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THY-1 Cell Surface Antigen (CD90) Has an Important Role in the Initial Stage of Human Cytomegalovirus Infection
Human cytomegalovirus (HCMV) is an important human pathogen that infects about half the US population and is a major cause of birth defects and morbidity in transplant recipients. Despite extensive research, much is still unknown regarding how the virus enters cells. We identified THY-1, a protein on the surface of many different cell types susceptible to CMV infection, as having an important role for facilitating virus infection. We found that antibody to THY-1 or soluble THY-1 protein blocked HCMV infection in multiple cell types, suggesting that THY-1 might serve as a potential therapeutic target to reduce infection. Expression of exogenous THY-1 increased susceptibility of cells to HCMV infection. We showed that THY-1 has an important role in a host signaling pathway that is initiated when HCMV infects cells. Furthermore, we found that THY-1 interacted with HCMV glycoproteins that initiate entry of virus into the cell. THY-1 is known to interact with several host cell proteins important for infection and is expressed on numerous types of cells that can be infected by HCMV. Thus, we have identified THY-1 as a molecule that has an important role in the initial stage of HCMV infection.
Vyšlo v časopise: THY-1 Cell Surface Antigen (CD90) Has an Important Role in the Initial Stage of Human Cytomegalovirus Infection. PLoS Pathog 11(7): e32767. doi:10.1371/journal.ppat.1004999
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004999Souhrn
Human cytomegalovirus (HCMV) is an important human pathogen that infects about half the US population and is a major cause of birth defects and morbidity in transplant recipients. Despite extensive research, much is still unknown regarding how the virus enters cells. We identified THY-1, a protein on the surface of many different cell types susceptible to CMV infection, as having an important role for facilitating virus infection. We found that antibody to THY-1 or soluble THY-1 protein blocked HCMV infection in multiple cell types, suggesting that THY-1 might serve as a potential therapeutic target to reduce infection. Expression of exogenous THY-1 increased susceptibility of cells to HCMV infection. We showed that THY-1 has an important role in a host signaling pathway that is initiated when HCMV infects cells. Furthermore, we found that THY-1 interacted with HCMV glycoproteins that initiate entry of virus into the cell. THY-1 is known to interact with several host cell proteins important for infection and is expressed on numerous types of cells that can be infected by HCMV. Thus, we have identified THY-1 as a molecule that has an important role in the initial stage of HCMV infection.
Zdroje
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- The Lung Microbiome: New Principles for Respiratory Bacteriology in Health and Disease
- Extracellular Virions: The Advance Guard of Poxvirus Infections
- Risks of Antibiotic Exposures Early in Life on the Developing Microbiome
- RNA Virus Reassortment: An Evolutionary Mechanism for Host Jumps and Immune Evasion
- Exploiting Fungal Virulence-Regulating Transcription Factors As Novel Antifungal Drug Targets
- N-acetylglucosamine Regulates Virulence Properties in Microbial Pathogens
- Periodontal Diseases: Bug Induced, Host Promoted
- Mechanisms of Host Behavioral Change in Rodent Association
- The Endosymbiotic Bacterium Selectively Kills Male Hosts by Targeting the Masculinizing Gene
- HIV Reactivation from Latency after Treatment Interruption Occurs on Average Every 5-8 Days—Implications for HIV Remission
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- Suppression of Long-Lived Humoral Immunity Following Infection
- The Role of VP1 Amino Acid Residue 145 of Enterovirus 71 in Viral Fitness and Pathogenesis in a Cynomolgus Monkey Model
- Utilizing Chemical Genomics to Identify Cytochrome as a Novel Drug Target for Chagas Disease
- The Emerging Role for RNA Polymerase II in Regulating Virulence Gene Expression in Malaria Parasites
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- Characterization of a Prefusion-Specific Antibody That Recognizes a Quaternary, Cleavage-Dependent Epitope on the RSV Fusion Glycoprotein
- The Serine Protease EspC from Enteropathogenic Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System
- Existing Infection Facilitates Establishment and Density of Malaria Parasites in Their Mosquito Vector
- Evaluating Human T-Cell Therapy of Cytomegalovirus Organ Disease in HLA-Transgenic Mice
- Neuronal Interferon Signaling Is Required for Protection against Herpes Simplex Virus Replication and Pathogenesis
- Epstein-Barr Virus Proteins EBNA3A and EBNA3C Together Induce Expression of the Oncogenic MicroRNA Cluster miR-221/miR-222 and Ablate Expression of Its Target p57
- Colonization of the Mouse Gastrointestinal Tract Is Modulated by Wall Teichoic Acid, Capsule, and Surface Proteins
- Virulence of Group A Streptococci Is Enhanced by Human Complement Inhibitors
- Identification of Caspase Cleavage Sites in KSHV Latency-Associated Nuclear Antigen and Their Effects on Caspase-Related Host Defense Responses
- Calprotectin Increases the Activity of the SaeRS Two Component System and Murine Mortality during Infections
- Type VI Secretion System Transports Zn to Combat Multiple Stresses and Host Immunity
- Lv4 Is a Capsid-Specific Antiviral Activity in Human Blood Cells That Restricts Viruses of the SIV/SIV/HIV-2 Lineage Prior to Integration
- Phenylbutyrate Is Bacteriostatic against and Regulates the Macrophage Response to Infection, Synergistically with 25-Hydroxy-Vitamin D₃
- An Internally Translated MAVS Variant Exposes Its Amino-terminal TRAF-Binding Motifs to Deregulate Interferon Induction
- PLOS Pathogens
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Najčítanejšie v tomto čísle- RNA Virus Reassortment: An Evolutionary Mechanism for Host Jumps and Immune Evasion
- Activation of TLR2 and TLR6 by Dengue NS1 Protein and Its Implications in the Immunopathogenesis of Dengue Virus Infection
- N-acetylglucosamine Regulates Virulence Properties in Microbial Pathogens
- Characterization of a Prefusion-Specific Antibody That Recognizes a Quaternary, Cleavage-Dependent Epitope on the RSV Fusion Glycoprotein
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