Asset Details
Do you wish to reserve the book?
T4SS-dependent TLR5 activation by Helicobacter pylori infection
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
T4SS-dependent TLR5 activation by Helicobacter pylori infection
Do you wish to request the book?
T4SS-dependent TLR5 activation by Helicobacter pylori infection
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
T4SS-dependent TLR5 activation by Helicobacter pylori infection
2019
Overview
Toll-like receptor TLR5 recognizes a conserved domain, termed D1, that is present in flagellins of several pathogenic bacteria but not in
Helicobacter pylori
. Highly virulent
H. pylori
strains possess a type IV secretion system (T4SS) for delivery of virulence factors into gastric epithelial cells. Here, we show that one of the
H. pylori
T4SS components, protein CagL, can act as a flagellin-independent TLR5 activator. CagL contains a D1-like motif that mediates adherence to TLR5
+
epithelial cells, TLR5 activation, and downstream signaling in vitro. TLR5 expression is associated with
H. pylori
infection and gastric lesions in human biopsies. Using
Tlr5
-knockout and wild-type mice, we show that TLR5 is important for efficient control of
H. pylori
infection. Our results indicate that CagL, by activating TLR5, may modulate immune responses to
H. pylori
.
Toll-like receptor TLR5 recognizes a domain, D1, that is present in flagellins of several pathogenic bacteria but not in
Helicobacter pylori
. Here, the authors show that TLR5 can be activated independently of flagellin by a component of the
H. pylori
type IV secretion system that contains a D1-like motif.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/1
/ 13/106
/ 13/109
/ 13/31
/ 13/51
/ 13/95
/ 14
/ 38
/ 38/61
/ 38/77
/ 38/79
/ 42
/ 42/70
/ 64
/ 64/60
/ 82/29
/ 82/83
/ Animals
/ Bacteria
/ Bacterial Proteins - immunology
/ Bacterial Proteins - metabolism
/ Biopsy
/ Female
/ Gastric Mucosa - microbiology
/ Genes
/ Helicobacter Infections - immunology
/ Helicobacter Infections - microbiology
/ Helicobacter pylori - immunology
/ Helicobacter pylori - metabolism
/ Host-Pathogen Interactions - immunology
/ Humanities and Social Sciences
/ Humans
/ Mice
/ Peptides
/ Proteins
/ Science
/ Signal Transduction - immunology
/ Toll-Like Receptor 5 - genetics
/ Toll-Like Receptor 5 - immunology
/ Toll-Like Receptor 5 - metabolism
/ Type IV Secretion Systems - immunology
