Crimean-Congo hemorrhagic fever virus utilizes a clathrin- and early endosome-dependent entry pathway

Virology. 2013 Sep;444(1-2):45-54. doi: 10.1016/j.virol.2013.05.030. Epub 2013 Jun 19.

Abstract

The early events in Crimean-Congo hemorrhagic fever virus (CCHFV) have not been completely characterized. Earlier work indicated that CCHFV likely enters cells by clathrin-mediated endocytosis (CME). Here we provide confirmatory evidence for CME entry by showing that CCHFV infection is inhibited in cells treated with Pitstop 2, a drug that specifically and reversibly interferes with the dynamics of clathrin-coated pits. Additionally, we show that CCHFV infection is inhibited by siRNA depletion of the clathrin pit associated protein AP-2. Following CME entry, we show that CCHFV has a pH-dependent entry step, with virus inactivation occurring at pH 6.0 and below. To more precisely define the endosomal trafficking of CCHFV, we show for the first time that overexpression of the dominant negative forms of Rab5 protein but not Rab7 protein inhibits CCHFV infection. These results indicate that CCHFV likely enters cells through the early endosomal compartment.

Keywords: Bunyavirus; CCHF; Crimean–Congo hemorrhagic fever; Nairovirus; Virus entry.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adaptor Protein Complex 2 / metabolism
  • Clathrin / metabolism*
  • Clathrin-Coated Vesicles / virology*
  • Endocytosis*
  • Hemorrhagic Fever Virus, Crimean-Congo / physiology*
  • Humans
  • Hydrogen-Ion Concentration
  • Virus Internalization*
  • rab GTP-Binding Proteins / metabolism
  • rab5 GTP-Binding Proteins / metabolism
  • rab7 GTP-Binding Proteins

Substances

  • Adaptor Protein Complex 2
  • Clathrin
  • rab7 GTP-Binding Proteins
  • rab7 GTP-binding proteins, human
  • rab GTP-Binding Proteins
  • rab5 GTP-Binding Proteins