[go: up one dir, main page]

Seidel et al., 2021 - Google Patents

A slowly cleaved viral signal peptide acts as a protein-integral immune evasion domain

Seidel et al., 2021

View HTML @Full View
Document ID
6523997169152275564
Author
Seidel E
Dassa L
Kahlon S
Tirosh B
Halenius A
Seidel Malkinson T
Mandelboim O
Publication year
Publication venue
Nature communications

External Links

Snippet

Stress can induce cell surface expression of MHC-like ligands, including MICA, that activate NK cells. Human cytomegalovirus (HCMV) glycoprotein US9 downregulates the activating immune ligand MICA* 008 to avoid NK cell activation, but the underlying mechanism …
Continue reading at www.nature.com (HTML) (other versions)

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/177—Receptors; Cell surface antigens; Cell surface determinants
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C07K14/70503—Immunoglobulin superfamily
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00—Medicinal preparations containing organic active ingredients
    • A61K31/70—Carbohydrates; Sugars; Derivatives thereof
    • A61K31/7088—Compounds having three or more nucleosides or nucleotides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00—Medicinal preparations containing organic active ingredients
    • A61K31/33—Heterocyclic compounds
    • A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine, rifamycins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
    • A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca

Similar Documents

Publication Publication Date Title
Seidel et al. Dynamic co-evolution of host and pathogen: HCMV downregulates the prevalent allele MICA∗ 008 to escape elimination by NK cells
Wang et al. TRIM37, a novel E3 ligase for PEX5-mediated peroxisomal matrix protein import
Vo et al. Activation of NIX-mediated mitophagy by an interferon regulatory factor homologue of human herpesvirus
Baldauf et al. SAMHD1 restricts HIV-1 infection in resting CD4+ T cells
Seidel et al. A slowly cleaved viral signal peptide acts as a protein-integral immune evasion domain
Chen et al. Molecular dissection of 2B4 signaling: implications for signal transduction by SLAM-related receptors
Kueck et al. Serine phosphorylation of HIV-1 Vpu and its binding to tetherin regulates interaction with clathrin adaptors
Bae et al. Trafficking of LAG-3 to the surface on activated T cells via its cytoplasmic domain and protein kinase C signaling
Magadán et al. Transmembrane domain determinants of CD4 Downregulation by HIV-1 Vpu
Swingler et al. Apoptotic killing of HIV-1–infected macrophages is subverted by the viral envelope glycoprotein
Fukui et al. Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic cells toward DNA-but against RNA-sensing
Hsu et al. Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141
Lee et al. The role of receptor internalization in CD95 signaling
Pao et al. Syk, but not Lyn, recruitment to B cell antigen receptor and activation following stimulation of CD45-B cells
Döring et al. R ab33 B and its autophagic A tg5/12/16 L 1 effector assist in hepatitis B virus naked capsid formation and release
Voskoboinik et al. Addressing the mysteries of perforin function
Choi et al. Peroxisomes support human herpesvirus 8 latency by stabilizing the viral oncogenic protein vFLIP via the MAVS-TRAF complex
Rapiteanu et al. A genetic screen identifies a critical role for the WDR81‐WDR91 complex in the trafficking and degradation of tetherin
Foster et al. Inhibiting the ins and outs of HIV replication: cell-intrinsic antiretroviral restrictions at the plasma membrane
Stoneham et al. A conserved acidic-cluster motif in SERINC5 confers partial resistance to antagonism by HIV-1 Nef
Bouchet et al. Single-domain antibody-SH3 fusions for efficient neutralization of HIV-1 Nef functions
WO2019108589A1 (en) Compositions and methods for treating cancer
Ceriani et al. The deubiquitinating enzyme UBPy/USP8 interacts with TrkA and inhibits neuronal differentiation in PC12 cells
Seidel et al. The human cytomegalovirus protein UL147A downregulates the most prevalent MICA allele: MICA* 008, to evade NK cell-mediated killing
Mun et al. Macrophage migration inhibitory factor down‐regulates the RANKL–RANK signaling pathway by activating Lyn tyrosine kinase in mouse models