Investigating the role of nucleotide-binding oligomerization domain-like receptors in bacterial lung infection.
Lower respiratory tract infections (LRTIs) are a persistent and pervasive public health problem worldwide. Pneumonia and other LRTIs will be among the leading causes of death in adults, and pneumonia is the single largest cause of death in children. LRTIs are also an important cause of acute lung injury and acute exacerbations of chronic obstructive pulmonary disease. Because innate immunity is the first line of defense against pathogens, understanding the role of innate immunity in the pulmonary system is of paramount importance. Pattern recognition molecules (PRMs) that recognize microbial-associated molecular patterns are an integral component of the innate immune system and are located in both cell membranes and cytosol. Toll-like receptors and nucleotide-binding oligomerization domain-like receptors (NLRs) are the major sensors at the forefront of pathogen recognition. Although Toll-like receptors have been extensively studied in host immunity, NLRs have diverse and important roles in immune and inflammatory responses, ranging from antimicrobial properties to adaptive immune responses. The lung contains NLR-expressing immune cells such as leukocytes and nonimmune cells such as epithelial cells that are in constant and close contact with invading microbes. This pulmonary perspective addresses our current understanding of the structure and function of NLR family members, highlighting advances and gaps in knowledge, with a specific focus on immune responses in the respiratory tract during bacterial infection. Further advances in exploring cellular and molecular responses to bacterial pathogens are critical to develop improved strategies to treat and prevent devastating infectious diseases of the lung.
1 Department of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana.
Mary
M
Leissinger
Ritwij
R
Kulkarni
Rachel L
RL
Zemans
Gregory P
GP
Downey
Samithamby
S
Jeyaseelan
D048868:Adaptor Proteins, Signal Transducing / Q000276:immunology*; D001424:Bacterial Infections / Q000276:immunology*; D053468:CARD Signaling Adaptor Proteins / Q000276:immunology; D002135:Calcium-Binding Proteins / Q000276:immunology; D002352:Carrier Proteins / Q000276:immunology; D006801:Humans; D058847:Inflammasomes / Q000276:immunology; D000071199:NLR Family, Pyrin Domain-Containing 3 Protein; D051616:Neuronal Apoptosis-Inhibitory Protein / Q000276:immunology; D053474:Nod1 Signaling Adaptor Protein / Q000276:immunology; D053473:Nod2 Signaling Adaptor Protein / Q000276:immunology; D018160:Receptors, Cytoplasmic and Nuclear / Q000276:immunology*; D012141:Respiratory Tract Infections / Q000276:immunology*
D048868:Adaptor Proteins, Signal Transducing; D053468:CARD Signaling Adaptor Proteins; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D058847:Inflammasomes; C496800:NAIP protein, human; D000071199:NLR Family, Pyrin Domain-Containing 3 Protein; C435692:NLRC4 protein, human; C453881:NLRP3 protein, human; D051616:Neuronal Apoptosis-Inhibitory Protein; D053474:Nod1 Signaling Adaptor Protein; D053473:Nod2 Signaling Adaptor Protein; D018160:Receptors, Cytoplasmic and Nuclear
bacterial infection; inflammasome; lung; nucleotide-binding oligomerization domain–like receptors