Biomaterial Database

The role of respiratory epithelium in host defence against influenza virus infection. 2018

Laura Denney, and Ling-Pei Ho

MRC Human Immunology Unit, MRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.

The respiratory epithelium is the major interface between the environment and the host. Sophisticated barrier, sensing, anti-microbial and immune regulatory mechanisms have evolved to help maintain homeostasis and to defend the lung against foreign substances and pathogens. During influenza virus infection, these specialised structural cells and populations of resident immune cells come together to mount the first response to the virus, one which would play a significant role in the immediate and long term outcome of the infection. In this review, we focus on the immune defence machinery of the respiratory epithelium and briefly explore how it repairs and regenerates after infection.

UI	MeSH Term	Description	Entries
D007251	Influenza, Human	An acute viral infection in humans involving the respiratory tract. It is marked by inflammation of the NASAL MUCOSA; the PHARYNX; and conjunctiva, and by headache and severe, often generalized, myalgia.	Grippe,Human Flu,Human Influenza,Influenza in Humans,Influenza,Flu, Human,Human Influenzas,Influenza in Human,Influenzas,Influenzas, Human
D007372	Interferons	Proteins secreted by vertebrate cells in response to a wide variety of inducers. They confer resistance against many different viruses, inhibit proliferation of normal and malignant cells, impede multiplication of intracellular parasites, enhance macrophage and granulocyte phagocytosis, augment natural killer cell activity, and show several other immunomodulatory functions.	Interferon
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000070576	NLR Proteins	Intracellular signaling proteins that are defined by the presence of a NUCLEOTIDE-binding region and LEUCINE-rich repeats. Their general structure consists of any of a variety of effector domains at their N-termini such as a caspase recruitment domain (CARD), a central nucleotide-binding domain, and a variable number of C-terminal leucine-rich repeats. They are important for pathogen recognition in the INNATE IMMUNE RESPONSE of animals and plants. Members of the NLR protein family include the NOD SIGNALING ADAPTOR PROTEINS.	NOD-like Receptor,Nucleotide-Binding Domain Leucine-Rich Repeat Protein,NLR Protein,NOD-like Receptors,Nucleotide-binding Domain Leucine-rich Repeat Proteins,NOD like Receptor,NOD like Receptors,Nucleotide Binding Domain Leucine Rich Repeat Protein,Nucleotide binding Domain Leucine rich Repeat Proteins,Protein, NLR,Proteins, NLR,Receptor, NOD-like,Receptors, NOD-like
D000071457	DEAD Box Protein 58	A DEAD-box RNA helicase that contains an N-terminal DEATH-LIKE DOMAIN, AAA+ ATPase domain, and C-terminal RNA HELICASE activity. It functions as an innate immune receptor through its recognition of viral nucleic acids. It also induces the expression of INTERFERON TYPE I and proinflammatory CYTOKINES. Its ligands include: 5'-triphosphorylated SINGLE-STRANDED RNA, DOUBLE-STRANDED RNA (dsRNA), and short dsRNA (less than 1 kb in length).	DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58,Probable ATP-Dependent RNA Helicase DDX58,RIG-I-like Receptor 1,Probable ATP Dependent RNA Helicase DDX58,RIG I like Receptor 1
D016207	Cytokines	Non-antibody proteins secreted by inflammatory leukocytes and some non-leukocytic cells, that act as intercellular mediators. They differ from classical hormones in that they are produced by a number of tissue or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.	Cytokine
D016764	Cell Polarity	Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.	Cell Polarities,Polarities, Cell,Polarity, Cell
D051193	Toll-Like Receptors	A family of pattern recognition receptors characterized by an extracellular leucine-rich domain and a cytoplasmic domain that share homology with the INTERLEUKIN 1 RECEPTOR and the DROSOPHILA toll protein. Following pathogen recognition, toll-like receptors recruit and activate a variety of SIGNAL TRANSDUCING ADAPTOR PROTEINS.	Receptors, Toll-Like,Toll-Like Receptor,Receptor, Toll-Like,Receptors, Toll Like,Toll Like Receptor,Toll Like Receptors
D018925	Chemokines	Class of pro-inflammatory cytokines that have the ability to attract and activate leukocytes. They can be divided into at least three structural branches: C; (CHEMOKINES, C); CC; (CHEMOKINES, CC); and CXC; (CHEMOKINES, CXC); according to variations in a shared cysteine motif.	Chemokine,Chemotactic Cytokine,Chemotactic Cytokines,Cytokines, Chemotactic,Intercrine,Intercrines,Cytokine, Chemotactic
D019108	Tight Junctions	Cell-cell junctions that seal adjacent epithelial cells together, preventing the passage of most dissolved molecules from one side of the epithelial sheet to the other. (Alberts et al., Molecular Biology of the Cell, 2nd ed, p22)	Occluding Junctions,Zonula Occludens,Junction, Occluding,Junction, Tight,Junctions, Occluding,Junctions, Tight,Occluden, Zonula,Occludens, Zonula,Occluding Junction,Tight Junction,Zonula Occluden