Abstract

As compared to the previous precipitin inhibition tests differences were found in thereactivities of monoclonal antibodies (MAbs), a-4 and a-84 with Streptococcus cricetus (serotype a) in an enzyme immunoassay using whole cells, purified cell wall antigen and haptenic sugars coated onto microtitre wells. Investigation into the differences led to the finding that the purified antigen from S. cricetus cells consisted mainly of three forms with different molecular weights and sugar contents. MAb a-4 reacted with a high molecular weight form (AgI, molecular weight of 46 000) and low molecular weight forms (AgII and AgIII, molecular weights of 9 800 and 20 000, respectively) whereas MAb a-84 reacted only with the high-molecular form. Gas chromatographic analysis revealed that all antigens contained rhamnose, galactose and glucose but in different ratios of the sugars. Although the binding site of AgII/AgIII with MAb a-4 seemed to be slightly different from that of AgI with MAb a-84, the predominant immunodeterminant of the antigens was considered to be the same. On the basis of these results, the chemical structures of the antigenic determinants are suggested. The nature of the antigen-antibody reactions is discussed.

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