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Human β-defensin-1 (HβD-1) is a cysteine-rich cationic skin-antimicrobial peptide (SAP) produced by epithelial surfaces, circulatory cells, and cells of the reproductive tract. It exhibits antimicrobial activity against a wide range of sperm bacteria.

The DEFB1 gene, encoding for the constitutively expressed human beta-defensin 1 (hBD1) antimicrobial peptide is a potential candidate when studying genetic susceptibility to caries. DEFB1 genetic variations have been reported as contributing to hBD1 production impairment, leading to a greater susceptibility to be infected by oral pathogens, also leading to periodontitis. To counteract host immunity, Cryptosporidium parvum has evolved multiple strategies to suppress host antimicrobial defense. One such strategy is to reduce the production of the antimicrobial peptide beta-defensin 1 (DEFB1) by host epithelial cells. Beta-Defensin-1, an antimicrobial peptide encoded by the DEFB1 gene, is known to play an important role in lung mucosal immunity.

β-Defensin 1 (DEFB1) is a member of the β-defensin family, which is highly expressed by epithelial cells. β-defensins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal peptide. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-defensin 1 is an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization. Defects in β-Defensin-1 contribute to asthma diagnosis, with apparent gender-specific effects in human. β-defensin 1 may also play a role in the pathogenesis of severe sepsis. In addition, β-defensin 1 is associated with induction profiles in gingival keratinocytes.