Recent Advances in Lipopolysaccharide Recognition Systems
Lipopolysaccharide (LPS), commonly known as endotoxin, is ubiquitous and the most-studied pathogen-associated molecular pattern. A component of Gram-negative bacteria, extracellular LPS is sensed by our immune system via the toll-like receptor (TLR)-4. Given that TLR4 is membrane bound, it recognize...
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doaj-8ec6815b1d5242b38a4799274568ef912020-11-25T01:12:57ZengMDPI AGInternational Journal of Molecular Sciences1422-00672020-01-0121237910.3390/ijms21020379ijms21020379Recent Advances in Lipopolysaccharide Recognition SystemsLalita Mazgaeen0Prajwal Gurung1Inflammation Program, University of Iowa, Iowa City, IA 52242, USAInflammation Program, University of Iowa, Iowa City, IA 52242, USALipopolysaccharide (LPS), commonly known as endotoxin, is ubiquitous and the most-studied pathogen-associated molecular pattern. A component of Gram-negative bacteria, extracellular LPS is sensed by our immune system via the toll-like receptor (TLR)-4. Given that TLR4 is membrane bound, it recognizes LPS in the extracellular milieu or within endosomes. Whether additional sensors, if any, play a role in LPS recognition within the cytoplasm remained unknown until recently. The last decade has seen an unprecedented unfolding of TLR4-independent LPS sensing pathways. First, transient receptor potential (TRP) channels have been identified as non-TLR membrane-bound sensors of LPS and, second, caspase-4/5 (and caspase-11 in mice) have been established as the cytoplasmic sensors for LPS. Here in this review, we detail the brief history of LPS discovery, followed by the discovery of TLR4, TRP as the membrane-bound sensor, and our current understanding of caspase-4/5/11 as cytoplasmic sensors.https://www.mdpi.com/1422-0067/21/2/379lpsendotoxintlr4trpa1trpv4caspase-11 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lalita Mazgaeen Prajwal Gurung |
spellingShingle |
Lalita Mazgaeen Prajwal Gurung Recent Advances in Lipopolysaccharide Recognition Systems International Journal of Molecular Sciences lps endotoxin tlr4 trpa1 trpv4 caspase-11 |
author_facet |
Lalita Mazgaeen Prajwal Gurung |
author_sort |
Lalita Mazgaeen |
title |
Recent Advances in Lipopolysaccharide Recognition Systems |
title_short |
Recent Advances in Lipopolysaccharide Recognition Systems |
title_full |
Recent Advances in Lipopolysaccharide Recognition Systems |
title_fullStr |
Recent Advances in Lipopolysaccharide Recognition Systems |
title_full_unstemmed |
Recent Advances in Lipopolysaccharide Recognition Systems |
title_sort |
recent advances in lipopolysaccharide recognition systems |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2020-01-01 |
description |
Lipopolysaccharide (LPS), commonly known as endotoxin, is ubiquitous and the most-studied pathogen-associated molecular pattern. A component of Gram-negative bacteria, extracellular LPS is sensed by our immune system via the toll-like receptor (TLR)-4. Given that TLR4 is membrane bound, it recognizes LPS in the extracellular milieu or within endosomes. Whether additional sensors, if any, play a role in LPS recognition within the cytoplasm remained unknown until recently. The last decade has seen an unprecedented unfolding of TLR4-independent LPS sensing pathways. First, transient receptor potential (TRP) channels have been identified as non-TLR membrane-bound sensors of LPS and, second, caspase-4/5 (and caspase-11 in mice) have been established as the cytoplasmic sensors for LPS. Here in this review, we detail the brief history of LPS discovery, followed by the discovery of TLR4, TRP as the membrane-bound sensor, and our current understanding of caspase-4/5/11 as cytoplasmic sensors. |
topic |
lps endotoxin tlr4 trpa1 trpv4 caspase-11 |
url |
https://www.mdpi.com/1422-0067/21/2/379 |
work_keys_str_mv |
AT lalitamazgaeen recentadvancesinlipopolysacchariderecognitionsystems AT prajwalgurung recentadvancesinlipopolysacchariderecognitionsystems |
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