4.8 Review

Role of Hepatitis C Virus Envelope Glycoprotein E1 in Virus Entry and Assembly

Journal

FRONTIERS IN IMMUNOLOGY
Volume 9, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fimmu.2018.01411

Keywords

hepatitis C virus; envelope protein; E1; virus entry; virus assembly; fusion

Categories

Funding

  1. National Natural Science Foundation of China [31670172, 31770189]
  2. Chinese National 973 Program [2015CB554300]
  3. Chinese Academy of Sciences (100 talent program) [153211KYSB20160001]
  4. Ministry of Science and Technology international grant [2016YFE133500]
  5. Shanghai municipality 1000 Talent program

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Hepatitis C virus (HCV) glycoproteins E1 and E2 form a heterodimer to constitute viral envelope proteins, which play an essential role in virus entry. E1 does not directly interact with host receptors, and its functions in viral entry are exerted mostly through its interaction with E2 that directly binds the receptors. HCV enters the host cell via receptor-mediated endocytosis during which the fusion of viral and host endosomal membranes occurs to release viral genome to cytoplasm. A putative fusion peptide in E1 has been proposed to participate in membrane fusion, but its exact role and underlying molecular mechanisms remain to be deciphered. Recently solved crystal structures of the E2 ectodomains and N-terminal of E1 fail to reveal a classical fusion-like structure in HCV envelope glycoproteins. In addition, accumulating evidence suggests that E1 also plays an important role in virus assembly. In this mini-review, we summarize current knowledge on HCV E1 including its structure and biological functions in virus entry, fusion, and assembly, which may provide clues for developing HCV vaccines and more effective antivirals.

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