Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Objective And Design: The heterogeneity of response to SARS-CoV-2 infection is directly linked to the individual genetic background. Genetic variants of inflammasome-related genes have been pointed as risk factors for several inflammatory sterile and infectious disease. In the group of inflammasome receptors, NLRP1 stands out as a good novel candidate as severity factor for COVID-19 disease.

Methods: To address this question, we performed an association study of NLRP1, DPP9, CARD8, IL1B, and IL18 single nucleotide variants (SNVs) in a cohort of 945 COVID-19 patients.

Results: The NLRP1 p.Leu155His in the linker region, target of viral protease, was significantly associated to COVID-19 severity, which could contribute to the excessive cytokine release reported in severe cases.

Conclusion: Inflammasome genetic background contributes to individual response to SARS-CoV-2.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9684769PMC
http://dx.doi.org/10.1007/s00011-022-01670-3DOI Listing

Publication Analysis

Top Keywords

linker region
8
response sars-cov-2
8
genetic background
8
common variant
4
variant close
4
close "tripwire"
4
"tripwire" linker
4
nlrp1
4
region nlrp1
4
nlrp1 contributes
4

Similar Publications

Animal models of the pathology of Parkinson's disease (PD) have provided most of the treatments to date, but the disease is restricted to human patients. In vitro models using human pluripotent stem cells (hPSCs)-derived neural organoids have provided improved access to study PD etiology. This study established a method to generate human striatal-midbrain assembloids (hSMAs) from hPSCs for modeling alpha-synuclein (α-syn) propagation and recapitulating basal ganglia circuits, including nigrostriatal and striatonigral pathways.

View Article and Find Full Text PDF

Ferlins are vesicle trafficking proteins composed of folded C2 domains conjugated by linkers which are largely disordered. Although a role for the C2 domains as calcium sensors has been established it remains unclear whether the linkers function beyond acting as passive spacers. We examined the C2A-C2B linker sequences of vertebrate ferlins and found both putative short linear motifs (SLiMs) as well as membrane binding sequences for members of the protein family.

View Article and Find Full Text PDF

Ca/Calmodulin-Dependent Protein Kinase II (CaMKII)-Targeted Drug Discovery: Challenges and Strategies.

Ageing Res Rev

September 2025

Department of Pharmaceutical Toxicology, School of Pharmacy, China Medical University, Shenyang, 110122, China; Laboratory of Naturel Medicine for drug discovery, School of Pharmacy, China Medical University, Shenyang, 110122, China. Electronic address:

Calcium (Ca)/calmodulin (CaM)-dependent protein kinase II (CaMKII) is an emerging drug target for age-related diseases. It is a multifunctional kinase with complex activation modes, numerous isoforms, broad tissue distribution, and a dual role in health and disease. In particular, its isoforms share a high degree of conservation within the catalytic and regulatory domains, with only minor differences confined to the linker region.

View Article and Find Full Text PDF

Investigating the role of the I-II linker in Nav1.5 channel function.

J Gen Physiol

November 2025

Department of Biomedical Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA.

The cardiac voltage-gated sodium channel, Nav1.5, initiates the cardiac action potential. Its dysfunction can lead to dangerous arrhythmias, sudden cardiac arrest, and death.

View Article and Find Full Text PDF

The Rcs signal transduction system is a phosphorelay responsible for sensing enterobacterial cell envelope stresses. In Escherichia coli, the Rcs system is required to survive treatment with A22 and mecillinam, antibiotics that perturb cell size. To test whether size changes are correlated with envelope damage and thereby sensed by the Rcs system, we tuned E.

View Article and Find Full Text PDF