In:
PLOS Pathogens, Public Library of Science (PLoS), Vol. 19, No. 2 ( 2023-2-23), p. e1011200-
Abstract:
In the mammalian intestine, flagellar motility can provide microbes competitive advantage, but also threatens the spatial segregation established by the host at the epithelial surface. Unlike microbicidal defensins, previous studies indicated that the protective activities of human α-defensin 6 (HD6), a peptide secreted by Paneth cells of the small intestine, resides in its remarkable ability to bind microbial surface proteins and self-assemble into protective fibers and nets. Given its ability to bind flagellin, we proposed that HD6 might be an effective inhibitor of bacterial motility. Here, we utilized advanced automated live cell fluorescence imaging to assess the effects of HD6 on actively swimming Salmonella enterica in real time. We found that HD6 was able to effectively restrict flagellar motility of individual bacteria. Flagellin-specific antibody, a classic inhibitor of flagellar motility that utilizes a mechanism of agglutination, lost its activity at low bacterial densities, whereas HD6 activity was not diminished. A single amino acid variant of HD6 that was able to bind flagellin, but not self-assemble, lost ability to inhibit flagellar motility. Together, these results suggest a specialized role of HD6 self-assembly into polymers in targeting and restricting flagellar motility.
Type of Medium:
Online Resource
ISSN:
1553-7374
DOI:
10.1371/journal.ppat.1011200
DOI:
10.1371/journal.ppat.1011200.g001
DOI:
10.1371/journal.ppat.1011200.g002
DOI:
10.1371/journal.ppat.1011200.g003
DOI:
10.1371/journal.ppat.1011200.g004
DOI:
10.1371/journal.ppat.1011200.s001
DOI:
10.1371/journal.ppat.1011200.s002
DOI:
10.1371/journal.ppat.1011200.s003
DOI:
10.1371/journal.ppat.1011200.s004
DOI:
10.1371/journal.ppat.1011200.s005
DOI:
10.1371/journal.ppat.1011200.s006
DOI:
10.1371/journal.ppat.1011200.s007
DOI:
10.1371/journal.ppat.1011200.s008
DOI:
10.1371/journal.ppat.1011200.s009
DOI:
10.1371/journal.ppat.1011200.s010
DOI:
10.1371/journal.ppat.1011200.s011
DOI:
10.1371/journal.ppat.1011200.s012
DOI:
10.1371/journal.ppat.1011200.s013
DOI:
10.1371/journal.ppat.1011200.s014
DOI:
10.1371/journal.ppat.1011200.s015
DOI:
10.1371/journal.ppat.1011200.s016
DOI:
10.1371/journal.ppat.1011200.s017
DOI:
10.1371/journal.ppat.1011200.s018
DOI:
10.1371/journal.ppat.1011200.s019
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2023
detail.hit.zdb_id:
2205412-1
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