Open AccessEvidence for the role of glycoprotein G of respiratory syncytial virus in binding of Neisseria meningitidis to HEp‐2 cells
Author(s) -
Raza Muhammad W.,
Caroline Blackwell C.,
Ogilvie Marie M.,
Saadi Abdulrahman T.,
Stewart John,
Elton Robert A.,
Weir Donald M.
Publication year - 1994
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1994.tb00007.x
Subject(s) - monoclonal antibody , glycoprotein , biology , virus , virology , antibody , immunofluorescence , flow cytometry , neisseria meningitidis , microbiology and biotechnology , mononegavirales , paramyxoviridae , bacteria , viral disease , immunology , genetics
Viral glycoproteins G and F are expressed on the surface of cells infected with respiratory syncytial virus (RSV). We investigated the role of these proteins in the previously reported enhanced binding of Neisseria meningitidis to RSV‐infected HEp‐2 cells. Virus particles attached to bacteria were detected by immunofluorescence with flow cytometry. Binding of FITC‐labelled bacteria to RSV‐infected cells was significantly inhibited by monoclonal antibody against glycoprotein G. Unlabelled bacteria interfered with binding of the anti‐G monoclonal antibody to these cells. These interactions were not found with a monoclonal antibody against glycoprotein F. We propose that glycoprotein G of RSV expressed on the surface of infected cells might act as an additional receptor for meningococci.