Journal article
Reevaluation of the Requirement for TIP47 in Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Incorporation
Journal of virology, v 87(6), pp 3561-3570
Mar 2013
PMID: 23325685
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Incorporation of the human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins into assembling particles is crucial for virion infectivity. Genetic and biochemical data indicate that the matrix (MA) domain of Gag and the cytoplasmic tail of the transmembrane glycoprotein gp41 play an important role in coordinating Env incorporation; however, the molecular mechanism and possible role of host factors in this process remain to be defined. Recent studies suggested that Env incorporation is mediated by interactions between matrix and tail-interacting protein of 47 kDa (TIP47; also known as perilipin-3 and mannose-6-phosphate receptor-binding protein 1), a member of the perilipin, adipophilin, TIP47 (PAT) family of proteins implicated in protein sorting and lipid droplet biogenesis. We have confirmed by nuclear magnetic resonance spectroscopy titration experiments and surface plasmon resonance that MA binds TIP47. We also reevaluated the role of TIP47 in HIV-1 Env incorporation in HeLa cells and in the Jurkat T-cell line. In HeLa cells, TIP47 overexpression or RNA interference (RNAi)-mediated depletion had no significant effect on HIV-1 Env incorporation, virus release, or particle infectivity. Similarly, depletion of TIP47 in Jurkat cells did not impair HIV-1 Env incorporation, virus release, infectivity, or replication. Our results thus do not support a role for TIP47 in HIV-1 Env incorporation or virion infectivity.
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Details
- Title
- Reevaluation of the Requirement for TIP47 in Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Incorporation
- Creators
- Mary Ann Checkley - Virus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USABenjamin G Luttge - Virus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USAPeter Y Mercredi - Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USASampson K Kyere - Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USAJustin Donlan - Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USATsutomu Murakami - AIDS Research Center, National Institute of Infectious Diseases, Shinjuku, Tokyo, JapanMichael F Summers - Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USASimon Cocklin - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USAEric O Freed - Virus-Cell Interaction Section, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USA
- Publication Details
- Journal of virology, v 87(6), pp 3561-3570
- Publisher
- American Society for Microbiology; 1752 N St., N.W., Washington, DC
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000315348500052
- Scopus ID
- 2-s2.0-84874747909
- Other Identifier
- 991014878001604721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Virology