurate peptide identification. Mol Cell Proteomics. 2012;11(4):M111 010587.
- Romero-Molina S, Ruiz-Blanco YB, Green JR, et al. ProtDCal-Suite: a web server for the numerical codification and functional analysis of proteins. Protein Sci. 2019;28(9):1734–1743.
- Li W, Godzik A. Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics. 2006;22(13):1658–1659.
- Fu L, Niu B, Zhu Z, et al. CD-HIT: accelerated for clustering the next-generation sequencing data. Bioinformatics. 2012;28(23):3150–3152.
- Torrent M, Nogues VM, Boix E. A theoretical approach to spot active regions in antimicrobial proteins. BMC Bioinformatics. 2009;10:373.
- Torrent M, Di Tommaso P, Pulido D, et al. AMPA: an automated web server for prediction of protein antimicrobial regions. Bioinformatics. 2012;28(1):130–131.
- Waghu FH, Barai RS, Gurung P, et al. CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides. Nucleic Acids Res. 2016;44(D1):D1094–1097.
- Lata S, Mishra NK, Raghava GP. AntiBP2: improved version of antibacterial peptide prediction. BMC Bioinformatics. 2010;11(Suppl 1):S19.
- Joseph S, Karnik S, Nilawe P, et al. ClassAMP: a prediction tool for classification of antimicrobial peptides. IEEE/ACM Trans Comput Biol Bioinform. 2012;9(5):1535–1538.
- Veltri D, Kamath U, Shehu A. Deep learning improves antimicrobial peptide recognition. Bioinformatics. 2018;34(16):2740–2747.
- Meher PK, Sahu TK, Saini V, et al. Predicting antimicrobial peptides with improved accuracy by incorporating the compositional, physico-chemical and structural features into Chou’s general PseAAC. Sci Rep. 2017;7:42362.
- Richter R, Schulz-Knappe P, Schrader M, et al. Composition of the peptide fraction in human blood plasma: database of circulating human peptides. J Chromatogr B Biomed Sci Appl. 1999;726(1–2):25–35.
- Ivanova MI, Sawaya MR, Gingery M, et al. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci U S A. 2004;101(29):10584–10589.
- Yolamanova M, Meier C, Shaytan AK, et al. Peptide nanofibrils boost retroviral gene transfer and provide a rapid means for concentrating viruses. Nat Nanotechnol. 2013;8(2):130–136.
- Fleming A. On a remarkable bacteriolytic element found in tissues and secretions. Proc R Soc Lond Ser B Biol sci. 1922;93(653):306–317.
- Berko D, Carmi Y, Cafri G, et al. Membrane-anchored beta 2-microglobulin stabilizes a highly receptive state of MHC class I molecules. J Immunol. 2005;174(4):2116–2123.
- Ratjen F, Kreuzfelder E. Immunoglobulin and beta 2-microglobulin concentrations in bronchoalveolar lavage of children and adults. Lung. 1996;174(6):383–391.
- Cole AM, Liao HI, Stuchlik O, et al. Cationic polypeptides are required for antibacterial activity of human airway fluid. J Immunol. 2002;169(12):6985–6991.
- Roberts AD, Ordway DJ, Orme IM. Listeria monocytogenes infection in beta 2 microglobulin-deficient mice. Infect Immun. 1993;61(3):1113–1116.
- Cogen AL, Moore TA. Beta2-microglobulin-dependent bacterial clearance and survival during murine Klebsiella pneumoniae bacteremia. Infect Immun. 2009;77(1):360–366.
- Gejyo F, Yamada T, Odani S, et al. A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. Biochem Biophys Res Commun. 1985;129(3):701–706.
- Soscia SJ, Kirby JE, Washicosky KJ, et al. The Alzheimer’s disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS One. 2010;5(3):e9505.
- Brothers HM, Gosztyla ML, Robinson SR. The physiological roles of amyloid-beta peptide hint at new ways to treat Alzheimer’s disease. Front Aging Neurosci. 2018;10:118.
- Kagan BL, Jang H, Capone R, et al. Antimicrobial properties of amyloid peptides. Mol Pharm. 2012;9(4):708–717.
- Goodchild SC, Sheynis T, Thompson R, et al. beta2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH. PLoS One. 2014;9(8):e104492.
- Mahlapuu M, Hakansson J, Ringstad L, et al. Antimicrobial peptides: an emerging category of therapeutic agents. Front Cell Infect Microbiol. 2016;6:194.
- Malik E, Dennison SR, Harris F, et al. pH dependent antimicrobial peptides and proteins, their mechanisms of action and potential as therapeutic agents. Pharmaceuticals (Basel). 2016;9:4.
- Gross R, Bauer R, Kruger F, et al. A placenta derived C-terminal fragment of beta-hemoglobin with combined antibacterial and antiviral activity. Front Microbiol. 2020;11:508.
- Park JH, Park GT, Cho IH, et al. An antimicrobial protein, lactoferrin exists in the sweat: proteomic analysis of sweat. Exp Dermatol. 2011;20(4):369–371.