دورية أكاديمية
Comparative Characterization of the Sindbis Virus Proteome from Mammalian and Invertebrate Hosts Identifies nsP2 as a Component of the Virion and Sorting Nexin 5 as a Significant Host Factor for Alphavirus Replication.
| العنوان: | Comparative Characterization of the Sindbis Virus Proteome from Mammalian and Invertebrate Hosts Identifies nsP2 as a Component of the Virion and Sorting Nexin 5 as a Significant Host Factor for Alphavirus Replication. |
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| المؤلفون: | Schuchman R; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA., Kilianski A; U.S. Army Edgewood Chemical Biological Center, Aberdeen Proving Ground, Maryland, USA., Piper A; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA., Vancini R; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA., Ribeiro JMC; National Institute of Allergy and Infectious Diseases, Laboratory of Malaria and Vector Research, Rockville, Maryland, USA., Sprague TR; U.S. Army Medical Research Institute of Infectious Diseases, Fort Detrick, Maryland, USA., Nasar F; U.S. Army Medical Research Institute of Infectious Diseases, Fort Detrick, Maryland, USA., Boyd G; Excet, Inc., Springfield, Virginia, USA., Hernandez R; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA Raquel_Hernandez@NCSU.edu trevor.g.glaros.civ@mail.mil., Glaros T; U.S. Army Edgewood Chemical Biological Center, Aberdeen Proving Ground, Maryland, USA Raquel_Hernandez@NCSU.edu trevor.g.glaros.civ@mail.mil. |
| المصدر: | Journal of virology [J Virol] 2018 Jun 29; Vol. 92 (14). Date of Electronic Publication: 2018 Jun 29 (Print Publication: 2018). |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0113724 Publication Model: Electronic-Print Cited Medium: Internet ISSN: 1098-5514 (Electronic) Linking ISSN: 0022538X NLM ISO Abbreviation: J Virol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington Dc : American Society For Microbiology Original Publication: Baltimore, American Society for Microbiology. |
| مواضيع طبية MeSH: | Virion*, Alphavirus Infections/*metabolism , Culicidae/*metabolism , Cysteine Endopeptidases/*metabolism , Proteome/*metabolism , Sindbis Virus/*physiology , Sorting Nexins/*metabolism, Alphavirus Infections/virology ; Amino Acid Sequence ; Animals ; Cricetinae ; Culicidae/virology ; HEK293 Cells ; Humans ; Sequence Homology ; Virus Replication |
| مستخلص: | Recent advances in mass spectrometry methods and instrumentation now allow for more accurate identification of proteins in low abundance. This technology was applied to Sindbis virus, the prototypical alphavirus, to investigate the viral proteome. To determine if host proteins are specifically packaged into alphavirus virions, Sindbis virus (SINV) was grown in multiple host cells representing vertebrate and mosquito hosts, and total protein content of purified virions was determined. This analysis identified host factors not previously associated with alphavirus entry, replication, or egress. One host protein, sorting nexin 5 (SNX5), was shown to be critical for the replication of three different alphaviruses, Sindbis, Mayaro, and Chikungunya viruses. The most significant finding was that in addition to the host proteins, SINV nonstructural protein 2 (nsP2) was detected within virions grown in all host cells examined. The protein and RNA-interacting capabilities of nsP2 coupled with its presence in the virion support a role for nsP2 during packaging and/or entry of progeny virus. This function has not been identified for this protein. Taken together, this strategy identified at least one host factor integrally involved in alphavirus replication. Identification of other host proteins provides insight into alphavirus-host interactions during viral replication in both vertebrate and invertebrate hosts. This method of virus proteome analysis may also be useful for the identification of protein candidates for host-based therapeutics. IMPORTANCE Pathogenic alphaviruses, such as Chikungunya and Mayaro viruses, continue to plague public health in developing and developed countries alike. Alphaviruses belong to a group of viruses vectored in nature by hematophagous (blood-feeding) insects and are termed arboviruses (arthropod-borne viruses). This group of viruses contains many human pathogens, such as dengue fever, West Nile, and Yellow fever viruses. With few exceptions, there are no vaccines or prophylactics for these agents, leaving one-third of the world population at risk of infection. Identifying effective antivirals has been a long-term goal for combating these diseases not only because of the lack of vaccines but also because they are effective during an ongoing epidemic. Mass spectrometry-based analysis of the Sindbis virus proteome can be effective in identifying host genes involved in virus replication and novel functions for virus proteins. Identification of these factors is invaluable for the prophylaxis of this group of viruses. (Copyright © 2018 Schuchman et al.) |
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| فهرسة مساهمة: | Keywords: Sindbis virus; alphavirus; mass spectrometry; viral proteomics |
| المشرفين على المادة: | 0 (Proteome) 0 (SNX5 protein, human) 0 (Sorting Nexins) EC 3.4.22.- (Cysteine Endopeptidases) EC 3.4.22.- (nsP2 proteinase) |
| تواريخ الأحداث: | Date Created: 20180511 Date Completed: 20180724 Latest Revision: 20190320 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC6026752 |
| DOI: | 10.1128/JVI.00694-18 |
| PMID: | 29743363 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1098-5514 |
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| DOI: | 10.1128/JVI.00694-18 |