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Defensins are small cysteine-rich cationic proteins across cellular life, including vertebrate [1] and invertebrate [2] animals, plants, [3] [4] and fungi. [5] They are host defense peptides , with members displaying either direct antimicrobial activity , immune signaling activities, or both.
Red-eyed flies lacking antimicrobial peptide genes are susceptible to infection, while white-eyed flies have a wild-type immune response. Antimicrobial peptides are produced by species across the tree of life, including: bacteria (e.g. bacteriocin, and many others) fungi (e.g. peptaibols, plectasin, and many others) cnidaria (e.g. hydramacin ...
Defensin, alpha 1 also known as human alpha defensin 1, human neutrophil peptide 1 (HNP-1) or neutrophil defensin 1 is a human protein that is encoded by the DEFA1 gene. [ 3 ] [ 4 ] [ 5 ] Human alpha defensin 1 belongs to the alpha defensin family of antimicrobial peptides .
Defensins are 2-6 kDa, cationic, antimicrobial peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses, [2] containing three pairs of intramolecular disulfide bonds. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories.
Defensins are integral components of the innate immune system and belong to the ancient superfamily of antimicrobial peptides (AMPs). AMPs are also known as host defense peptides (HDPs), [2] and they are thought to have diverged about 1.4 billion years ago before the evolution of prokaryotes and eukaryotes.
The beta defensins are antimicrobial peptides implicated in the resistance of epithelial surfaces to microbial colonization. Defensins are 2 to 6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses, [ 1 ] containing three pairs of intramolecular disulfide bonds.
These four subunits could theoretically combine to produce 10 different processed defensins. However, only five have been observed: consisting of subunits A+A, A+B, A+C, A+D and B+B (Referred to as BTD-3, BTD-1, BTD-4, BTD7 and BTD-2 respectively). [7] Finally, orangutan genomes encode 4 θ-defensin precursor genes and gibbon genomes encode 2.
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 1, an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization.