TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
Identifieur interne : 002645 ( Ncbi/Merge ); précédent : 002644; suivant : 002646TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
Auteurs : Stephanie Jemielity [États-Unis] ; Jinyize J. Wang ; Ying Kai Chan ; Asim A. Ahmed ; Wenhui Li ; Sheena Monahan ; Xia Bu ; Michael Farzan ; Gordon J. Freeman ; Dale T. Umetsu ; Rosemarie H. Dekruyff ; Hyeryun ChoeSource :
- PLoS pathogens [ 1553-7374 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Antiviraux (pharmacologie), Capside, Chiens, Facteurs d'échange de nucléotides guanyliques (métabolisme), Humains, Interactions hôte-pathogène, Lignée cellulaire, Macrophages (métabolisme), Macrophages (virologie), Maladies virales (métabolisme), Maladies virales (virologie), Phosphatidylsérine (métabolisme), Protéines de l'enveloppe virale, Protéines proto-oncogènes (métabolisme), Pénétration virale, Rho guanine nucleotide exchange factors, Récepteurs viraux (métabolisme), Souris, Virion (métabolisme), Virus (pathogénicité).
- MESH :
- métabolisme : Facteurs d'échange de nucléotides guanyliques, Macrophages, Maladies virales, Phosphatidylsérine, Protéines proto-oncogènes, Récepteurs viraux, Virion.
- pathogénicité : Virus.
- pharmacologie : Antiviraux.
- virologie : Macrophages, Maladies virales.
- Animaux, Capside, Chiens, Humains, Interactions hôte-pathogène, Lignée cellulaire, Protéines de l'enveloppe virale, Pénétration virale, Rho guanine nucleotide exchange factors, Souris.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (pharmacology), Capsid, Cell Line, Dogs, Guanine Nucleotide Exchange Factors (metabolism), Host-Pathogen Interactions, Humans, Macrophages (metabolism), Macrophages (virology), Mice, Phosphatidylserines (metabolism), Proto-Oncogene Proteins (metabolism), Receptors, Virus (metabolism), Rho Guanine Nucleotide Exchange Factors, Viral Envelope Proteins, Virion (metabolism), Virus Diseases (metabolism), Virus Diseases (virology), Virus Internalization, Viruses (pathogenicity).
- MESH :
- chemical , metabolism : Guanine Nucleotide Exchange Factors, Phosphatidylserines, Proto-Oncogene Proteins, Receptors, Virus.
- chemical , pharmacology : Antiviral Agents.
- metabolism : Macrophages, Virion, Virus Diseases.
- pathogenicity : Viruses.
- virology : Macrophages, Virus Diseases.
- Animals, Capsid, Cell Line, Dogs, Host-Pathogen Interactions, Humans, Mice, Rho Guanine Nucleotide Exchange Factors, Viral Envelope Proteins, Virus Internalization.
Abstract
Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4) specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a cellular receptor for hepatitis A virus and Ebola virus and as an entry factor for dengue virus. Here we show that TIM1 promotes infection of retroviruses and virus-like particles (VLPs) pseudotyped with a range of viral entry proteins, in particular those from the filovirus, flavivirus, New World arenavirus and alphavirus families. TIM1 also robustly enhanced the infection of replication-competent viruses from the same families, including dengue, Tacaribe, Sindbis and Ross River viruses. All interactions between TIM1 and pseudoviruses or VLPs were PS-mediated, as demonstrated with liposome blocking and TIM1 mutagenesis experiments. In addition, other PS-binding proteins, such as Axl and TIM4, promoted infection similarly to TIM1. Finally, the blocking of PS receptors on macrophages inhibited the entry of Ebola VLPs, suggesting that PS receptors can contribute to infection in physiologically relevant cells. Notably, infection mediated by the entry proteins of Lassa fever virus, influenza A virus and SARS coronavirus was largely unaffected by TIM1 expression. Taken together our data show that TIM1 and related PS-binding proteins promote infection of diverse families of enveloped viruses, and may therefore be useful targets for broad-spectrum antiviral therapies.
DOI: 10.1371/journal.ppat.1003232
PubMed: 23555248
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001227
- to stream PubMed, to step Curation: 001227
- to stream PubMed, to step Checkpoint: 001091
Links to Exploration step
pubmed:23555248Le document en format XML
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<front><div type="abstract" xml:lang="en">Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4) specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a cellular receptor for hepatitis A virus and Ebola virus and as an entry factor for dengue virus. Here we show that TIM1 promotes infection of retroviruses and virus-like particles (VLPs) pseudotyped with a range of viral entry proteins, in particular those from the filovirus, flavivirus, New World arenavirus and alphavirus families. TIM1 also robustly enhanced the infection of replication-competent viruses from the same families, including dengue, Tacaribe, Sindbis and Ross River viruses. All interactions between TIM1 and pseudoviruses or VLPs were PS-mediated, as demonstrated with liposome blocking and TIM1 mutagenesis experiments. In addition, other PS-binding proteins, such as Axl and TIM4, promoted infection similarly to TIM1. Finally, the blocking of PS receptors on macrophages inhibited the entry of Ebola VLPs, suggesting that PS receptors can contribute to infection in physiologically relevant cells. Notably, infection mediated by the entry proteins of Lassa fever virus, influenza A virus and SARS coronavirus was largely unaffected by TIM1 expression. Taken together our data show that TIM1 and related PS-binding proteins promote infection of diverse families of enveloped viruses, and may therefore be useful targets for broad-spectrum antiviral therapies.</div>
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<Abstract><AbstractText>Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4) specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a cellular receptor for hepatitis A virus and Ebola virus and as an entry factor for dengue virus. Here we show that TIM1 promotes infection of retroviruses and virus-like particles (VLPs) pseudotyped with a range of viral entry proteins, in particular those from the filovirus, flavivirus, New World arenavirus and alphavirus families. TIM1 also robustly enhanced the infection of replication-competent viruses from the same families, including dengue, Tacaribe, Sindbis and Ross River viruses. All interactions between TIM1 and pseudoviruses or VLPs were PS-mediated, as demonstrated with liposome blocking and TIM1 mutagenesis experiments. In addition, other PS-binding proteins, such as Axl and TIM4, promoted infection similarly to TIM1. Finally, the blocking of PS receptors on macrophages inhibited the entry of Ebola VLPs, suggesting that PS receptors can contribute to infection in physiologically relevant cells. Notably, infection mediated by the entry proteins of Lassa fever virus, influenza A virus and SARS coronavirus was largely unaffected by TIM1 expression. Taken together our data show that TIM1 and related PS-binding proteins promote infection of diverse families of enveloped viruses, and may therefore be useful targets for broad-spectrum antiviral therapies.</AbstractText>
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