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5CUJ

Crystal structure of Human Defensin-5 Y27A mutant crystal form 2.

Summary for 5CUJ
Entry DOI10.2210/pdb5cuj/pdb
Related1ZMP 5CUI 5CUM
DescriptorDefensin-5, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordspaneth cells defensin, human alpha-defensin, intestinal defensin, antimicrobial protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains6
Total formula weight21872.91
Authors
Tolbert, W.D.,Gohain, N.,Pazgier, M. (deposition date: 2015-07-24, release date: 2016-07-27, Last modification date: 2024-11-13)
Primary citationXu, D.,Liao, C.,Zhang, B.,Tolbert, W.D.,He, W.,Dai, Z.,Zhang, W.,Yuan, W.,Pazgier, M.,Liu, J.,Yu, J.,Sansonetti, P.J.,Bevins, C.L.,Shao, Y.,Lu, W.
Human Enteric alpha-Defensin 5 Promotes Shigella Infection by Enhancing Bacterial Adhesion and Invasion.
Immunity, 2018
Cited by
PubMed Abstract: Shigella is a Gram-negative bacterium that causes bacillary dysentery worldwide. It invades the intestinal epithelium to elicit intense inflammation and tissue damage, yet the underlying mechanisms of its host selectivity and low infectious inoculum remain perplexing. Here, we report that Shigella co-opts human α-defensin 5 (HD5), a host defense peptide important for intestinal homeostasis and innate immunity, to enhance its adhesion to and invasion of mucosal tissues. HD5 promoted Shigella infection in vitro in a structure-dependent manner. Shigella, commonly devoid of an effective host-adhesion apparatus, preferentially targeted HD5 to augment its ability to colonize the intestinal epithelium through interactions with multiple bacterial membrane proteins. HD5 exacerbated infectivity and Shigella-induced pathology in a culture of human colorectal tissues and three animal models. Our findings illuminate how Shigella exploits innate immunity by turning HD5 into a virulence factor for infection, unveiling a mechanism of action for this highly proficient human pathogen.
PubMed: 29858013
DOI: 10.1016/j.immuni.2018.04.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.08 Å)
Structure validation

230083

数据于2025-01-15公开中

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