Open AccessEbolavirus Glycoprotein GP Masks both Its Own Epitopes and the Presence of Cellular Surface Proteins
Author(s) -
Olivier Reynard,
Malgorzata Borowiak,
Valentina A. Volchkova,
Sébastien Delpeut,
Mathieu Mateo,
Viktor E. Volchkov
Publication year - 2009
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00784-09
Subject(s) - epitope , biology , glycoprotein , ebolavirus , downregulation and upregulation , virology , membrane glycoproteins , antigen , major histocompatibility complex , ebola virus , membrane protein , virus , antigenic variation , plasma protein binding , microbiology and biotechnology , immunology , gene , genetics , membrane
Ebolavirus (EBOV) is the etiological agent of a severe hemorrhagic fever with a high mortality rate. The spike glycoprotein (GP) is believed to be one of the major determinants of virus pathogenicity. In this study, we demonstrated the molecular mechanism responsible for the downregulation of surface markers caused by EBOV GP expression. We showed that expression of mature GP on the plasma membrane results in the masking of cellular surface proteins, including major histocompatibility complex class I. Overexpression of GP also results in the masking of certain antigenic epitopes on GP itself, causing an illusory effect of disappearance from the plasma membrane.