Previous work has demonstrated that B cells in the lymphocytic choriomeningitis virus (LCM) carrier mouse do not produce anti-LCM antibody. Studies were undertaken to determine the binding specificity of immunoglobulin (Ig) eluted from kidneys of LCM-infected SWR/J mice. Kidneys from neonatally infected LCM carrier mice (5 to 7 months of age) were homogenized in 0.05 M EDTA PBS (pH 7.4), centrifuged at 12,000 × G for 10 min at 4°C and the sediment was washed three times. The sediment was eluted with citrate buffer (pH 3.2) for 90 min at 37°C, centrifuged as before, neutralized, and concentrated by vacuum dialysis. These elution conditions destroyed the binding capacity of LCM antigen in infected tissues and in commercial complement fixation LCM antigen solutions. The amount of Ig eluted was 22 to 24 µg/kidney from LCM-infected mice but less than 1 µg/kidney from uninfected mice. Eluted Ig did not bind to LCM-infected tissue although SWR/J anti-LCM antiserum subjected to the eluting conditions retained its LCM antigen-binding ability. NZB × NZW F1 hybrid kidneys eluted as above yielded similar amounts of Ig that had antinuclear binding ability. Eluted Ig did not induce complement fixation when added to LCM antigen although SWR/J anti-LCM antiserum subjected to elution conditions retained its LCM antigen complement-fixing properties. These observations indicate that Ig deposited in glomeruli of LCM carrier mice is not specific for LCM antigens and favors the position that the LCM carrier mouse is tolerant to LCM virus.
This work was supported by National Institutes of Health Grants AM-09976, AM-05248, and Training Grant AM-07126.