Open AccessRheumatoid factors react with fab fragments of monoclonal antibodies to herpes simplex virus types 1 and 2 fcγ‐binding proteins
Author(s) -
Tsuchiya Naoyuki,
Malone Christine,
HuttFletcher Lindsey M.,
Williams Ralph C.
Publication year - 1991
Publication title -
arthritis & rheumatism
Language(s) - English
Resource type - Journals
eISSN - 1529-0131
pISSN - 0004-3591
DOI - 10.1002/art.1780340710
Subject(s) - polyclonal antibodies , monoclonal antibody , herpes simplex virus , monoclonal , microbiology and biotechnology , chemistry , virology , rheumatoid factor , antibody , virus , biology , immunology
Human polyclonal IgM rheumatoid factors (RF) were tested in an enzyme‐linked immunosorbent assay with monoclonal antibodies (MAb) (II‐481 and B10/A8) to glycoprotein E (gE), the Fcγ‐binding protein of herpes simplex virus type 1 (HSV‐1), as well as with MAb 88‐S to gE of HSV‐2. Most of the RF reacted with II‐481 and 88‐S. Positive reactions were recorded for RF reacting with whole MAb II‐481 and 88‐S, as well as with their Fab, but not their Fc, fragments. Human monoclonal IgM RF isolated from mixed cryoglobulins showed a similar profile, with reactivity for both whole MAb II‐481 and 88‐S and for their Fab fragments. Reactivity with MAb to gE was observed regardless of the Gm specificity of the polyclonal RF and the crossreactive idiotypes (6B6, 17.109, or G6) of the monoclonal RF. No positive reactions were noted between protein A and Fab fragments of any of the anti‐gE MAb. These findings indicate that many RF may bear the internal image of the Fcγ‐binding regions of 2 different herpesviruses: HSV‐1 and HSV‐2.