Toll‐like receptor 4: the missing link of the cerebral innate immune response triggered by circulating gram‐negative bacterial cell wall components

2001 ◽  
Vol 15 (1) ◽  
pp. 155-163 ◽  
Author(s):  
NATHALIE LAFLAMME ◽  
SERGE RIVEST
Keyword(s):  
Immune Response ◽  
Cell Wall ◽  
Innate Immune Response ◽  
Bacterial Cell ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Gram Negative ◽  
Cell Wall Components ◽  
Wall Components

scholarly journals Variability among Macaca fascicularis in the innate immune response to Toll‐like receptor 4 (TLR4) agonists

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Charles Wayne Frevert ◽  
Renee Hukkanen ◽  
Steve Mongovin ◽  
Kay Larsen ◽  
Mike Agy ◽  
...  
Keyword(s):  
Immune Response ◽  
Innate Immune Response ◽  
Macaca Fascicularis ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4

Toll-like receptor-4 expressed on gastric pit cells may initiate innate immune response of gastric mucosa against Helicobactor pylori infection

2001 ◽  
Vol 120 (5) ◽  
pp. A59
Author(s):  
Kazuhito Rokutan ◽  
Shigetada Teshima ◽  
Tsukasa Kawahara ◽  
Tomoko Kawai ◽  
Takeshi Nikawa ◽  
...  
Keyword(s):  
Immune Response ◽  
Gastric Mucosa ◽  
Innate Immune Response ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Helicobactor Pylori ◽  
Pit Cells

scholarly journals Energetics of Endotoxin Recognition in the Toll-Like Receptor 4 Innate Immune Response

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Teresa Paramo ◽  
Susana M. Tomasio ◽  
Kate L. Irvine ◽  
Clare E. Bryant ◽  
Peter J. Bond
Keyword(s):  
Immune Response ◽  
Innate Immune Response ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4

scholarly journals Specific bacterial cell wall components influence the stability of Coxsackievirus B3

2021 ◽  
Author(s):  
Adeeba H Dhalech ◽  
Tara D Fuller ◽  
Christopher M Robinson
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Enteric Viruses ◽  
Enteric Virus ◽  
Coxsackievirus B3 ◽  
Gram Negative ◽  
Cell Wall Components ◽  
E Coli ◽  
Wall Components

Enteric viruses infect the mammalian gastrointestinal tract and lead to significant morbidity and mortality worldwide. Data indicate that enteric viruses can utilize intestinal bacteria to promote viral replication and pathogenesis. However, the precise interactions between enteric viruses and bacteria are unknown. Here we examined the interaction between bacteria and Coxsackievirus B3, an enteric virus from the picornavirus family. We found that bacteria enhance the infectivity of Coxsackievirus B3 (CVB3) in vitro. Notably, specific bacteria are required as gram-negative Salmonella enterica, but not Escherichia coli, enhanced CVB3 infectivity and stability. Investigating the cell wall components of both S. enterica and E. coli revealed that structures in the O-antigen or core of lipopolysaccharide, a major component of the gram-negative bacterial cell wall, were required for S. enterica to enhance CVB3. To determine if these requirements were necessary for similar enteric viruses, we investigated if S. enterica and E. coli enhanced infectivity of poliovirus, another enteric virus in the picornavirus family. We found that, in contrast to CVB3, these bacteria enhanced the infectivity of poliovirus in vitro. Overall, these data indicate that distinct bacteria enhance CVB3 infectivity and stability, and specific enteric viruses may have differing requirements for their interactions with specific bacterial species.

CD14, An Innate Immune Receptor for Various Bacterial Cell Wall Components

2020 ◽  
pp. 463-471
Author(s):  
Artur J. Ulmer ◽  
Volker T. El-Samalouti ◽  
Ernst T. Rietschel ◽  
Hans-Dieter Flad ◽  
Roman Dziarski
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Innate Immune ◽  
Immune Receptor ◽  
Cell Wall Components ◽  
Innate Immune Receptor ◽  
Wall Components

scholarly journals Identification of PGN_1123 as the Gene Encoding Lipid A Deacylase, an Enzyme Required for Toll-Like Receptor 4 Evasion, inPorphyromonas gingivalis

2019 ◽  
Vol 201 (11) ◽  
Author(s):  
Sumita Jain ◽  
Ana M. Chang ◽  
Manjot Singh ◽  
Jeffrey S. McLean ◽  
Stephen R. Coats ◽  
...  
Keyword(s):  
Immune Response ◽  
Porphyromonas Gingivalis ◽  
Innate Immune Response ◽  
Lipid A ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Gene Encoding ◽  
Content Type ◽  
Chronic Inflammatory Condition

ABSTRACTRemoval of one acyl chain from bacterial lipid A by deacylase activity is a mechanism used by many pathogenic bacteria to evade the host's Toll-like receptor 4 (TLR4)-mediated innate immune response. InPorphyromonas gingivalis, a periodontal pathogen, lipid A deacylase activity converts a majority of the initially synthesized penta-acylated lipid A, a TLR4 agonist, to tetra-acylated structures, which effectively evade TLR4 sensing by being either inert or antagonistic at TLR4. In this paper, we report successful identification of the gene that encodes theP. gingivalislipid A deacylase enzyme. This gene, PGN_1123 inP. gingivalis33277, is highly conserved withinP. gingivalis, and putative orthologs are phylogenetically restricted to theBacteroidetesphylum. Lipid A of ΔPGN_1123 mutants is penta-acylated and devoid of tetra-acylated structures, and the mutant strain provokes a strong TLR4-mediated proinflammatory response, in contrast to the negligible response elicited by wild-typeP. gingivalis. Heterologous expression of PGN_1123 inBacteroides thetaiotaomicronpromoted lipid A deacylation, confirming that PGN_1123 encodes the lipid A deacylase enzyme.IMPORTANCEPeriodontitis, commonly referred to as gum disease, is a chronic inflammatory condition that affects a large proportion of the population.Porphyromonas gingivalisis a bacterium closely associated with periodontitis, although how and if it is a cause for the disease are not known. It has a formidable capacity to dampen the host's innate immune response, enabling its persistence in diseased sites and triggering microbial dysbiosis in animal models of infection.P. gingivalisis particularly adept at evading the host's TLR4-mediated innate immune response by modifying the structure of lipid A, the TLR4 ligand. In this paper, we report identification of the gene encoding lipid A deacylase, a key enzyme that modifies lipid A to TLR4-evasive structures.

Sign in / Sign up

Export Citation Format

Share Document