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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.4
- 수록면
- 286 - 291 (6page)
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초록· 키워드
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Epstein-Barr virus (EBV) is the prototypical ?-herpesvirus and an obligate human pathogen that infects mainly epithelial cells and B cells, which can result in ma-lignancies. EBV infects these target cells by fusing with the viral and cellular lipid bilayer membranes using multiple viral factors and host receptor(s) thus exhibiting a unique complexity in its entry machinery. To enter epithelial cells, EBV requires minimally the conserved core fusion machinery comprised of the glycoproteins gH/gL acting as the receptor-binding complex and gB as the fusogen. EBV can enter B cells using gp42, which binds tightly to gH/gL and interacts with host HLA class II, activating fusion. Previously, we published the individual crystal structures of EBV entry factors, such as gH/gL and gp42, the EBV/host receptor complex, gp42/HLA-DR1, and the fusion protein EBV gB in a postfusion conformation, which allowed us to identify structural determinants and regions critical for receptor-binding and membrane fusion. Recently, we reported different low resolution models of the EBV B cell entry triggering complex (gHgL/gp42/HLA class II) in “open” and “closed” states based on negative-stain single particle electron microscopy, which provide further mechanistic insights. This review summarizes the current knowledge of these key players in EBV entry and how their structures impact receptor-binding and the triggering of gB-mediated fusion.
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참고문헌 (66)
참고문헌 신청
Adler, B. / 2015 / A viral pilot for HCMV navigation? / Viruses 7:3857~3862
Atanasiu, D. / 2010 / Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion / J. Virol 84:3825~3834
Backovic, M. / 2007 / Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity / J. Virol 81:9596~9600
Backovic, M. / 2007 / Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins / Virology 368:102~113
Backovic, M. / 2009 / Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B / Proc. Natl. Acad. Sci. USA 106:2880~2885
Atanasiu, D. / 2010 / Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion / J. Virol 84:3825~3834
Backovic, M. / 2007 / Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity / J. Virol 81:9596~9600
Backovic, M. / 2007 / Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins / Virology 368:102~113
Backovic, M. / 2009 / Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B / Proc. Natl. Acad. Sci. USA 106:2880~2885
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