Selected article for: "acid sequence and sequence homology"
Author: Cheng Wang; Shaobo Wang; Daixi Li; Xia Zhao; Songling Han; Tao Wang; Gaomei Zhao; Yin Chen; Fang Chen; Jianqi Zhao; Liting Wang; Wei Sun; Yi Huang; Yongping Su; Dongqing Wei; Jinghong Zhao; Junping Wang
Title: Lectin-like Intestinal Defensin Inhibits 2019-nCoV Spike binding to ACE2
  • Document date: 2020_3_31
    • ID: bzq1xxqb_6
    Snippet: It is well known that intestinal epithelium directly interacts with the external environment and encounters trillions of microorganisms including various viruses. To cope with the microbial threat, intestinal cells have evolved to produce a plenty of antimicrobial peptides (AMPs) to strengthen the mucosal barrier 21 . Defensin is a group of small (2-5 KD) and amphiphilic AMPs. Human defensins (HDs) are divided into two subgroups, α and β, based.....
    Document: It is well known that intestinal epithelium directly interacts with the external environment and encounters trillions of microorganisms including various viruses. To cope with the microbial threat, intestinal cells have evolved to produce a plenty of antimicrobial peptides (AMPs) to strengthen the mucosal barrier 21 . Defensin is a group of small (2-5 KD) and amphiphilic AMPs. Human defensins (HDs) are divided into two subgroups, α and β, based on the amino acid sequence homology and disulfide connectivity. Paneth cells, the major secretory cells located in the crypts of small intestine, specifically secrete two kinds of α defensins (HD5 and HD6) 22 . As reported, HD5 is the most abundant α defensin in intestine 23 .

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