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From the Transplantation and Immunology Division and the Institute of Reconstructive Plastic Surgery, Department of Surgery, New York University Medical Center, New York, New York 10016, and the Hektoen Institute for Medical Research of The Cook County Hospital, Chicago, Illinois 60612
Abstract
A water-soluble, dialyzable glycoprotein extract of group A type 12 nephritogenic streptococcal membranes, which has previously shown transplantation antigen-like activity in mice and induced nephritis in rhesus monkeys and in dogs, has the capacity to protect human lymphocytes from the cytotoxic effects of isospecific HL-A typing antisera. This effect is not a consequence of a serologic reaction between HL-A antibodies and streptococcal extract (TGCM). Rather, it is due to the firm binding of TGCM to the lymphocyte surface, in a manner which resists dissociation by vigorous repeated washings. The protective effects of TGCM against HL-A antisera appear thus far to be limited to lymphocytes, as TGCM failed to protect human fibroblasts obtained from donors of known HL-A genotypes from the cytotoxic effects of such antisera. Immunofluorescence studies indicate that TGCM binding sites occur in diffuse fashion on the lymphocyte surface. In addition, the results of absorption-inhibition tests utilizing lymphocytes from donors of known HL-A phenotypes, speciesspecific anti-human heteroantisera and isospecific HL-A antisera point to a close spatial relationship between HL-A, species-specific, and TGCM binding sites on the surface of the human lymphocyte.
Footnotes
1 This investigation was supported by a grant from The John A. Hartford Foundation, Inc., and supported in part by The Billy Rose Foundation, Inc., The Irwin Strasburger Memorial Medical Foundation, Inc., and United States Public Health Service Grant AM-04459. FTR is an Irma T. Hirschl Career Scientist.
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